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Conserved domains on  [gi|1338686448|ref|NP_001347389|]
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START domain-containing protein 10 isoform 1 [Mus musculus]

Protein Classification

START domain-containing protein( domain architecture ID 10172287)

START domain-containing protein, such as STARD10 that may play metabolic roles in sperm maturation or fertilization

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 92-314 9.81e-145

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).


:

Pssm-ID: 176880  Cd Length: 222  Bit Score: 408.57  E-value: 9.81e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448  92 RESVQVPDDQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSN 171
Cdd:cd08871     1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPE-NSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 172 VIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGP 251
Cdd:cd08871    80 MIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGP 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1338686448 252 KSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKYPEWKQKHQPHFKPWLHPEQ 314
Cdd:cd08871   160 KGCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKNNPEFKPWLYPEQ 222
 
Name Accession Description Interval E-value
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 92-314 9.81e-145

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).


Pssm-ID: 176880  Cd Length: 222  Bit Score: 408.57  E-value: 9.81e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448  92 RESVQVPDDQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSN 171
Cdd:cd08871     1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPE-NSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 172 VIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGP 251
Cdd:cd08871    80 MIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGP 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1338686448 252 KSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKYPEWKQKHQPHFKPWLHPEQ 314
Cdd:cd08871   160 KGCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKNNPEFKPWLYPEQ 222
START pfam01852
START domain;
149-297 4.64e-24

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 97.86  E-value: 4.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 149 DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYS----WrcPKPLKNRDVITLRSWLPMGAD-YIIMNYSV 223
Cdd:pfam01852  53 MVAALLVAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVaalvA--PSPLSPRDFVFLRYWRRLGGGvYVIVDRSV 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1338686448 224 KHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKYPE 297
Cdd:pfam01852 131 THPQFPPSSGYVRAERLPSGYLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCE 204
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 110-299 9.32e-22

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 91.72  E-value: 9.32e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448  110 CEAEVGWNLTYSKAGVSVWVQAVEMDRTLHKIkcrMECC----DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNA 185
Cdd:smart00234  14 AASEEGWVLSSENENGDEVRSIFSPGRKPGEA---FRLVgvvpMVCADLVEELMDDLEYRPEWDKNVAKAETLEVIDNGT 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448  186 DVGYYSWRCP-KPLKNRDVITLRSWLPMGAD-YIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVD 263
Cdd:smart00234  91 VIYHYVSKFAaGPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGPSKVTWVSHAD 170

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1338686448  264 PKGSLPKWVVNkSSQFLAPKAMKKMYKACIKYPEWK 299
Cdd:smart00234 171 LKGWLPHWLVR-SLIKSGLAEFAKTLVATLQKHCAK 205
 
Name Accession Description Interval E-value
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 92-314 9.81e-145

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).


Pssm-ID: 176880  Cd Length: 222  Bit Score: 408.57  E-value: 9.81e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448  92 RESVQVPDDQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSN 171
Cdd:cd08871     1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPE-NSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 172 VIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGP 251
Cdd:cd08871    80 MIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGP 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1338686448 252 KSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKYPEWKQKHQPHFKPWLHPEQ 314
Cdd:cd08871   160 KGCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKNNPEFKPWLYPEQ 222
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 100-292 1.63e-52

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 172.52  E-value: 1.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 100 DQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVIETFDIA 179
Cdd:cd00177     1 EEAIEELLELLEEPEGWKLVKEKDGVKIYTKPYE-DSGLKLLKAEGVI-PASPEQVFELLMDIDLRKKWDKNFEEFEVIE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 180 RLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGAD-YIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITY 258
Cdd:cd00177    79 EIDEHTDIIYYKTKPPWPVSPRDFVYLRRRRKLDDGtYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTY 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1338686448 259 LAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKAC 292
Cdd:cd00177   159 VLQVDPKGSIPKSLVNSAAKKQLASFLKDLRKAK 192
START pfam01852
START domain;
149-297 4.64e-24

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 97.86  E-value: 4.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 149 DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYS----WrcPKPLKNRDVITLRSWLPMGAD-YIIMNYSV 223
Cdd:pfam01852  53 MVAALLVAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVaalvA--PSPLSPRDFVFLRYWRRLGGGvYVIVDRSV 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1338686448 224 KHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKYPE 297
Cdd:pfam01852 131 THPQFPPSSGYVRAERLPSGYLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCE 204
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 110-299 9.32e-22

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 91.72  E-value: 9.32e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448  110 CEAEVGWNLTYSKAGVSVWVQAVEMDRTLHKIkcrMECC----DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNA 185
Cdd:smart00234  14 AASEEGWVLSSENENGDEVRSIFSPGRKPGEA---FRLVgvvpMVCADLVEELMDDLEYRPEWDKNVAKAETLEVIDNGT 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448  186 DVGYYSWRCP-KPLKNRDVITLRSWLPMGAD-YIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVD 263
Cdd:smart00234  91 VIYHYVSKFAaGPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGPSKVTWVSHAD 170

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1338686448  264 PKGSLPKWVVNkSSQFLAPKAMKKMYKACIKYPEWK 299
Cdd:smart00234 171 LKGWLPHWLVR-SLIKSGLAEFAKTLVATLQKHCAK 205
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 106-295 2.14e-17

Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD2 is a cytosolic phosphatidycholine (PtdCho) transfer protein, which traffics PtdCho, the most common class of phospholipids in eukaryotes, between membranes. It represents a minimal START domain structure. STARD2 plays roles in hepatic cholesterol metabolism, in the development of atherosclerosis, and may have a mitochondrial function.


Pssm-ID: 176919  Cd Length: 207  Bit Score: 79.84  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 106 FRSECeAEVG--------WNLTYSKAGVSVWvQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFD 177
Cdd:cd08910    10 FREAC-AELQqpaldgaaWELLVESSGISIY-RLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQYVKELYE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 178 iaRLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADY----IIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKS 253
Cdd:cd08910    88 --KECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGrkiwVILARSTSLPQLPEKPGVIRVKQYKQSLAIESDGKKG 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1338686448 254 CVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKY 295
Cdd:cd08910   166 SKVFMYYFDNPGGMIPSWLINWAAKNGVPNFLKDMQKACQNY 207
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 111-295 8.11e-17

Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD7 (also known as gestational trophoblastic tumor 1/GTT1). It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of phosphatidycholine (PtdCho) to mitochondria. STARD7 was shown to be surface active and to interact differentially with phospholipid monolayers, it showed a preference for phosphatidylserine, cholesterol, and phosphatidylglycerol.


Pssm-ID: 176920  Cd Length: 207  Bit Score: 78.10  E-value: 8.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 111 EAEVGWNLTYSKAGVSVWVQAvEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTV-NADVGY 189
Cdd:cd08911    18 QEPDGWEPFIEKKDMLVWRRE-HPGTGLYEYKVYGSFDDVTARDFLNVQLDLEYRKKWDATAVELEVVDEDPEtGSEIIY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 190 YSWRCPKPLKNRDVITLRSWLpmgADY-----IIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSC-----VITYL 259
Cdd:cd08911    97 WEMQWPKPFANRDYVYVRRYI---IDEenkliVIVSKAVQHPSYPESPKKVRVEDYWSYMVIRPHKSFDEpgfefVLTYF 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1338686448 260 AqvDPKGSLPK----WVVNKSsqflAPKAMKKMYKACIKY 295
Cdd:cd08911   174 D--NPGVNIPSyitsWVAMSG----MPDFLERLRNAALKY 207
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 149-286 2.63e-16

Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176877  Cd Length: 208  Bit Score: 76.62  E-value: 2.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 149 DVPAETLYDVL-HDIEYRKKWDSNVIETFDIARLTVNADVGYyswRCPKPLKN-----RDVITLRSWLPMGADYIIMNYS 222
Cdd:cd08868    57 DCPAEFLYNELvLNVESLPSWNPTVLECKIIQVIDDNTDISY---QVAAEAGGglvspRDFVSLRHWGIRENCYLSSGVS 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1338686448 223 VKHPKYPPRKDLVRAVSIQTGYLIQSTG--PKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMK 286
Cdd:cd08868   134 VEHPAMPPTKNYVRGENGPGCWILRPLPnnPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMK 199
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 97-295 7.66e-16

Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD2 (also known as phosphatidylcholine transfer protein/PC-TP), and STARD7 (also known as gestational trophoblastic tumor 1/GTT1). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD2 is a cytosolic phosphatidycholine (PtdCho) transfer protein, which traffics PtdCho, the most common class of phospholipids in eukaryotes, between membranes. It represents a minimal START domain structure. STARD2 plays roles in hepatic cholesterol metabolism, in the development of atherosclerosis, and may also have a mitochondrial function. The gene encoding STARD7 is overexpressed in choriocarcinoma. STARD7 appears to be involved in the intracellular trafficking of PtdCho to mitochondria. STARD7 was shown to be surface active and to interact differentially with phospholipid monolayers. It showed a preference for phosphatidylserine, cholesterol, and phosphatidylglycerol.


Pssm-ID: 176879  Cd Length: 209  Bit Score: 75.49  E-value: 7.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448  97 VPDDQDFRSF---RSECEAEVGWNLTYSKAGVSVWVQA---VEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDS 170
Cdd:cd08870     2 HVSEEDLRDLvqeLQEGAEGQAWQQVMDKSTPDMSYQAwrrKPKGTGLYEYLVRGVFEDCTPELLRDFYWDDEYRKKWDE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 171 NVIETFDIARLTVNA-DVGYYSWRCPKPLKNRD-VITLRSWLPMGADYIIMNYSVKHPKYPPRKDL-VRAVSIQTGYLIQ 247
Cdd:cd08870    82 TVIEHETLEEDEKSGtEIVRWVKKFPFPLSDREyVIARRLWESDDRSYVCVTKGVPYPSVPRSGRKrVDDYESSLVIRAV 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1338686448 248 STGPK--SCVITYLAQvdPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKY 295
Cdd:cd08870   162 KGDGQgsACEVTYFHN--PDGGIPRELAKLAVKRGMPGFLKKLENALRKY 209
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 113-275 2.72e-15

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176885  Cd Length: 195  Bit Score: 73.46  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 113 EVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYSW 192
Cdd:cd08876    16 DGDWQLVKDKDGIKVYTRDVE-GSPLKEFKAVAEV-DASIEAFLALLRDTESYPQWMPNCKESRVLKRTDDNERSVYTVI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 193 RCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPP-RKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKW 271
Cdd:cd08876    94 DLPWPVKDRDMVLRSTTEQDADDGSVTITLEAAPEALPeQKGYVRIKTVEGQWTFTPLGNGKTRVTYQAYADPGGSIPGW 173


                  ....
gi 1338686448 272 VVNK 275
Cdd:cd08876   174 LANA 177
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 106-276 4.00e-15

C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear.


Pssm-ID: 176878  Cd Length: 197  Bit Score: 73.11  E-value: 4.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 106 FRSECEAEVGWNLTYSKAGVSVWVQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDieyRKKWDSNVIETFDIARLTVNA 185
Cdd:cd08869    11 LREARDKSKGWVSVSSSDHVELAFKKVDDGHPLRLWRASTEVEAPPEEVLQRILRE---RHLWDDDLLQWKVVETLDEDT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 186 DVGYYSWRCPKPLKNRDVITLRSW---LPMGADYIIMNySVKHPK-YPPRkdLVRAVSIQTGYLIQSTGPKSCVITYLAQ 261
Cdd:cd08869    88 EVYQYVTNSMAPHPTRDYVVLRTWrtdLPKGACVLVET-SVEHTEpVPLG--GVRAVVLASRYLIEPCGSGKSRVTHICR 164

                         170
                  ....*....|....*
gi 1338686448 262 VDPKGSLPKWvVNKS 276
Cdd:cd08869   165 VDLRGRSPEW-YNKV 178
START_STARD12-like cd08908
C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also ...
 142-286 4.93e-10

C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subgroup also have an N-terminal SAM (sterile alpha motif) domain and a RhoGAP domain, and have a SAM-RhoGAP-START domain organization. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176917  Cd Length: 204  Bit Score: 58.49  E-value: 4.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 142 KCRMECCDVPAETLYDVLHDieyRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSW---LPMGADYII 218
Cdd:cd08908    55 RTTIEVPAAPEEILKRLLKE---QHLWDVDLLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWrtnLPKGACALL 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1338686448 219 MNySVKHPKYPPRKdlVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMK 286
Cdd:cd08908   132 AT-SVDHDRAPVAG--VRVNVLLSRYLIEPCGSGKSKLTYMCRIDLRGHMPEWYTKSFGHLCAAEVVK 196
START_STARD13-like cd08909
C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also ...
 151-271 1.39e-09

C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176918  Cd Length: 205  Bit Score: 57.23  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 151 PAETLYDVLHDieyRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSW---LPMGAdYIIMNYSVKHPK 227
Cdd:cd08909    64 PSVVLNRVLRE---RHLWDEDFLQWKVVETLDKQTEVYQYVLNCMAPHPSRDFVVLRSWrtdLPKGA-CSLVSVSVEHEE 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1338686448 228 YPPRKDlVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKW 271
Cdd:cd08909   140 APLLGG-VRAVVLDSQYLIEPCGSGKSRLTHICRVDLKGHSPEW 182
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 112-297 3.70e-09

Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114) and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD15/ACOT12 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. Human STARD15/ACOT12 may have roles in cholesterol metabolism and in beta-oxidation.


Pssm-ID: 176922  Cd Length: 236  Bit Score: 56.45  E-value: 3.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 112 AEVGWNLTysKAGVSVWVQAVEmDRTLHKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVI--ETFDiarlTVNADVGY 189
Cdd:cd08914    54 AKSGWEVT--STVEKIKIYTLE-EHDVLSVWVEKHV-KRPAHLAYRLLSDFTKRPLWDPHFLscEVID----WVSEDDQI 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 190 YSWRCP--KPLKNRDVITL---RSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDP 264
Cdd:cd08914   126 YHITCPivNNDKPKDLVVLvsrRKPLKDGNTYVVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISA 205

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1338686448 265 kGSLPKWVVNKSSQflaPKAMKKMYKACIKYPE 297
Cdd:cd08914   206 -SILPYFAGNLGGW---SKSIEETAASCIQFLE 234
START_2 cd08877
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 107-295 4.27e-09

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176886  Cd Length: 215  Bit Score: 56.15  E-value: 4.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 107 RSECEAEVGWNLTYSKAGVSVWVQaVEMDRTLHKikCRMECC-DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNA 185
Cdd:cd08877    15 LKDLDESDGWTLQKESEGIRVYYK-FEPDGSLLS--LRMEGEiDGPLFNLLALLNEVELYKTWVPFCIRSKKVKQLGRAD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 186 DVGYYSWRCPKPLKNRDVItLRSWlpmGADYI-------IMNYSVKHPKYPPRKDL----------VRAVSIQTGYLIQS 248
Cdd:cd08877    92 KVCYLRVDLPWPLSNREAV-FRGF---GVDRLeengqivILLKSIDDDPEFLKLTDldipstsakgVRRIIKYYGFVITP 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1338686448 249 TGPKSCVITYLAQVDPKGSL-PKWVVNkssqFLAPKAMKKMYKACIKY 295
Cdd:cd08877   168 ISPTKCYLRFVANVDPKMSLvPKSLLN----FVARKFAGLLFEKIQKA 211
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 151-271 1.65e-07

C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176916  Cd Length: 205  Bit Score: 51.08  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 151 PAETLYDVLHDieyRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSW---LPMGAdYIIMNYSVKHPK 227
Cdd:cd08907    64 PSVVLQRVLRE---RHLWDEDLLHSQVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWrsdLPRGG-CLLVSQSVDHDN 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1338686448 228 YPPRKDlVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKW 271
Cdd:cd08907   140 PQLEAG-VRAVLLTSQYLIEPCGMGRSRLTHICRADLRGRSPDW 182
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 140-276 7.83e-07

Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD3 (also known as metastatic lymph node 64/MLN64) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD3 has a high affinity for cholesterol. It may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176915  Cd Length: 209  Bit Score: 49.09  E-value: 7.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 140 KIKCRMECcdvPAETLY-DVLHDIEYRKKWDSNVIETFDIARLTVNADVGY--YSWRCPKPLKNRDVITLRSWLPMGADY 216
Cdd:cd08906    52 ILKAFMQC---PAELVYqEVILQPEKMVLWNKTVSACQVLQRVDDNTLVSYdvAAGAAGGVVSPRDFVNVRRIERRRDRY 128

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1338686448 217 IIMNYSVKHPKYPPRKDLVRAVSIQTGYLI--QSTGPKSCVITYLAQVDPKGSLPKWVVNKS 276
Cdd:cd08906   129 VSAGISTTHSHKPPLSKYVRGENGPGGFVVlkSASNPSVCTFIWILNTDLKGRLPRYLIHQS 190
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 150-295 1.56e-06

Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974), STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 and STARD15/ACOT12 are type II acetyl-CoA thioesterases; they catalyze the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, STARD14 and STARD15 each have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice. Human STARD15 may have roles in cholesterol metabolism and in beta-oxidation.


Pssm-ID: 176882  Cd Length: 235  Bit Score: 48.75  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 150 VPAETLYDVLHDIEYRKKWDSNVIETFDIARltVNADVGYYSWRCP-----KPlknRDVITL---RSWLPMGADYIIMNY 221
Cdd:cd08873    87 TCASDAFDLLSDPFKRPEWDPHGRSCEEVKR--VGEDDGIYHTTMPsltseKP---NDFVLLvsrRKPATDGDPYKVAFR 161

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1338686448 222 SVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKgslpkwVVNKSSQFLA--PKAMKKMYKACIKY 295
Cdd:cd08873   162 SVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPK------LLSYVTCNLAglSALYCRTFHCCEQF 231
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 112-295 1.99e-04

Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice.


Pssm-ID: 176921  Cd Length: 240  Bit Score: 42.55  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 112 AEVGWNLTYSKAGVSVWVqaVEMDRTLhKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVIETFDIARltVNADVGYYS 191
Cdd:cd08913    57 AKDNWVLSSEKNQVRLYT--LEEDKFL-SFKVEMVV-HVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQ--VDEDDAIYH 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 192 WRCP---KPLKNRDVITLRSWLP---MGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPk 265
Cdd:cd08913   131 VTSPslsGHGKPQDFVILASRRKpcdNGDPYVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATP- 209

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1338686448 266 GSLP---KWVVNKSSQFlapkamKKMYKACIKY 295
Cdd:cd08913   210 GVLPyisTDIAGLSSEF------YSTFSACSQF 236
START_STARD11-like cd08872
Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily ...
 216-294 2.96e-04

Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD11 and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD11 can mediate transfer of the natural ceramide isomers, dihydroceramide and phytoceramide, as well as ceramides having C14, C16, C18, and C20 chains. They can also transfer diacylglycerol, but with a lower efficiency. STARD11 is synthesized from two major transcripts: a larger one encoding Goodpasture antigen-binding protein (GPBP)/ceramide transporter long form (CERTL); and a smaller one encoding GPBPdelta26/CERT, which is deleted for 26 amino acids. Both splicing variants mediate ceramide transfer from the ER to the Golgi, in a non-vesicular manner. It is likely that these two carry out different functions in specific sub-cellular locations. These proteins have roles in brain homeostasis and disease processes. GPBP/CERTL exists in multiple isoforms originating from alternative translation initiation sites and post-translational modifications. Goodpasture syndrome is a human disorder caused by antibodies directed against the a3-chain of collagen type IV. GPBP/CERTL binds and phosphorylates this antigen. The human gene encoding STARD11 is referred to as COL4A3BP referring to its collagen binding function. It is unknown whether the ceramide-transfer function of GPBP/CERTL is related to this collagen interaction. The expression of GPBP/CERTL is elevated in these and other spontaneous autoimmune disorders including cutaneous lupus erythematosus, pemphigoid, and lichen planus. GPBL/CERTL contains an N-terminal pleckstrin homology domain (PH), which targets the protein to the Golgi, a middle region containing two serine-rich domains (SR1, SR2), a FFAT (two phenylalanine amino acids in an acidic tract) motif which is involved in endoplasmic reticulum targeting, and this C-terminal SMART domain. The shorter splicing variant, CERT, lacks the SR2 domain.


Pssm-ID: 176881  Cd Length: 235  Bit Score: 41.94  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 216 YIIMNYSVKHPKYPPRKDLVRA---VSI--QTgyLIQSTGPK--------SCVITYLAQVDPKGSLPKWVVNKSSQFLAP 282
Cdd:cd08872   137 WIVCNFSVDHDSAPLNNKCVRAkltVAMicQT--FVSPPDGNqeitrdniLCKITYVANVNPGGWAPASVLRAVYKREYP 214

                          90
                  ....*....|..
gi 1338686448 283 KAMKKMYKACIK 294
Cdd:cd08872   215 KFLKRFTSYVQE 226
DUF3074 pfam11274
Protein of unknown function (DUF3074); This eukaryotic family of proteins has no known ...
 195-276 4.34e-04

Protein of unknown function (DUF3074); This eukaryotic family of proteins has no known function but appears to be part of the START superfamily.


Pssm-ID: 431775  Cd Length: 181  Bit Score: 40.70  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 195 PKPLKNRDVITL---------RSWLPMGADYIIMNYSVK-HPKYPPRKDLVRA--VSIQTGYLI----QSTGPKSCV--- 255
Cdd:pfam11274  67 PGPLTPRDFVVLlltadlppeESPGSEHAEFMVVSIPVDdHPDAPPRKGFVRGqyESVERIREIpvddEYDEETGPVewi 146

                          90       100
                  ....*....|....*....|..
gi 1338686448 256 -ITylaQVDPKGSLPKWVVNKS 276
Cdd:pfam11274 147 mAT---ASDAGGSIPRWLQEKG 165
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 115-275 5.65e-04

Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4, -5, and -6. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7a-hydroxycholesterol. STARD4 and STARD5 are ubiquitously expressed, with highest levels in liver and kidney. STRAD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.


Pssm-ID: 176876  Cd Length: 206  Bit Score: 40.52  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 115 GWNLTYSKAGVSVWVQA-VEMDRTLHKIKCRMeccDVPAETLYDVLHDIE--YRKKWDSNVIETFDIARLTVNADVGYYS 191
Cdd:cd08867    23 GWKVLKTVKNITVSWKPsTEFTGHLYRAEGIV---DALPEKVIDVIIPPCggLRLKWDKSLKHYEVLEKISEDLCVGRTI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 192 wrCPKPLKN----RDVITLrSWLPMGADYIIMN--YSVKHPKYPPRKDLVRAVSIQTGYLIQST--GPKSCVITYLAQVD 263
Cdd:cd08867   100 --TPSAAMGlispRDFVDL-VYVKRYEDNQWSSsgKSVDIPERPPTPGFVRGYNHPCGYFCSPLkgSPDKSFLVLYVQTD 176

                         170
                  ....*....|..
gi 1338686448 264 PKGSLPKWVVNK 275
Cdd:cd08867   177 LRGMIPQSLVES 188
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 149-275 3.92e-03

Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD1 has a high affinity for cholesterol. It can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads.


Pssm-ID: 176914  Cd Length: 209  Bit Score: 38.28  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686448 149 DVPAETLYDVLHD-IEYRKKWDSNVIETFDIARLTVNADVGYYSwrCPKPLKN----RDVITLRSWLPMGADYIIMNYSV 223
Cdd:cd08905    58 DQPLDNLYSELVDrMEQMGEWNPNVKEVKILQRIGKDTLITHEV--AAETAGNvvgpRDFVSVRCAKRRGSTCVLAGMAT 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1338686448 224 KHPKYPPRKDLVRAVSIQTGYLIQSTG--PKSCVITYLAQVDPKGSLPKWVVNK 275
Cdd:cd08905   136 HFGLMPEQKGFIRAENGPTCIVLRPLAgdPSKTKLTWLLSIDLKGWLPKSIINQ 189
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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