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Conserved domains on  [gi|1494863088|ref|NP_001036998|]
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carotenoid-binding protein isoform 1 [Bombyx mori]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 246-470 4.78e-107

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: 316.60  E-value: 4.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 246 EQIDEYKSQANESMANAWRIITLPNWTVEKRGSvRGDVVESRKVEGYGKVYRFTGVVNCPARFLYEEFKNNLTKLPEWNP 325
Cdd:cd08868     1 SQELEYLKQGAEALARAWSILTDPGWKLEKNTT-WGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 326 TILKCEIIKEIGDGVDLSYQVTAGGGRGIITPRDFVILRRIALLSregrvvddnpHGYISSGVSVQVPGYPPLKEMVRGH 405
Cdd:cd08868    80 TVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRE----------NCYLSSGVSVEHPAMPPTKNYVRGE 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1494863088 406 NKVGCWYLQPRTVqtaggkIEDQTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRKFVAEA 470
Cdd:cd08868   150 NGPGCWILRPLPN------NPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIATL 208
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 49-227 6.19e-81

Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal membrane protein, and carries this MENTAL (MLN64N-terminal) domain at its N-terminus. The domain is composed of four trans-membrane helices with three short intervening loops. The function of the domain is to capture cholesterol and pass it to the associated START domain pfam01852 for transfer to a cytosolic acceptor protein or membrane. In mammals, the MENTAL domain is involved in the localization of MLN64 and MENTHO in late endosomes, and also in homo-and of hetero-interactions of these two proteins.


:

Pssm-ID: 463097  Cd Length: 177  Bit Score: 248.36  E-value: 6.19e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088  49 SSVRRFFCLFVTFDLMFTSLMWLICVMVRNETLDQILQREIISYNIKLSLFDIVVLAVIRFTILLLFYALLYINNWSVIA 128
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINGENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 129 LSTSGTCAFLIAKVFVFVWSDASQPVYQVFLILTSFTLSWGEAWFLDFRVLPQELHcKEILDSLAQHSVSERTPLLDPQP 208
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLSSSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAE-AERRYLAAITSADERAPLLQPGP 159

                         170
                  ....*....|....*....
gi 1494863088 209 GVNSTYAESTvKWFSPVDT 227
Cdd:pfam10457 160 EGRSNNQSDG-NFYSPPES 177
 
Name Accession Description Interval E-value
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 246-470 4.78e-107

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: 316.60  E-value: 4.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 246 EQIDEYKSQANESMANAWRIITLPNWTVEKRGSvRGDVVESRKVEGYGKVYRFTGVVNCPARFLYEEFKNNLTKLPEWNP 325
Cdd:cd08868     1 SQELEYLKQGAEALARAWSILTDPGWKLEKNTT-WGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 326 TILKCEIIKEIGDGVDLSYQVTAGGGRGIITPRDFVILRRIALLSregrvvddnpHGYISSGVSVQVPGYPPLKEMVRGH 405
Cdd:cd08868    80 TVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRE----------NCYLSSGVSVEHPAMPPTKNYVRGE 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1494863088 406 NKVGCWYLQPRTVqtaggkIEDQTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRKFVAEA 470
Cdd:cd08868   150 NGPGCWILRPLPN------NPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIATL 208
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 49-227 6.19e-81

Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal membrane protein, and carries this MENTAL (MLN64N-terminal) domain at its N-terminus. The domain is composed of four trans-membrane helices with three short intervening loops. The function of the domain is to capture cholesterol and pass it to the associated START domain pfam01852 for transfer to a cytosolic acceptor protein or membrane. In mammals, the MENTAL domain is involved in the localization of MLN64 and MENTHO in late endosomes, and also in homo-and of hetero-interactions of these two proteins.


Pssm-ID: 463097  Cd Length: 177  Bit Score: 248.36  E-value: 6.19e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088  49 SSVRRFFCLFVTFDLMFTSLMWLICVMVRNETLDQILQREIISYNIKLSLFDIVVLAVIRFTILLLFYALLYINNWSVIA 128
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINGENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 129 LSTSGTCAFLIAKVFVFVWSDASQPVYQVFLILTSFTLSWGEAWFLDFRVLPQELHcKEILDSLAQHSVSERTPLLDPQP 208
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLSSSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAE-AERRYLAAITSADERAPLLQPGP 159

                         170
                  ....*....|....*....
gi 1494863088 209 GVNSTYAESTvKWFSPVDT 227
Cdd:pfam10457 160 EGRSNNQSDG-NFYSPPES 177
START pfam01852
START domain;
267-473 1.63e-26

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 106.33  E-value: 1.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 267 TLPNWtVEKRGSVRGDVVESRKVEGYGKVYRFTGVVNCPARFLYEEFKNNLTKLPEWNPTILKCEIIKEIGDGVDLSYQV 346
Cdd:pfam01852  17 DEPGW-VLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 347 TAGGGRGIITPRDFVILRRIallsREgrvvdDNPHGYISSGVSVQVPGYPPLKEMVRGHNKVGCWYLQPrtvqTAGGKie 426
Cdd:pfam01852  96 AALVAPSPLSPRDFVFLRYW----RR-----LGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQP----CGNGP-- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1494863088 427 dqTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRKFVAEAKAR 473
Cdd:pfam01852 161 --SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 269-473 4.57e-25

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 102.12  E-value: 4.57e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088  269 PNWtVEKRGSVRGDVVESRKVEGY--GKVYRFTGVVNCPARFLYEEFKNNLTKLPEWNPTILKCEIIKEIGDGVDLSYQV 346
Cdd:smart00234  18 EGW-VLSSENENGDEVRSIFSPGRkpGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYHYV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088  347 TAGGGrGIITPRDFVILRRIALLSREGRVVddnphgyisSGVSVQVPGYPPLKEMVRGHNKVGCWYLQPRtvqtAGGKie 426
Cdd:smart00234  97 SKFAA-GPVSPRDFVFVRYWREDEDGSYAV---------VDVSVTHPTSPPESGYVRAENLPSGLLIEPL----GNGP-- 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1494863088  427 dqTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRKFVAEAKAR 473
Cdd:smart00234 161 --SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
 
Name Accession Description Interval E-value
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 246-470 4.78e-107

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: 316.60  E-value: 4.78e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 246 EQIDEYKSQANESMANAWRIITLPNWTVEKRGSvRGDVVESRKVEGYGKVYRFTGVVNCPARFLYEEFKNNLTKLPEWNP 325
Cdd:cd08868     1 SQELEYLKQGAEALARAWSILTDPGWKLEKNTT-WGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 326 TILKCEIIKEIGDGVDLSYQVTAGGGRGIITPRDFVILRRIALLSregrvvddnpHGYISSGVSVQVPGYPPLKEMVRGH 405
Cdd:cd08868    80 TVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRE----------NCYLSSGVSVEHPAMPPTKNYVRGE 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1494863088 406 NKVGCWYLQPRTVqtaggkIEDQTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRKFVAEA 470
Cdd:cd08868   150 NGPGCWILRPLPN------NPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIATL 208
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 49-227 6.19e-81

Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal membrane protein, and carries this MENTAL (MLN64N-terminal) domain at its N-terminus. The domain is composed of four trans-membrane helices with three short intervening loops. The function of the domain is to capture cholesterol and pass it to the associated START domain pfam01852 for transfer to a cytosolic acceptor protein or membrane. In mammals, the MENTAL domain is involved in the localization of MLN64 and MENTHO in late endosomes, and also in homo-and of hetero-interactions of these two proteins.


Pssm-ID: 463097  Cd Length: 177  Bit Score: 248.36  E-value: 6.19e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088  49 SSVRRFFCLFVTFDLMFTSLMWLICVMVRNETLDQILQREIISYNIKLSLFDIVVLAVIRFTILLLFYALLYINNWSVIA 128
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINGENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 129 LSTSGTCAFLIAKVFVFVWSDASQPVYQVFLILTSFTLSWGEAWFLDFRVLPQELHcKEILDSLAQHSVSERTPLLDPQP 208
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLSSSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAE-AERRYLAAITSADERAPLLQPGP 159

                         170
                  ....*....|....*....
gi 1494863088 209 GVNSTYAESTvKWFSPVDT 227
Cdd:pfam10457 160 EGRSNNQSDG-NFYSPPES 177
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 246-469 7.09e-34

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: 126.51  E-value: 7.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 246 EQIDEYKSQANESMANAWRIITL-PNWTVEKRGSVrGDVVESRKVEGYGKVYRFTGVVNCPARFLYEEFKNNLTKLPEWN 324
Cdd:cd08906     1 PQEREYVRQGKEALAVVEQILAQeENWKFEKNNDN-GDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 325 PTILKCEIIKEIGDGVDLSYQVTAGGGRGIITPRDFVILRRIAllsregRVVDDnphgYISSGVSVQVPGYPPLKEMVRG 404
Cdd:cd08906    80 KTVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIE------RRRDR----YVSAGISTTHSHKPPLSKYVRG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1494863088 405 HNKVGCWYLQPrtvqtaGGKIEDQTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRKFVAE 469
Cdd:cd08906   150 ENGPGGFVVLK------SASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIRD 208
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 251-470 3.12e-28

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: 111.08  E-value: 3.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 251 YKSQANESMANAWRIIT-LPNWTVEKRgSVRGDVVESRKVEGYGKVYRFTGVVNCPARFLYEEFKNNLTKLPEWNPTILK 329
Cdd:cd08905     6 YIKQGEEALQKSLSILQdQEGWKTEIV-AENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNPNVKE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 330 CEIIKEIGDGVDLSYQVTAGGGRGIITPRDFVILRriaLLSREGRVVddnphgyISSGVSVQVPGYPPLKEMVRGHNKVG 409
Cdd:cd08905    85 VKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVR---CAKRRGSTC-------VLAGMATHFGLMPEQKGFIRAENGPT 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1494863088 410 CWYLQPrtvqTAGGKieDQTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRKFVAEA 470
Cdd:cd08905   155 CIVLRP----LAGDP--SKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRMASS 209
START pfam01852
START domain;
267-473 1.63e-26

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 106.33  E-value: 1.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 267 TLPNWtVEKRGSVRGDVVESRKVEGYGKVYRFTGVVNCPARFLYEEFKNNLTKLPEWNPTILKCEIIKEIGDGVDLSYQV 346
Cdd:pfam01852  17 DEPGW-VLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 347 TAGGGRGIITPRDFVILRRIallsREgrvvdDNPHGYISSGVSVQVPGYPPLKEMVRGHNKVGCWYLQPrtvqTAGGKie 426
Cdd:pfam01852  96 AALVAPSPLSPRDFVFLRYW----RR-----LGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQP----CGNGP-- 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1494863088 427 dqTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRKFVAEAKAR 473
Cdd:pfam01852 161 --SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 269-473 4.57e-25

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 102.12  E-value: 4.57e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088  269 PNWtVEKRGSVRGDVVESRKVEGY--GKVYRFTGVVNCPARFLYEEFKNNLTKLPEWNPTILKCEIIKEIGDGVDLSYQV 346
Cdd:smart00234  18 EGW-VLSSENENGDEVRSIFSPGRkpGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYHYV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088  347 TAGGGrGIITPRDFVILRRIALLSREGRVVddnphgyisSGVSVQVPGYPPLKEMVRGHNKVGCWYLQPRtvqtAGGKie 426
Cdd:smart00234  97 SKFAA-GPVSPRDFVFVRYWREDEDGSYAV---------VDVSVTHPTSPPESGYVRAENLPSGLLIEPL----GNGP-- 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1494863088  427 dqTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRKFVAEAKAR 473
Cdd:smart00234 161 --SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 269-468 6.02e-25

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: 101.65  E-value: 6.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 269 PNWTVEKRGSvrGDVVESRKVEGYG-KVYRFTGVVNCPARFLYEEFkNNLTKLPEWNPTILKCEIIKEIGDGVDLSYQVT 347
Cdd:cd00177    15 EGWKLVKEKD--GVKIYTKPYEDSGlKLLKAEGVIPASPEQVFELL-MDIDLRKKWDKNFEEFEVIEEIDEHTDIIYYKT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 348 AGGGrgIITPRDFVILRRIallsregrvVDDNPHGYISSGVSVQVPGYPPLKEMVRGHNKVGCWYLQPrtvqtaggKIED 427
Cdd:cd00177    92 KPPW--PVSPRDFVYLRRR---------RKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEP--------LDPG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1494863088 428 QTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRKFVA 468
Cdd:cd00177   153 KTKVTYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLRKAKK 193
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 271-465 4.28e-19

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: 85.59  E-value: 4.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 271 WTVEKRGSvrgDVVESRK--VEGYGKVYRFTGVVNCPARFLYEEFKNNLTKLP-EWNPTILKCEIIKEIGDGVDLSYQVT 347
Cdd:cd08867    24 WKVLKTVK---NITVSWKpsTEFTGHLYRAEGIVDALPEKVIDVIIPPCGGLRlKWDKSLKHYEVLEKISEDLCVGRTIT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 348 AGGGRGIITPRDFVILRRIallsregRVVDDNphGYISSGVSVQVPGYPPLKEMVRGHNKVGCWYLQPRTVQTAGGKIEd 427
Cdd:cd08867   101 PSAAMGLISPRDFVDLVYV-------KRYEDN--QWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPLKGSPDKSFLV- 170

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1494863088 428 qTLFQwlmcCDLKGKIPQFVLDVAFATVMLDYIVHVRK 465
Cdd:cd08867   171 -LYVQ----TDLRGMIPQSLVESAMPSNLVNFYTDLVK 203
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 271-467 1.33e-10

Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD5, 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. STARD5 is ubiquitously expressed, with highest levels in liver and kidney. STARD5 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.


Pssm-ID: 176912  Cd Length: 208  Bit Score: 61.01  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 271 WTVEKRGsvRGDVVESR-KVEGYGKVYRFTGVVNCPARFLYEEFKNNLTKL-PEWNPTILKCEIIKEIGDGVDLSYQVTA 348
Cdd:cd08903    24 WKTCRRT--NEVAVSWRpSAEFAGNLYKGEGIVYATLEQVWDCLKPAAGGLrVKWDQNVKDFEVVEAISDDVSVCRTVTP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 349 GGGRGIITPRDFVilrRIALLSRegrvVDDnphGYISSGVS-VQVPGYPPLKEMVRGHNK-VGCwYLQPrtVQTAGGKIE 426
Cdd:cd08903   102 SAAMKIISPRDFV---DVVLVKR----YED---GTISSNATnVEHPLCPPQAGFVRGFNHpCGC-FCEP--VPGEPDKTQ 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1494863088 427 DQTLFQwlmcCDLKGKIPQFVLDVAFATVMLDYIVHVRKFV 467
Cdd:cd08903   169 LVSFFQ----TDLSGYLPQTVVDSFFPASMAEFYNNLTKAV 205
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 293-460 1.40e-07

Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD6 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. 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: 176913  Cd Length: 204  Bit Score: 51.83  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 293 GKVYRFTGVV-NCPAR---FLYeeFKNNLTKlpeWNPTILKCEIIKEIGDGVDLSYQVTAGGGRGIITPRDFVILRRIAL 368
Cdd:cd08904    45 GNLYRVEGIIpESPAKliqFMY--QPEHRIK---WDKSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKR 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 369 LsrEGRVVddnphgyISSGVSVQVPGYPPLKEMVRGHNKVGCWYLQPRTVQTAGGKIedqTLFqwlMCCDLKGKIPQFVL 448
Cdd:cd08904   120 Y--EGNMN-------IVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPENPAYSKL---VMF---VQPELRGNLSRSVI 184

                         170
                  ....*....|..
gi 1494863088 449 DVAFATVMLDYI 460
Cdd:cd08904   185 EKTMPTNLVNLI 196
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 271-465 8.20e-07

Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4 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. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7alpha-hydroxycholesterol. STARD4 is ubiquitously expressed, with highest levels in liver and kidney.


Pssm-ID: 176911  Cd Length: 202  Bit Score: 49.57  E-value: 8.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 271 WTVEKRGSvrgDVVESRKV--EGYGKVYRFTGVVNCPARFLYEEFKNNLTKLpEWNPTILKCEIIKEIGDGVDLSYQVTA 348
Cdd:cd08902    25 WRVAKKSK---DVTVWRKPseEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRL-DWDSLMTSMDIIEEFEENCCVMRYTTA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 349 GGGRGIITPRDFVilrriallsrEGRVVDDNPHGYISSGVSVQVPGYPPlkEMVRGHNKVGCWYLQPrtvqtaggkIED- 427
Cdd:cd08902   101 GQLLNIISPREFV----------DFSYTTQYEDGLLSCGVSIEYEEARP--NFVRGFNHPCGWFCVP---------LKDn 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1494863088 428 --QTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRK 465
Cdd:cd08902   160 psHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKK 199
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 301-404 2.18e-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: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 301 VVNCPARFLYEEFKNnLTKLPEWNPTILKCEIIKEIGDGvDLSYQVTAgGGRGIITPRDFVIlrriaLLSREGRVVDDNP 380
Cdd:cd08873    84 KVQTCASDAFDLLSD-PFKRPEWDPHGRSCEEVKRVGED-DGIYHTTM-PSLTSEKPNDFVL-----LVSRRKPATDGDP 155

                          90       100
                  ....*....|....*....|....
gi 1494863088 381 hgYISSGVSVQVPGYPPLKEMVRG 404
Cdd:cd08873   156 --YKVAFRSVTLPRVPQTPGYSRT 177
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 238-403 4.09e-06

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: 47.97  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 238 GEQVILTQEQIDEYKSQANEsmaNAWRII-TLPN---WTVEKRgsvrgDVVeSRKVEGYGKVyrftgvvncPARFLYEeF 313
Cdd:cd08914    36 GNQASLSDSNVEALKKLAAK---SGWEVTsTVEKikiYTLEEH-----DVL-SVWVEKHVKR---------PAHLAYR-L 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 314 KNNLTKLPEWNPTILKCEIIKEIGDGvDLSYQVTAGGGRGiITPRDFVIlrriaLLSREGRVVDDNPhgYISSGVSVQVP 393
Cdd:cd08914    97 LSDFTKRPLWDPHFLSCEVIDWVSED-DQIYHITCPIVNN-DKPKDLVV-----LVSRRKPLKDGNT--YVVAVKSVILP 167

                         170
                  ....*....|
gi 1494863088 394 GYPPLKEMVR 403
Cdd:cd08914   168 SVPPSPQYIR 177
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 355-447 4.50e-04

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: 41.47  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 355 ITPRDFVILRriALLsregrvvdDNPHGYISSGVSVQVPGYPPLKEMVRGHNKVGCWYLQPrtvqtaggKIEDQTLFQWL 434
Cdd:cd08871   106 LKNRDFVNLR--SWL--------EFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRP--------TGPKGCTLTYV 167

                          90
                  ....*....|...
gi 1494863088 435 MCCDLKGKIPQFV 447
Cdd:cd08871   168 TQNDPKGSLPKWV 180
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 269-465 9.66e-04

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: 40.33  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 269 PNWTVEKRGSvrGDVVESRKVEGyGKVYRFTGVVNCPARFlyEEFK---NNLTKLPEWNPTILKCEIIKEIGDGVDLSYQ 345
Cdd:cd08876    17 GDWQLVKDKD--GIKVYTRDVEG-SPLKEFKAVAEVDASI--EAFLallRDTESYPQWMPNCKESRVLKRTDDNERSVYT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 346 VTAgggrgiiTP-----RDFVILRRIALLSREGRVVDDNPHgyissgvsvqVPGYPPLKE-MVRGHNKVGCWYLQPRTvq 419
Cdd:cd08876    92 VID-------LPwpvkdRDMVLRSTTEQDADDGSVTITLEA----------APEALPEQKgYVRIKTVEGQWTFTPLG-- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1494863088 420 taggkiEDQTLFQWLMCCDLKGKIPQFVLDVAFATVMLDYIVHVRK 465
Cdd:cd08876   153 ------NGKTRVTYQAYADPGGSIPGWLANAFAKDAPYNTLENLRK 192
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 315-404 1.31e-03

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: 40.24  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1494863088 315 NNLTKLPEWNPTILKCEIIKEIgDGVDLSYQVTAGGGRGIITPRDFVILRriallSRegRVVDDNPHGYISSGVSVQVPG 394
Cdd:cd08913   101 SDLRRRPEWDKHYRSCELVQQV-DEDDAIYHVTSPSLSGHGKPQDFVILA-----SR--RKPCDNGDPYVIALRSVTLPT 172

                          90
                  ....*....|
gi 1494863088 395 YPPLKEMVRG 404
Cdd:cd08913   173 HPPTPEYTRG 182
 
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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