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Conserved domains on  [gi|808688331|ref|NP_001294987|]
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stAR-related lipid transfer protein 4 isoform b [Homo sapiens]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 5-137 2.93e-92

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


The actual alignment was detected with superfamily member cd08902:

Pssm-ID: 472699  Cd Length: 202  Bit Score: 266.43  E-value: 2.93e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688331   5 SDVASFATKLKNTLIQYHSIEEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMT 84
Cdd:cd08902    1 LDIASKTTKLQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 808688331  85 SLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGNNLN 137
Cdd:cd08902   81 SMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIE 133
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 5-137 2.93e-92

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: 266.43  E-value: 2.93e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688331   5 SDVASFATKLKNTLIQYHSIEEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMT 84
Cdd:cd08902    1 LDIASKTTKLQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 808688331  85 SLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGNNLN 137
Cdd:cd08902   81 SMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIE 133
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 24-122 2.23e-03

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 37.03  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688331    24 IEEDKW--RVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDD----LVYSIIDHIRPgpcRLDWDSLMTSLDILENFEENCC 97
Cdd:smart00234  15 ASEEGWvlSSENENGDEVRSIFSPGRKPGEAFRLVGVVPMvcadLVEELMDDLEY---RPEWDKNVAKAETLEVIDNGTV 91

                           90       100
                   ....*....|....*....|....*
gi 808688331    98 VMRYTTAGQlWNIISPREFVDFSYT 122
Cdd:smart00234  92 IYHYVSKFA-AGPVSPRDFVFVRYW 115
START pfam01852
START domain;
25-121 5.80e-03

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 35.84  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688331   25 EEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVID----DLVYSIIDHirpGPCRLDWDSLMTSLDILENFEENCCVMR 100
Cdd:pfam01852  17 DEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPmvaaLLVAELLKD---MEYRAQWDKDVRSAETLEVISSGGDLQY 93

                          90       100
                  ....*....|....*....|.
gi 808688331  101 YTTAGQLWNIISPREFVDFSY 121
Cdd:pfam01852  94 YVAALVAPSPLSPRDFVFLRY 114
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 5-137 2.93e-92

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: 266.43  E-value: 2.93e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688331   5 SDVASFATKLKNTLIQYHSIEEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMT 84
Cdd:cd08902    1 LDIASKTTKLQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 808688331  85 SLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGNNLN 137
Cdd:cd08902   81 SMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIE 133
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 5-133 8.92e-57

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: 176.50  E-value: 8.92e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688331   5 SDVASFATKLKNTLIQYHSIEeDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRP--GPCRLDWDSL 82
Cdd:cd08867    1 MDFKVIAEKLANEALQYINDT-DGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIPpcGGLRLKWDKS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 808688331  83 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEG-LLSCG 133
Cdd:cd08867   80 LKHYEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNqWSSSG 131
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 5-131 8.12e-21

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: 84.50  E-value: 8.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688331   5 SDVASFATKLKNTLIQYHSiEEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRP--GPCRLDWDSL 82
Cdd:cd08903    1 MDYAELAESVADKMLLYRR-DESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPaaGGLRVKWDQN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 808688331  83 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLS 131
Cdd:cd08903   80 VKDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTIS 128
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 25-144 9.29e-18

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: 75.84  E-value: 9.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688331  25 EEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMTSLDILENFEENCCVMRYTTA 104
Cdd:cd00177   13 EPEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHTDIIYYKTK 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 808688331 105 GQLwnIISPREFVDFSYTvgYKEgllscGNNLNMLCFFSV 144
Cdd:cd00177   93 PPW--PVSPRDFVYLRRR--RKL-----DDGTYVIVSKSV 123
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 29-128 8.32e-13

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: 63.00  E-value: 8.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688331  29 WRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMTSLDILENFEENCCVMRYTTAGQLW 108
Cdd:cd08904   24 WKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAM 103

                         90       100
                 ....*....|....*....|
gi 808688331 109 NIISPREFVDFSYtVGYKEG 128
Cdd:cd08904  104 GSISPRDFVDLVH-IKRYEG 122
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 24-122 2.23e-03

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 37.03  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688331    24 IEEDKW--RVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDD----LVYSIIDHIRPgpcRLDWDSLMTSLDILENFEENCC 97
Cdd:smart00234  15 ASEEGWvlSSENENGDEVRSIFSPGRKPGEAFRLVGVVPMvcadLVEELMDDLEY---RPEWDKNVAKAETLEVIDNGTV 91

                           90       100
                   ....*....|....*....|....*
gi 808688331    98 VMRYTTAGQlWNIISPREFVDFSYT 122
Cdd:smart00234  92 IYHYVSKFA-AGPVSPRDFVFVRYW 115
START pfam01852
START domain;
25-121 5.80e-03

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 35.84  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808688331   25 EEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVID----DLVYSIIDHirpGPCRLDWDSLMTSLDILENFEENCCVMR 100
Cdd:pfam01852  17 DEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPmvaaLLVAELLKD---MEYRAQWDKDVRSAETLEVISSGGDLQY 93

                          90       100
                  ....*....|....*....|.
gi 808688331  101 YTTAGQLWNIISPREFVDFSY 121
Cdd:pfam01852  94 YVAALVAPSPLSPRDFVFLRY 114
 
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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