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Conserved domains on  [gi|61556854|ref|NP_001013087|]
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START domain-containing protein 10 [Rattus norvegicus]

Protein Classification

START domain-containing protein( domain architecture ID 10172287)

START (steroidogenic acute regulatory protein (StAR)-related lipid transfer) domain-containing protein may bind lipids; similar to STARD10 that may play metabolic roles in sperm maturation or fertilization

CATH:  3.30.530.20
Gene Ontology:  GO:0008289
PubMed:  10322415|31927098
SCOP:  4002052

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 ...
 19-241 4.81e-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: 406.26  E-value: 4.81e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  19 RESVQVPDDQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSN 98
Cdd:cd08871   1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPE-NSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  99 VIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGP 178
Cdd:cd08871  80 MIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGP 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61556854 179 KSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKYPEWKQKHQPHFKPWLHPEQ 241
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 ...
 19-241 4.81e-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: 406.26  E-value: 4.81e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  19 RESVQVPDDQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSN 98
Cdd:cd08871   1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPE-NSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  99 VIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGP 178
Cdd:cd08871  80 MIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGP 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61556854 179 KSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKYPEWKQKHQPHFKPWLHPEQ 241
Cdd:cd08871 160 KGCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKNNPEFKPWLYPEQ 222
START pfam01852
START domain;
76-224 1.43e-24

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 97.86  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854    76 DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYS----WrcPKPLKNRDVITLRSWLPMGAD-YIIMNYSV 150
Cdd:pfam01852  53 MVAALLVAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVaalvA--PSPLSPRDFVFLRYWRRLGGGvYVIVDRSV 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61556854   151 KHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKYPE 224
Cdd:pfam01852 131 THPQFPPSSGYVRAERLPSGYLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCE 204
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 37-226 4.74e-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: 91.34  E-value: 4.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854     37 CEAEVGWNLTYSKAGVSVWVQAVEMDRTLHKIkcrMECC----DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNA 112
Cdd:smart00234  14 AASEEGWVLSSENENGDEVRSIFSPGRKPGEA---FRLVgvvpMVCADLVEELMDDLEYRPEWDKNVAKAETLEVIDNGT 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854    113 DVGYYSWRCP-KPLKNRDVITLRSWLPMGAD-YIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVD 190
Cdd:smart00234  91 VIYHYVSKFAaGPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGPSKVTWVSHAD 170

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 61556854    191 PKGSLPKWVVNkSSQFLAPKAMKKMYKACIKYPEWK 226
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 ...
 19-241 4.81e-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: 406.26  E-value: 4.81e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  19 RESVQVPDDQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSN 98
Cdd:cd08871   1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPE-NSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  99 VIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGP 178
Cdd:cd08871  80 MIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGP 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61556854 179 KSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKYPEWKQKHQPHFKPWLHPEQ 241
Cdd:cd08871 160 KGCTLTYVTQNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKYPEWKAKNNPEFKPWLYPEQ 222
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 27-219 9.15e-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: 168.29  E-value: 9.15e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  27 DQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVIETFDIA 106
Cdd:cd00177   1 EEAIEELLELLEEPEGWKLVKEKDGVKIYTKPYE-DSGLKLLKAEGVI-PASPEQVFELLMDIDLRKKWDKNFEEFEVIE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854 107 RLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGAD-YIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITY 185
Cdd:cd00177  79 EIDEHTDIIYYKTKPPWPVSPRDFVYLRRRRKLDDGtYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTY 158

                       170       180       190
                ....*....|....*....|....*....|....
gi 61556854 186 LAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKAC 219
Cdd:cd00177 159 VLQVDPKGSIPKSLVNSAAKKQLASFLKDLRKAK 192
START pfam01852
START domain;
76-224 1.43e-24

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 97.86  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854    76 DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYS----WrcPKPLKNRDVITLRSWLPMGAD-YIIMNYSV 150
Cdd:pfam01852  53 MVAALLVAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVaalvA--PSPLSPRDFVFLRYWRRLGGGvYVIVDRSV 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61556854   151 KHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKYPE 224
Cdd:pfam01852 131 THPQFPPSSGYVRAERLPSGYLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCE 204
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 37-226 4.74e-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: 91.34  E-value: 4.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854     37 CEAEVGWNLTYSKAGVSVWVQAVEMDRTLHKIkcrMECC----DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNA 112
Cdd:smart00234  14 AASEEGWVLSSENENGDEVRSIFSPGRKPGEA---FRLVgvvpMVCADLVEELMDDLEYRPEWDKNVAKAETLEVIDNGT 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854    113 DVGYYSWRCP-KPLKNRDVITLRSWLPMGAD-YIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVD 190
Cdd:smart00234  91 VIYHYVSKFAaGPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGPSKVTWVSHAD 170

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 61556854    191 PKGSLPKWVVNkSSQFLAPKAMKKMYKACIKYPEWK 226
Cdd:smart00234 171 LKGWLPHWLVR-SLIKSGLAEFAKTLVATLQKHCAK 205
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 33-222 2.02e-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: 78.69  E-value: 2.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  33 FRSECeAEVG--------WNLTYSKAGVSVWvQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFD 104
Cdd:cd08910  10 FREAC-AELQqpaldgaaWELLVESSGISIY-RLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQYVKELYE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854 105 iaRLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADY----IIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKS 180
Cdd:cd08910  88 --KECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGrkiwVILARSTSLPQLPEKPGVIRVKQYKQSLAIESDGKKG 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 61556854 181 CVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKY 222
Cdd:cd08910 166 SKVFMYYFDNPGGMIPSWLINWAAKNGVPNFLKDMQKACQNY 207
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 38-222 4.78e-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: 77.71  E-value: 4.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  38 EAEVGWNLTYSKAGVSVWVQAvEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTV-NADVGY 116
Cdd:cd08911  18 QEPDGWEPFIEKKDMLVWRRE-HPGTGLYEYKVYGSFDDVTARDFLNVQLDLEYRKKWDATAVELEVVDEDPEtGSEIIY 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854 117 YSWRCPKPLKNRDVITLRSWLpmgADY-----IIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSC-----VITYL 186
Cdd:cd08911  97 WEMQWPKPFANRDYVYVRRYI---IDEenkliVIVSKAVQHPSYPESPKKVRVEDYWSYMVIRPHKSFDEpgfefVLTYF 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 61556854 187 AqvDPKGSLPK----WVVNKSsqflAPKAMKKMYKACIKY 222
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 ...
 76-213 1.87e-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: 76.24  E-value: 1.87e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  76 DVPAETLYDVL-HDIEYRKKWDSNVIETFDIARLTVNADVGYyswRCPKPLKN-----RDVITLRSWLPMGADYIIMNYS 149
Cdd:cd08868  57 DCPAEFLYNELvLNVESLPSWNPTVLECKIIQVIDDNTDISY---QVAAEAGGglvspRDFVSLRHWGIRENCYLSSGVS 133

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61556854 150 VKHPKYPPRKDLVRAVSIQTGYLIQSTG--PKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMK 213
Cdd:cd08868 134 VEHPAMPPTKNYVRGENGPGCWILRPLPnnPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMK 199
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 24-222 5.29e-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: 74.72  E-value: 5.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  24 VPDDQDFRSF---RSECEAEVGWNLTYSKAGVSVWVQA---VEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDS 97
Cdd:cd08870   2 HVSEEDLRDLvqeLQEGAEGQAWQQVMDKSTPDMSYQAwrrKPKGTGLYEYLVRGVFEDCTPELLRDFYWDDEYRKKWDE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  98 NVIETFDIARLTVNA-DVGYYSWRCPKPLKNRD-VITLRSWLPMGADYIIMNYSVKHPKYPPRKDL-VRAVSIQTGYLIQ 174
Cdd:cd08870  82 TVIEHETLEEDEKSGtEIVRWVKKFPFPLSDREyVIARRLWESDDRSYVCVTKGVPYPSVPRSGRKrVDDYESSLVIRAV 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 61556854 175 STGPK--SCVITYLAQvdPKGSLPKWVVNKSSQFLAPKAMKKMYKACIKY 222
Cdd:cd08870 162 KGDGQgsACEVTYFHN--PDGGIPRELAKLAVKRGMPGFLKKLENALRKY 209
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 40-202 1.01e-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: 73.84  E-value: 1.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  40 EVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYSW 119
Cdd:cd08876  16 DGDWQLVKDKDGIKVYTRDVE-GSPLKEFKAVAEV-DASIEAFLALLRDTESYPQWMPNCKESRVLKRTDDNERSVYTVI 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854 120 RCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPP-RKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKW 198
Cdd:cd08876  94 DLPWPVKDRDMVLRSTTEQDADDGSVTITLEAAPEALPeQKGYVRIKTVEGQWTFTPLGNGKTRVTYQAYADPGGSIPGW 173


                ....
gi 61556854 199 VVNK 202
Cdd:cd08876 174 LANA 177
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 33-203 1.32e-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: 73.50  E-value: 1.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  33 FRSECEAEVGWNLTYSKAGVSVWVQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDieyRKKWDSNVIETFDIARLTVNA 112
Cdd:cd08869  11 LREARDKSKGWVSVSSSDHVELAFKKVDDGHPLRLWRASTEVEAPPEEVLQRILRE---RHLWDDDLLQWKVVETLDEDT 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854 113 DVGYYSWRCPKPLKNRDVITLRSW---LPMGADYIIMNySVKHPK-YPPRkdLVRAVSIQTGYLIQSTGPKSCVITYLAQ 188
Cdd:cd08869  88 EVYQYVTNSMAPHPTRDYVVLRTWrtdLPKGACVLVET-SVEHTEpVPLG--GVRAVVLASRYLIEPCGSGKSRVTHICR 164

                       170
                ....*....|....*
gi 61556854 189 VDPKGSLPKWvVNKS 203
Cdd:cd08869 165 VDLRGRSPEW-YNKV 178
START_STARD12-like cd08908
C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also ...
 69-213 3.01e-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: 3.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  69 KCRMECCDVPAETLYDVLHDieyRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSW---LPMGADYII 145
Cdd:cd08908  55 RTTIEVPAAPEEILKRLLKE---QHLWDVDLLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWrtnLPKGACALL 131

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61556854 146 MNySVKHPKYPPRKdlVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMK 213
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 ...
 78-198 8.80e-10

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: 8.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  78 PAETLYDVLHDieyRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSW---LPMGAdYIIMNYSVKHPK 154
Cdd:cd08909  64 PSVVLNRVLRE---RHLWDEDFLQWKVVETLDKQTEVYQYVLNCMAPHPSRDFVVLRSWrtdLPKGA-CSLVSVSVEHEE 139

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 61556854 155 YPPRKDlVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKW 198
Cdd:cd08909 140 APLLGG-VRAVVLDSQYLIEPCGSGKSRLTHICRVDLKGHSPEW 182
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 39-224 2.15e-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: 2.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  39 AEVGWNLTysKAGVSVWVQAVEmDRTLHKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVI--ETFDiarlTVNADVGY 116
Cdd:cd08914  54 AKSGWEVT--STVEKIKIYTLE-EHDVLSVWVEKHV-KRPAHLAYRLLSDFTKRPLWDPHFLscEVID----WVSEDDQI 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854 117 YSWRCP--KPLKNRDVITL---RSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDP 191
Cdd:cd08914 126 YHITCPivNNDKPKDLVVLvsrRKPLKDGNTYVVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISA 205

                       170       180       190
                ....*....|....*....|....*....|...
gi 61556854 192 kGSLPKWVVNKSSQflaPKAMKKMYKACIKYPE 224
Cdd:cd08914 206 -SILPYFAGNLGGW---SKSIEETAASCIQFLE 234
START_2 cd08877
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 34-222 8.46e-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: 54.61  E-value: 8.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  34 RSECEAEVGWNLTYSKAGVSVWVQaVEMDRTLHKikCRMECC-DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNA 112
Cdd:cd08877  15 LKDLDESDGWTLQKESEGIRVYYK-FEPDGSLLS--LRMEGEiDGPLFNLLALLNEVELYKTWVPFCIRSKKVKQLGRAD 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854 113 DVGYYSWRCPKPLKNRDVItLRSWlpmGADYI-------IMNYSVKHPKYPPRKDL----------VRAVSIQTGYLIQS 175
Cdd:cd08877  92 KVCYLRVDLPWPLSNREAV-FRGF---GVDRLeengqivILLKSIDDDPEFLKLTDldipstsakgVRRIIKYYGFVITP 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 61556854 176 TGPKSCVITYLAQVDPKGSL-PKWVVNkssqFLAPKAMKKMYKACIKY 222
Cdd:cd08877 168 ISPTKCYLRFVANVDPKMSLvPKSLLN----FVARKFAGLLFEKIQKA 211
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 78-198 6.01e-08

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: 51.85  E-value: 6.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  78 PAETLYDVLHDieyRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSW---LPMGAdYIIMNYSVKHPK 154
Cdd:cd08907  64 PSVVLQRVLRE---RHLWDEDLLHSQVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWrsdLPRGG-CLLVSQSVDHDN 139

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 61556854 155 YPPRKDlVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKW 198
Cdd:cd08907 140 PQLEAG-VRAVLLTSQYLIEPCGMGRSRLTHICRADLRGRSPDW 182
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 67-203 3.99e-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: 49.47  E-value: 3.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  67 KIKCRMECcdvPAETLY-DVLHDIEYRKKWDSNVIETFDIARLTVNADVGY--YSWRCPKPLKNRDVITLRSWLPMGADY 143
Cdd:cd08906  52 ILKAFMQC---PAELVYqEVILQPEKMVLWNKTVSACQVLQRVDDNTLVSYdvAAGAAGGVVSPRDFVNVRRIERRRDRY 128

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 61556854 144 IIMNYSVKHPKYPPRKDLVRAVSIQTGYLI--QSTGPKSCVITYLAQVDPKGSLPKWVVNKS 203
Cdd:cd08906 129 VSAGISTTHSHKPPLSKYVRGENGPGGFVVlkSASNPSVCTFIWILNTDLKGRLPRYLIHQS 190
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 77-222 7.63e-07

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: 49.13  E-value: 7.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  77 VPAETLYDVLHDIEYRKKWDSNVIETFDIARltVNADVGYYSWRCP-----KPlknRDVITL---RSWLPMGADYIIMNY 148
Cdd:cd08873  87 TCASDAFDLLSDPFKRPEWDPHGRSCEEVKR--VGEDDGIYHTTMPsltseKP---NDFVLLvsrRKPATDGDPYKVAFR 161

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61556854 149 SVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKgslpkwVVNKSSQFLA--PKAMKKMYKACIKY 222
Cdd:cd08873 162 SVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPK------LLSYVTCNLAglSALYCRTFHCCEQF 231
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 39-222 1.04e-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: 42.93  E-value: 1.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  39 AEVGWNLTYSKAGVSVWVqaVEMDRTLhKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVIETFDIARltVNADVGYYS 118
Cdd:cd08913  57 AKDNWVLSSEKNQVRLYT--LEEDKFL-SFKVEMVV-HVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQ--VDEDDAIYH 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854 119 WRCP---KPLKNRDVITLRSWLP---MGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPk 192
Cdd:cd08913 131 VTSPslsGHGKPQDFVILASRRKpcdNGDPYVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATP- 209

                       170       180       190
                ....*....|....*....|....*....|...
gi 61556854 193 GSLP---KWVVNKSSQFlapkamKKMYKACIKY 222
Cdd:cd08913 210 GVLPyisTDIAGLSSEF------YSTFSACSQF 236
START_STARD11-like cd08872
Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily ...
 143-221 2.44e-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: 41.56  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854 143 YIIMNYSVKHPKYPPRKDLVRA---VSI--QTgyLIQSTGPK--------SCVITYLAQVDPKGSLPKWVVNKSSQFLAP 209
Cdd:cd08872 137 WIVCNFSVDHDSAPLNNKCVRAkltVAMicQT--FVSPPDGNqeitrdniLCKITYVANVNPGGWAPASVLRAVYKREYP 214

                        90
                ....*....|..
gi 61556854 210 KAMKKMYKACIK 221
Cdd:cd08872 215 KFLKRFTSYVQE 226
DUF3074 pfam11274
Protein of unknown function (DUF3074); This eukaryotic family of proteins has no known ...
 122-203 2.50e-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: 41.09  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854   122 PKPLKNRDVITL---------RSWLPMGADYIIMNYSVK-HPKYPPRKDLVRA--VSIQTGYLI----QSTGPKSCV--- 182
Cdd:pfam11274  67 PGPLTPRDFVVLlltadlppeESPGSEHAEFMVVSIPVDdHPDAPPRKGFVRGqyESVERIREIpvddEYDEETGPVewi 146

                          90       100
                  ....*....|....*....|..
gi 61556854   183 -ITylaQVDPKGSLPKWVVNKS 203
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 ...
 42-202 4.36e-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: 4.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  42 GWNLTYSKAGVSVWVQA-VEMDRTLHKIKCRMeccDVPAETLYDVLHDIE--YRKKWDSNVIETFDIARLTVNADVGYYS 118
Cdd:cd08867  23 GWKVLKTVKNITVSWKPsTEFTGHLYRAEGIV---DALPEKVIDVIIPPCggLRLKWDKSLKHYEVLEKISEDLCVGRTI 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854 119 wrCPKPLKN----RDVITLrSWLPMGADYIIMN--YSVKHPKYPPRKDLVRAVSIQTGYLIQST--GPKSCVITYLAQVD 190
Cdd:cd08867 100 --TPSAAMGlispRDFVDL-VYVKRYEDNQWSSsgKSVDIPERPPTPGFVRGYNHPCGYFCSPLkgSPDKSFLVLYVQTD 176

                       170
                ....*....|..
gi 61556854 191 PKGSLPKWVVNK 202
Cdd:cd08867 177 LRGMIPQSLVES 188
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 76-202 2.77e-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: 2.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  76 DVPAETLYDVLHD-IEYRKKWDSNVIETFDIARLTVNADVGYYSwrCPKPLKN----RDVITLRSWLPMGADYIIMNYSV 150
Cdd:cd08905  58 DQPLDNLYSELVDrMEQMGEWNPNVKEVKILQRIGKDTLITHEV--AAETAGNvvgpRDFVSVRCAKRRGSTCVLAGMAT 135

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 61556854 151 KHPKYPPRKDLVRAVSIQTGYLIQSTG--PKSCVITYLAQVDPKGSLPKWVVNK 202
Cdd:cd08905 136 HFGLMPEQKGFIRAENGPTCIVLRPLAgdPSKTKLTWLLSIDLKGWLPKSIINQ 189
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 29-203 8.02e-03

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: 36.81  E-value: 8.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854  29 DFRSFRSECEAEV--------GWNLTYSKAGVSV-WVQAVEMDRTLHKIKCRMEccDVPAEtLYDVLHDIEYRKKWDSNV 99
Cdd:cd08904   2 DFKKIAQETSQEVlgysrdtsGWKVVKTSKKITVsWKPSRKYHGNLYRVEGIIP--ESPAK-LIQFMYQPEHRIKWDKSL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556854 100 ----------IETFDIARLTVNADVGYYSwrcpkPLKNRDVITLRSWlpMGADYIIMNYSVKHPKYPPRKDLVRAVSIQT 169
Cdd:cd08904  79 qvykmlqridSDTFICHTITQSFAMGSIS-----PRDFVDLVHIKRY--EGNMNIVSSVSVEYPQCPPSSNYIRGYNHPC 151

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 61556854 170 GYLIQ--STGPKSCVITYLAQVDPKGSLPKWVVNKS 203
Cdd:cd08904 152 GYVCSplPENPAYSKLVMFVQPELRGNLSRSVIEKT 187
 
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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