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Conserved domains on  [gi|149068741|gb|EDM18293|]
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START domain containing 10, isoform CRA_d [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 ...
 19-193 8.82e-108

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: 308.42  E-value: 8.82e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  19 RESVQVPDDQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSN 98
Cdd:cd08871    1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPE-NSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  99 VIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGP 178
Cdd:cd08871   80 MIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGP 159

                        170
                 ....*....|....*
gi 149068741 179 KSCVITYLAQVDPKG 193
Cdd:cd08871  160 KGCTLTYVTQNDPKG 174
 
Name Accession Description Interval E-value
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 19-193 8.82e-108

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: 308.42  E-value: 8.82e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  19 RESVQVPDDQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSN 98
Cdd:cd08871    1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPE-NSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  99 VIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGP 178
Cdd:cd08871   80 MIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGP 159

                        170
                 ....*....|....*
gi 149068741 179 KSCVITYLAQVDPKG 193
Cdd:cd08871  160 KGCTLTYVTQNDPKG 174
START pfam01852
START domain;
76-194 1.88e-19

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 82.07  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741   76 DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYS----WrcPKPLKNRDVITLRSWLPMGAD-YIIMNYSV 150
Cdd:pfam01852  53 MVAALLVAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVaalvA--PSPLSPRDFVFLRYWRRLGGGvYVIVDRSV 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 149068741  151 KHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGH 194
Cdd:pfam01852 131 THPQFPPSSGYVRAERLPSGYLIQPCGNGPSKVTWVSHADLKGW 174
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 37-194 6.96e-17

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 75.16  E-value: 6.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741    37 CEAEVGWNLTYSKAGVSVWVQAVEMDRTLHKIkcrMECC----DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNA 112
Cdd:smart00234  14 AASEEGWVLSSENENGDEVRSIFSPGRKPGEA---FRLVgvvpMVCADLVEELMDDLEYRPEWDKNVAKAETLEVIDNGT 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741   113 DVGYYSWRCP-KPLKNRDVITLRSWLPMGAD-YIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVD 190
Cdd:smart00234  91 VIYHYVSKFAaGPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGPSKVTWVSHAD 170


                   ....
gi 149068741   191 PKGH 194
Cdd:smart00234 171 LKGW 174
 
Name Accession Description Interval E-value
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 19-193 8.82e-108

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: 308.42  E-value: 8.82e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  19 RESVQVPDDQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSN 98
Cdd:cd08871    1 GGEVRLPTDADFEEFKKLCDSTDGWKLKYNKNNVKVWTKNPE-NSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  99 VIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGP 178
Cdd:cd08871   80 MIESFDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGP 159

                        170
                 ....*....|....*
gi 149068741 179 KSCVITYLAQVDPKG 193
Cdd:cd08871  160 KGCTLTYVTQNDPKG 174
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 27-193 2.84e-43

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: 143.63  E-value: 2.84e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  27 DQDFRSFRSECEAEVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVIETFDIA 106
Cdd:cd00177    1 EEAIEELLELLEEPEGWKLVKEKDGVKIYTKPYE-DSGLKLLKAEGVI-PASPEQVFELLMDIDLRKKWDKNFEEFEVIE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741 107 RLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGAD-YIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITY 185
Cdd:cd00177   79 EIDEHTDIIYYKTKPPWPVSPRDFVYLRRRRKLDDGtYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGKTKVTY 158


                 ....*...
gi 149068741 186 LAQVDPKG 193
Cdd:cd00177  159 VLQVDPKG 166
START pfam01852
START domain;
76-194 1.88e-19

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 82.07  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741   76 DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYS----WrcPKPLKNRDVITLRSWLPMGAD-YIIMNYSV 150
Cdd:pfam01852  53 MVAALLVAELLKDMEYRAQWDKDVRSAETLEVISSGGDLQYYVaalvA--PSPLSPRDFVFLRYWRRLGGGvYVIVDRSV 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 149068741  151 KHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGH 194
Cdd:pfam01852 131 THPQFPPSSGYVRAERLPSGYLIQPCGNGPSKVTWVSHADLKGW 174
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 37-194 6.96e-17

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 75.16  E-value: 6.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741    37 CEAEVGWNLTYSKAGVSVWVQAVEMDRTLHKIkcrMECC----DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNA 112
Cdd:smart00234  14 AASEEGWVLSSENENGDEVRSIFSPGRKPGEA---FRLVgvvpMVCADLVEELMDDLEYRPEWDKNVAKAETLEVIDNGT 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741   113 DVGYYSWRCP-KPLKNRDVITLRSWLPMGAD-YIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVD 190
Cdd:smart00234  91 VIYHYVSKFAaGPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGPSKVTWVSHAD 170


                   ....
gi 149068741   191 PKGH 194
Cdd:smart00234 171 LKGW 174
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 33-194 1.17e-14

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: 69.26  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  33 FRSECEAEVGWNLTYSKAGVSVWVQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDieyRKKWDSNVIETFDIARLTVNA 112
Cdd:cd08869   11 LREARDKSKGWVSVSSSDHVELAFKKVDDGHPLRLWRASTEVEAPPEEVLQRILRE---RHLWDDDLLQWKVVETLDEDT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741 113 DVGYYSWRCPKPLKNRDVITLRSW---LPMGADYIIMNySVKHPK-YPPRkdLVRAVSIQTGYLIQSTGPKSCVITYLAQ 188
Cdd:cd08869   88 EVYQYVTNSMAPHPTRDYVVLRTWrtdLPKGACVLVET-SVEHTEpVPLG--GVRAVVLASRYLIEPCGSGKSRVTHICR 164


                 ....*.
gi 149068741 189 VDPKGH 194
Cdd:cd08869  165 VDLRGR 170
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 38-163 1.56e-13

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: 66.16  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  38 EAEVGWNLTYSKAGVSVWVQAvEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTV-NADVGY 116
Cdd:cd08911   18 QEPDGWEPFIEKKDMLVWRRE-HPGTGLYEYKVYGSFDDVTARDFLNVQLDLEYRKKWDATAVELEVVDEDPEtGSEIIY 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 149068741 117 YSWRCPKPLKNRDVITLRSWLpmgADY-----IIMNYSVKHPKYPPRKDLVR 163
Cdd:cd08911   97 WEMQWPKPFANRDYVYVRRYI---IDEenkliVIVSKAVQHPSYPESPKKVR 145
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 76-193 3.32e-13

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: 65.45  E-value: 3.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  76 DVPAETLYDVL-HDIEYRKKWDSNVIETFDIARLTVNADVGYyswRCPKPLKN-----RDVITLRSWLPMGADYIIMNYS 149
Cdd:cd08868   57 DCPAEFLYNELvLNVESLPSWNPTVLECKIIQVIDDNTDISY---QVAAEAGGglvspRDFVSLRHWGIRENCYLSSGVS 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 149068741 150 VKHPKYPPRKDLVRAVSIQTGYLIQSTG--PKSCVITYLAQVDPKG 193
Cdd:cd08868  134 VEHPAMPPTKNYVRGENGPGCWILRPLPnnPNKCNFTWLLNTDLKG 179
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 40-193 2.59e-10

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: 57.28  E-value: 2.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  40 EVGWNLTYSKAGVSVWVQAVEmDRTLHKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYSW 119
Cdd:cd08876   16 DGDWQLVKDKDGIKVYTRDVE-GSPLKEFKAVAEV-DASIEAFLALLRDTESYPQWMPNCKESRVLKRTDDNERSVYTVI 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149068741 120 RCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPP-RKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKG 193
Cdd:cd08876   94 DLPWPVKDRDMVLRSTTEQDADDGSVTITLEAAPEALPeQKGYVRIKTVEGQWTFTPLGNGKTRVTYQAYADPGG 168
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 33-193 1.44e-09

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: 55.58  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  33 FRSECeAEVG--------WNLTYSKAGVSVWvQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFD 104
Cdd:cd08910   10 FREAC-AELQqpaldgaaWELLVESSGISIY-RLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQYVKELYE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741 105 iaRLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADY----IIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKS 180
Cdd:cd08910   88 --KECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGrkiwVILARSTSLPQLPEKPGVIRVKQYKQSLAIESDGKKG 165

                        170
                 ....*....|...
gi 149068741 181 CVITYLAQVDPKG 193
Cdd:cd08910  166 SKVFMYYFDNPGG 178
START_STARD13-like cd08909
C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also ...
 78-197 1.55e-09

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


Pssm-ID: 176918  Cd Length: 205  Bit Score: 55.31  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  78 PAETLYDVLHDieyRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSW---LPMGAdYIIMNYSVKHPK 154
Cdd:cd08909   64 PSVVLNRVLRE---RHLWDEDFLQWKVVETLDKQTEVYQYVLNCMAPHPSRDFVVLRSWrtdLPKGA-CSLVSVSVEHEE 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 149068741 155 YPPRKDlVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGHEED 197
Cdd:cd08909  140 APLLGG-VRAVVLDSQYLIEPCGSGKSRLTHICRVDLKGHSPE 181
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 39-191 1.93e-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: 55.29  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  39 AEVGWNLTysKAGVSVWVQAVEmDRTLHKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVI--ETFDiarlTVNADVGY 116
Cdd:cd08914   54 AKSGWEVT--STVEKIKIYTLE-EHDVLSVWVEKHV-KRPAHLAYRLLSDFTKRPLWDPHFLscEVID----WVSEDDQI 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741 117 YSWRCP--KPLKNRDVITL---RSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDP 191
Cdd:cd08914  126 YHITCPivNNDKPKDLVVLvsrRKPLKDGNTYVVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSNSCTVSYFNQISA 205
START_STARD12-like cd08908
C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also ...
 69-197 5.06e-09

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: 53.86  E-value: 5.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  69 KCRMECCDVPAETLYDVLHDieyRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSW---LPMGADYII 145
Cdd:cd08908   55 RTTIEVPAAPEEILKRLLKE---QHLWDVDLLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWrtnLPKGACALL 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 149068741 146 MNySVKHPKYPPRKdlVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGHEED 197
Cdd:cd08908  132 AT-SVDHDRAPVAG--VRVNVLLSRYLIEPCGSGKSKLTYMCRIDLRGHMPE 180
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 24-159 2.27e-08

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: 52.00  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  24 VPDDQDFRSF---RSECEAEVGWNLTYSKAGVSVWVQA---VEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDS 97
Cdd:cd08870    2 HVSEEDLRDLvqeLQEGAEGQAWQQVMDKSTPDMSYQAwrrKPKGTGLYEYLVRGVFEDCTPELLRDFYWDDEYRKKWDE 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149068741  98 NVIETFDIARLTVNA-DVGYYSWRCPKPLKNRD-VITLRSWLPMGADYIIMNYSVKHPKYPPRK 159
Cdd:cd08870   82 TVIEHETLEEDEKSGtEIVRWVKKFPFPLSDREyVIARRLWESDDRSYVCVTKGVPYPSVPRSG 145
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 77-192 5.83e-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: 48.36  E-value: 5.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  77 VPAETLYDVLHDIEYRKKWDSNVIETFDIARltVNADVGYYSWRCP-----KPlknRDVITL---RSWLPMGADYIIMNY 148
Cdd:cd08873   87 TCASDAFDLLSDPFKRPEWDPHGRSCEEVKR--VGEDDGIYHTTMPsltseKP---NDFVLLvsrRKPATDGDPYKVAFR 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 149068741 149 SVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPK 192
Cdd:cd08873  162 SVTLPRVPQTPGYSRTEVACAGFVIRQDCGTCTEVSYYNETNPK 205
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 78-197 1.02e-06

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: 47.22  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  78 PAETLYDVLHDieyRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSW---LPMGAdYIIMNYSVKHPK 154
Cdd:cd08907   64 PSVVLQRVLRE---RHLWDEDLLHSQVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWrsdLPRGG-CLLVSQSVDHDN 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 149068741 155 YPPRKDlVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGHEED 197
Cdd:cd08907  140 PQLEAG-VRAVLLTSQYLIEPCGMGRSRLTHICRADLRGRSPD 181
START_2 cd08877
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 34-192 2.77e-05

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: 43.44  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  34 RSECEAEVGWNLTYSKAGVSVWVQaVEMDRTLHKikCRMECC-DVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNA 112
Cdd:cd08877   15 LKDLDESDGWTLQKESEGIRVYYK-FEPDGSLLS--LRMEGEiDGPLFNLLALLNEVELYKTWVPFCIRSKKVKQLGRAD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741 113 DVGYYSWRCPKPLKNRDVItLRSWlpmGADYI-------IMNYSVKHPKYPPRKDL----------VRAVSIQTGYLIQS 175
Cdd:cd08877   92 KVCYLRVDLPWPLSNREAV-FRGF---GVDRLeengqivILLKSIDDDPEFLKLTDldipstsakgVRRIIKYYGFVITP 167

                        170
                 ....*....|....*..
gi 149068741 176 TGPKSCVITYLAQVDPK 192
Cdd:cd08877  168 ISPTKCYLRFVANVDPK 184
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 39-191 1.28e-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: 41.39  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  39 AEVGWNLTYSKAGVSVWVqaVEMDRTLhKIKCRMECcDVPAETLYDVLHDIEYRKKWDSNVIETFDIARltVNADVGYYS 118
Cdd:cd08913   57 AKDNWVLSSEKNQVRLYT--LEEDKFL-SFKVEMVV-HVDAAQAFLLLSDLRRRPEWDKHYRSCELVQQ--VDEDDAIYH 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149068741 119 WRCP---KPLKNRDVITLRSWLP---MGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDP 191
Cdd:cd08913  131 VTSPslsGHGKPQDFVILASRRKpcdNGDPYVIALRSVTLPTHPPTPEYTRGETLCSGFCIWEESDQLTKVSYYNQATP 209
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 67-193 7.56e-04

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: 39.07  E-value: 7.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068741  67 KIKCRMECcdvPAETLY-DVLHDIEYRKKWDSNVIETFDIARLTVNADVGY--YSWRCPKPLKNRDVITLRSWLPMGADY 143
Cdd:cd08906   52 ILKAFMQC---PAELVYqEVILQPEKMVLWNKTVSACQVLQRVDDNTLVSYdvAAGAAGGVVSPRDFVNVRRIERRRDRY 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 149068741 144 IIMNYSVKHPKYPPRKDLVRAVSIQTGYLI--QSTGPKSCVITYLAQVDPKG 193
Cdd:cd08906  129 VSAGISTTHSHKPPLSKYVRGENGPGGFVVlkSASNPSVCTFIWILNTDLKG 180
START_STARD11-like cd08872
Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily ...
 143-193 5.39e-03

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: 36.55  E-value: 5.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149068741 143 YIIMNYSVKHPKYPPRKDLVRA---VSIQTGYLIQSTGPK--------SCVITYLAQVDPKG 193
Cdd:cd08872  137 WIVCNFSVDHDSAPLNNKCVRAkltVAMICQTFVSPPDGNqeitrdniLCKITYVANVNPGG 198
 
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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