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Conserved domains on  [gi|148683930|gb|EDL15877|]
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phosphatidylcholine transfer protein, isoform CRA_a [Mus musculus]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 1-138 1.86e-92

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


The actual alignment was detected with superfamily member cd08910:

Pssm-ID: 472699  Cd Length: 207  Bit Score: 266.28  E-value: 1.86e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930   1 MDLDYRKQWDQYVKELYEKESDEQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGRKIYVVLAQSISAPQFPEKSGVIRV 80
Cdd:cd08910   70 MDLEYRKQWDQYVKELYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRV 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148683930  81 KQYKQSLAIESDGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNY 138
Cdd:cd08910  150 KQYKQSLAIESDGKKGSKVFMYYFDNPGGMIPSWLINWAAKNGVPNFLKDMQKACQNY 207
 
Name Accession Description Interval E-value
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 1-138 1.86e-92

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: 266.28  E-value: 1.86e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930   1 MDLDYRKQWDQYVKELYEKESDEQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGRKIYVVLAQSISAPQFPEKSGVIRV 80
Cdd:cd08910   70 MDLEYRKQWDQYVKELYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRV 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148683930  81 KQYKQSLAIESDGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNY 138
Cdd:cd08910  150 KQYKQSLAIESDGKKGSKVFMYYFDNPGGMIPSWLINWAAKNGVPNFLKDMQKACQNY 207
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 1-141 6.91e-36

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 122.54  E-value: 6.91e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930     1 MDLDYRKQWDQYVK--ELYEKESDEQMVAYWEVKYPF-PLSNRDYVYTRQRRdldVDGRKIYVVLAQSISAPQFPEKSGV 77
Cdd:smart00234  65 DDLEYRPEWDKNVAkaETLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWR---EDEDGSYAVVDVSVTHPTSPPESGY 141

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148683930    78 IRVKQYKQSLAIESDGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNYHKK 141
Cdd:smart00234 142 VRAENLPSGLLIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
START pfam01852
START domain;
1-141 3.62e-35

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 120.59  E-value: 3.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930    1 MDLDYRKQWDQYVK--ELYEKESDEQMVAYWEVKYPF--PLSNRDYVYTRQRRdldVDGRKIYVVLAQSISAPQFPEKSG 76
Cdd:pfam01852  64 KDMEYRAQWDKDVRsaETLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWR---RLGGGVYVIVDRSVTHPQFPPSSG 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148683930   77 VIRVKQYKQSLAIESDGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNYHKK 141
Cdd:pfam01852 141 YVRAERLPSGYLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
 
Name Accession Description Interval E-value
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 1-138 1.86e-92

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: 266.28  E-value: 1.86e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930   1 MDLDYRKQWDQYVKELYEKESDEQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGRKIYVVLAQSISAPQFPEKSGVIRV 80
Cdd:cd08910   70 MDLEYRKQWDQYVKELYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRV 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148683930  81 KQYKQSLAIESDGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNY 138
Cdd:cd08910  150 KQYKQSLAIESDGKKGSKVFMYYFDNPGGMIPSWLINWAAKNGVPNFLKDMQKACQNY 207
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 1-138 3.64e-48

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: 154.07  E-value: 3.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930   1 MDLDYRKQWDQYVKELYEKESDEQ---MVAYWEVKYPFPLSNRDYVYTRQRRDLDvdgRKIYVVLAQSISAPQFPEkSGV 77
Cdd:cd08870   71 WDDEYRKKWDETVIEHETLEEDEKsgtEIVRWVKKFPFPLSDREYVIARRLWESD---DRSYVCVTKGVPYPSVPR-SGR 146

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148683930  78 IRVKQYKQSLAIES--DGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNY 138
Cdd:cd08870  147 KRVDDYESSLVIRAvkGDGQGSACEVTYFHNPDGGIPRELAKLAVKRGMPGFLKKLENALRKY 209
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 1-141 6.91e-36

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 122.54  E-value: 6.91e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930     1 MDLDYRKQWDQYVK--ELYEKESDEQMVAYWEVKYPF-PLSNRDYVYTRQRRdldVDGRKIYVVLAQSISAPQFPEKSGV 77
Cdd:smart00234  65 DDLEYRPEWDKNVAkaETLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWR---EDEDGSYAVVDVSVTHPTSPPESGY 141

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148683930    78 IRVKQYKQSLAIESDGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNYHKK 141
Cdd:smart00234 142 VRAENLPSGLLIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
START pfam01852
START domain;
1-141 3.62e-35

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 120.59  E-value: 3.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930    1 MDLDYRKQWDQYVK--ELYEKESDEQMVAYWEVKYPF--PLSNRDYVYTRQRRdldVDGRKIYVVLAQSISAPQFPEKSG 76
Cdd:pfam01852  64 KDMEYRAQWDKDVRsaETLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWR---RLGGGVYVIVDRSVTHPQFPPSSG 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148683930   77 VIRVKQYKQSLAIESDGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNYHKK 141
Cdd:pfam01852 141 YVRAERLPSGYLIQPCGNGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 1-138 7.72e-32

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: 112.00  E-value: 7.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930   1 MDLDYRKQWDQYVKEL----YEKESDEQMVaYWEVKYPFPLSNRDYVYTRqRRDLDVDgRKIYVVLAQSISAPQFPEKSG 76
Cdd:cd08911   66 LDLEYRKKWDATAVELevvdEDPETGSEII-YWEMQWPKPFANRDYVYVR-RYIIDEE-NKLIVIVSKAVQHPSYPESPK 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148683930  77 VIRVKQYKQSLAIE---SDGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNY 138
Cdd:cd08911  143 KVRVEDYWSYMVIRphkSFDEPGFEFVLTYFDNPGVNIPSYITSWVAMSGMPDFLERLRNAALKY 207
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 1-136 2.10e-27

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: 100.49  E-value: 2.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930   1 MDLDYRKQWDQYVKELY--EKESDEQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGrkiYVVLAQSISAPQFPEKSGVI 78
Cdd:cd00177   59 MDIDLRKKWDKNFEEFEviEEIDEHTDIIYYKTKPPWPVSPRDFVYLRRRRKLDDGT---YVIVSKSVDHDSHPKEKGYV 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148683930  79 RVKQYKQSLAIESDGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQ 136
Cdd:cd00177  136 RAEIKLSGWIIEPLDPGKTKVTYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLRKAKK 193
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 1-138 1.83e-23

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: 90.78  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930   1 MDLDYRKQWDQYVKELYE--KESDEQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDgrkiYVVLAQSISAPQFPEKSGVI 78
Cdd:cd08871   68 HDPEYRKTWDSNMIESFDicQLNPNNDIGYYSAKCPKPLKNRDFVNLRSWLEFGGE----YIIFNHSVKHKKYPPRKGFV 143

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148683930  79 RVKQYKQSLAIESDGKKGSrvFMYYF--DNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNY 138
Cdd:cd08871  144 RAISLLTGYLIRPTGPKGC--TLTYVtqNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKY 203
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 8-136 1.55e-14

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: 66.91  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930   8 QWDQYVKE--LYEKESDEQMVAYWEVKYPFPLSNRDYV-YTRQRRDLDVDGRKIyvvlaQSISAPQ-FPEKSGVIRVKQY 83
Cdd:cd08876   68 QWMPNCKEsrVLKRTDDNERSVYTVIDLPWPVKDRDMVlRSTTEQDADDGSVTI-----TLEAAPEaLPEQKGYVRIKTV 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148683930  84 KQSLAIESDGKKGSRV-FMYYFDnPGGQIPSWLINWAAKNGVPNFLKDMVKACQ 136
Cdd:cd08876  143 EGQWTFTPLGNGKTRVtYQAYAD-PGGSIPGWLANAFAKDAPYNTLENLRKQLK 195
START_2 cd08877
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 24-137 1.65e-04

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


Pssm-ID: 176886  Cd Length: 215  Bit Score: 39.98  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930  24 QMVAYWEVKYPFPLSNRD-YVYTRQRRDLDVDGRkiYVVLAQSIS-APQFPEKSGvirvkqykqsLAIESDGKKGSRVFM 101
Cdd:cd08877   91 DKVCYLRVDLPWPLSNREaVFRGFGVDRLEENGQ--IVILLKSIDdDPEFLKLTD----------LDIPSTSAKGVRRII 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 148683930 102 YYFD------NPGGQ--------------IPSWLINWAAKNGVPNFLKDMVKACQN 137
Cdd:cd08877  159 KYYGfvitpiSPTKCylrfvanvdpkmslVPKSLLNFVARKFAGLLFEKIQKAAKN 214
START_STARD11-like cd08872
Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily ...
 2-137 8.99e-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: 37.71  E-value: 8.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683930   2 DLDYRKQWDQYVK--ELYEKESDEQMVAYWEVKYPFPLSNRDYVY----TRQRRDLDVDGRKIYVVLAQSISAPQFPEKS 75
Cdd:cd08872   74 DPDVRMDWETTLEnfHVVETLSQDTLIFHQTHKRVWPAAQRDALFvshiRKIPALEEPNAHDTWIVCNFSVDHDSAPLNN 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148683930  76 GVIRVK----QYKQSLAIESDGKK-------GSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQN 137
Cdd:cd08872  154 KCVRAKltvaMICQTFVSPPDGNQeitrdniLCKITYVANVNPGGWAPASVLRAVYKREYPKFLKRFTSYVQE 226
 
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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