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Conserved domains on  [gi|117320552|ref|NP_032822|]
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phosphatidylcholine transfer protein isoform 1 [Mus musculus]

Protein Classification

phosphatidylcholine transfer protein( domain architecture ID 10172360)

phosphatidylcholine transfer protein (PCTP) catalyzes the transfer of phosphatidylcholine between membranes

Gene Symbol:  PCTP
Gene Ontology:  GO:0008289|GO:0008525|GO:0015914
PubMed:  31927098|18922149

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 8-210 6.59e-138

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: 384.15  E-value: 6.59e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552   8 FSDEQFREACAELQKPALTGADWQLLVEASGITIYRLLDQPSGLYEYKVFGVLEGCSPALLADVYMDLDYRKQWDQYVKE 87
Cdd:cd08910    5 FSEEQFREACAELQQPALDGAAWELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQYVKE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  88 LYEKESDEQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGRKIYVVLAQSISAPQFPEKSGVIRVKQYKQSLAIESDGKK 167
Cdd:cd08910   85 LYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRVKQYKQSLAIESDGKK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 117320552 168 GSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNY 210
Cdd:cd08910  165 GSKVFMYYFDNPGGMIPSWLINWAAKNGVPNFLKDMQKACQNY 207
 
Name Accession Description Interval E-value
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 8-210 6.59e-138

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: 384.15  E-value: 6.59e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552   8 FSDEQFREACAELQKPALTGADWQLLVEASGITIYRLLDQPSGLYEYKVFGVLEGCSPALLADVYMDLDYRKQWDQYVKE 87
Cdd:cd08910    5 FSEEQFREACAELQQPALDGAAWELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQYVKE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  88 LYEKESDEQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGRKIYVVLAQSISAPQFPEKSGVIRVKQYKQSLAIESDGKK 167
Cdd:cd08910   85 LYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRVKQYKQSLAIESDGKK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 117320552 168 GSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNY 210
Cdd:cd08910  165 GSKVFMYYFDNPGGMIPSWLINWAAKNGVPNFLKDMQKACQNY 207
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 12-213 4.66e-51

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 164.14  E-value: 4.66e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552    12 QFREACAELQKPALTGADWQLLVEA--SGITIYRLLDQPSGLYEYKVFGVLEGCSPALLADVYMDLDYRKQWDQYVK--E 87
Cdd:smart00234   2 AEEAAAELLKMAAASEEGWVLSSENenGDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAkaE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552    88 LYEKESDEQMVAYWEVKYPF-PLSNRDYVYTRQRRdldVDGRKIYVVLAQSISAPQFPEKSGVIRVKQYKQSLAIESDGK 166
Cdd:smart00234  82 TLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWR---EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 117320552   167 KGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNYHKK 213
Cdd:smart00234 159 GPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
START pfam01852
START domain;
10-213 3.45e-48

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 156.79  E-value: 3.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552   10 DEQFREACAELQKPALTGADWQLLVEASGITIYRLLDQPSGLYEYKVFGVLEGCSPALLADVYMDLDYRKQWDQYVK--E 87
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRsaE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552   88 LYEKESDEQMVAYWEVKYPF--PLSNRDYVYTRQRRdldVDGRKIYVVLAQSISAPQFPEKSGVIRVKQYKQSLAIESDG 165
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWR---RLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 117320552  166 KKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNYHKK 213
Cdd:pfam01852 158 NGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
 
Name Accession Description Interval E-value
START_STARD2-like cd08910
Lipid-binding START domain of mammalian STARD2 and related proteins; This subgroup includes ...
 8-210 6.59e-138

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: 384.15  E-value: 6.59e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552   8 FSDEQFREACAELQKPALTGADWQLLVEASGITIYRLLDQPSGLYEYKVFGVLEGCSPALLADVYMDLDYRKQWDQYVKE 87
Cdd:cd08910    5 FSEEQFREACAELQQPALDGAAWELLVESSGISIYRLLDEQSGLYEYKVFGVLEDCSPSLLADVYMDLEYRKQWDQYVKE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  88 LYEKESDEQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGRKIYVVLAQSISAPQFPEKSGVIRVKQYKQSLAIESDGKK 167
Cdd:cd08910   85 LYEKECDGETVIYWEVKYPFPLSNRDYVYIRQRRDLDVEGRKIWVILARSTSLPQLPEKPGVIRVKQYKQSLAIESDGKK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 117320552 168 GSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNY 210
Cdd:cd08910  165 GSKVFMYYFDNPGGMIPSWLINWAAKNGVPNFLKDMQKACQNY 207
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 8-210 4.61e-74

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: 222.64  E-value: 4.61e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552   8 FSDEQFREACAELQKPALtGADWQLLVEASG----ITIYRLLDQPSGLYEYKVFGVLEGCSPALLADVYMDLDYRKQWDQ 83
Cdd:cd08870    3 VSEEDLRDLVQELQEGAE-GQAWQQVMDKSTpdmsYQAWRRKPKGTGLYEYLVRGVFEDCTPELLRDFYWDDEYRKKWDE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  84 YVKELYEKESDEQ---MVAYWEVKYPFPLSNRDYVYTRQRRDLDvdgRKIYVVLAQSISAPQFPEkSGVIRVKQYKQSLA 160
Cdd:cd08870   82 TVIEHETLEEDEKsgtEIVRWVKKFPFPLSDREYVIARRLWESD---DRSYVCVTKGVPYPSVPR-SGRKRVDDYESSLV 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 117320552 161 IES--DGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNY 210
Cdd:cd08870  158 IRAvkGDGQGSACEVTYFHNPDGGIPRELAKLAVKRGMPGFLKKLENALRKY 209
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 12-213 4.66e-51

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 164.14  E-value: 4.66e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552    12 QFREACAELQKPALTGADWQLLVEA--SGITIYRLLDQPSGLYEYKVFGVLEGCSPALLADVYMDLDYRKQWDQYVK--E 87
Cdd:smart00234   2 AEEAAAELLKMAAASEEGWVLSSENenGDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAkaE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552    88 LYEKESDEQMVAYWEVKYPF-PLSNRDYVYTRQRRdldVDGRKIYVVLAQSISAPQFPEKSGVIRVKQYKQSLAIESDGK 166
Cdd:smart00234  82 TLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWR---EDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 117320552   167 KGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNYHKK 213
Cdd:smart00234 159 GPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
START pfam01852
START domain;
10-213 3.45e-48

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 156.79  E-value: 3.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552   10 DEQFREACAELQKPALTGADWQLLVEASGITIYRLLDQPSGLYEYKVFGVLEGCSPALLADVYMDLDYRKQWDQYVK--E 87
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRsaE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552   88 LYEKESDEQMVAYWEVKYPF--PLSNRDYVYTRQRRdldVDGRKIYVVLAQSISAPQFPEKSGVIRVKQYKQSLAIESDG 165
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWR---RLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 117320552  166 KKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNYHKK 213
Cdd:pfam01852 158 NGPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START_STARD7-like cd08911
Lipid-binding START domain of mammalian STARD7 and related proteins; This subgroup includes ...
 29-210 3.19e-44

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: 146.67  E-value: 3.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  29 DWQLLVEASGITIYRLLDQPSGLYEYKVFGVLEGCSPALLADVYMDLDYRKQWDQYVKEL----YEKESDEQMVaYWEVK 104
Cdd:cd08911   22 GWEPFIEKKDMLVWRREHPGTGLYEYKVYGSFDDVTARDFLNVQLDLEYRKKWDATAVELevvdEDPETGSEII-YWEMQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552 105 YPFPLSNRDYVYTRqRRDLDVDgRKIYVVLAQSISAPQFPEKSGVIRVKQYKQSLAIE---SDGKKGSRVFMYYFDNPGG 181
Cdd:cd08911  101 WPKPFANRDYVYVR-RYIIDEE-NKLIVIVSKAVQHPSYPESPKKVRVEDYWSYMVIRphkSFDEPGFEFVLTYFDNPGV 178

                        170       180
                 ....*....|....*....|....*....
gi 117320552 182 QIPSWLINWAAKNGVPNFLKDMVKACQNY 210
Cdd:cd08911  179 NIPSYITSWVAMSGMPDFLERLRNAALKY 207
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 11-208 6.82e-41

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: 137.85  E-value: 6.82e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  11 EQFREACAElqkpaltGADWQLLVEASGITIYRLLDQPSGLYEYKVFGVLEgCSPALLADVYMDLDYRKQWDQYVKELY- 89
Cdd:cd00177    5 EELLELLEE-------PEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIP-ASPEQVFELLMDIDLRKKWDKNFEEFEv 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  90 -EKESDEQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGrkiYVVLAQSISAPQFPEKSGVIRVKQYKQSLAIESDGKKG 168
Cdd:cd00177   77 iEEIDEHTDIIYYKTKPPWPVSPRDFVYLRRRRKLDDGT---YVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPLDPGK 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 117320552 169 SRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQ 208
Cdd:cd00177  154 TKVTYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLRKAKK 193
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 11-210 3.25e-31

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: 113.51  E-value: 3.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  11 EQFREACaelqkpaLTGADWQLLVEASGITIYRLLDQPSGLYEYKVFGVLEGCSPALLADVYMDLDYRKQWDQYVKELYE 90
Cdd:cd08871   13 EEFKKLC-------DSTDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDVPAETLYDVLHDPEYRKTWDSNMIESFD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  91 KE-----SDeqmVAYWEVKYPFPLSNRDYVYTRQRRDLDVDgrkiYVVLAQSISAPQFPEKSGVIRVKQYKQSLAIESDG 165
Cdd:cd08871   86 ICqlnpnND---IGYYSAKCPKPLKNRDFVNLRSWLEFGGE----YIIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 117320552 166 KKGSrvFMYYF--DNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNY 210
Cdd:cd08871  159 PKGC--TLTYVtqNDPKGSLPKWVVNKATTKLAPKVMKKLHKAALKY 203
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 28-208 6.65e-21

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: 85.79  E-value: 6.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  28 ADWQLLVEASGITIYRLLDQPSGLYEYKVFGVLEGcSPALLADVYMDLDYRKQWDQYVKE--LYEKESDEQMVAYWEVKY 105
Cdd:cd08876   17 GDWQLVKDKDGIKVYTRDVEGSPLKEFKAVAEVDA-SIEAFLALLRDTESYPQWMPNCKEsrVLKRTDDNERSVYTVIDL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552 106 PFPLSNRDYV-YTRQRRDLDVDGRKIyvvlaQSISAPQ-FPEKSGVIRVKQYKQSLAIESDGKKGSRV-FMYYFDnPGGQ 182
Cdd:cd08876   96 PWPVKDRDMVlRSTTEQDADDGSVTI-----TLEAAPEaLPEQKGYVRIKTVEGQWTFTPLGNGKTRVtYQAYAD-PGGS 169

                        170       180
                 ....*....|....*....|....*.
gi 117320552 183 IPSWLINWAAKNGVPNFLKDMVKACQ 208
Cdd:cd08876  170 IPGWLANAFAKDAPYNTLENLRKQLK 195
START_2 cd08877
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 19-209 2.53e-07

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: 49.22  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  19 ELQKPALTGADWQLLVEASGITIYRLLDQPSGLYEYKVFGVLEGCSPALLAdVYMDLDYRKQWDQYVKELYEKESDE--Q 96
Cdd:cd08877   13 ENLKDLDESDGWTLQKESEGIRVYYKFEPDGSLLSLRMEGEIDGPLFNLLA-LLNEVELYKTWVPFCIRSKKVKQLGraD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  97 MVAYWEVKYPFPLSNRD-YVYTRQRRDLDVDGRkiYVVLAQSIS-APQFPEKSGvirvkqykqsLAIESDGKKGSRVFMY 174
Cdd:cd08877   92 KVCYLRVDLPWPLSNREaVFRGFGVDRLEENGQ--IVILLKSIDdDPEFLKLTD----------LDIPSTSAKGVRRIIK 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 117320552 175 YFD------NPGGQ--------------IPSWLINWAAKNGVPNFLKDMVKACQN 209
Cdd:cd08877  160 YYGfvitpiSPTKCylrfvanvdpkmslVPKSLLNFVARKFAGLLFEKIQKAAKN 214
START_STARD11-like cd08872
Ceramide-binding START domain of mammalian STARD11 and related domains; This subfamily ...
 30-209 2.67e-05

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: 43.48  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552  30 WQLLVEASGITIYRLLDQPSGLY--EYKVFGVLEGCSPALLADVYMDLDYRKQWDQYVK--ELYEKESDEQMVAYWEVKY 105
Cdd:cd08872   28 WQLFAEEGEMKVYRREVEEDGVVldPLKATHAVKGVTGHEVCHYFFDPDVRMDWETTLEnfHVVETLSQDTLIFHQTHKR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117320552 106 PFPLSNRDYVY----TRQRRDLDVDGRKIYVVLAQSISAPQFPEKSGVIRVK----QYKQSLAIESDGKK-------GSR 170
Cdd:cd08872  108 VWPAAQRDALFvshiRKIPALEEPNAHDTWIVCNFSVDHDSAPLNNKCVRAKltvaMICQTFVSPPDGNQeitrdniLCK 187

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 117320552 171 VFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQN 209
Cdd:cd08872  188 ITYVANVNPGGWAPASVLRAVYKREYPKFLKRFTSYVQE 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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