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Conserved domains on  [gi|392886864|ref|NP_001251251|]
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START domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START pfam01852
START domain;
34-237 3.51e-63

START domain;


:

Pssm-ID: 426476  Cd Length: 205  Bit Score: 196.08  E-value: 3.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864   34 EVFAEVEAIFNDENYLSHAGWFKDESNNEGDVVYAKDTP-HGRMVTISTELPMPVEDVMKETWNGMEALPEWNQNINFAA 112
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPdHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  113 RIAAPTSNFDIVTYGNNDVL--VVSGREFVSARIWRKVGDG-FILASRSVTVPSFKSkHKGKVRAHLHLAGARFRPNPEN 189
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWRRLGGGvYVIVDRSVTHPQFPP-SSGYVRAERLPSGYLIQPCGNG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392886864  190 PetTLTDVVMLADLKGYLPKMIVNQVIGRIMIMDTVTNRRHFQNLKAK 237
Cdd:pfam01852 160 P--SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
 
Name Accession Description Interval E-value
START pfam01852
START domain;
34-237 3.51e-63

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 196.08  E-value: 3.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864   34 EVFAEVEAIFNDENYLSHAGWFKDESNNEGDVVYAKDTP-HGRMVTISTELPMPVEDVMKETWNGMEALPEWNQNINFAA 112
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPdHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  113 RIAAPTSNFDIVTYGNNDVL--VVSGREFVSARIWRKVGDG-FILASRSVTVPSFKSkHKGKVRAHLHLAGARFRPNPEN 189
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWRRLGGGvYVIVDRSVTHPQFPP-SSGYVRAERLPSGYLIQPCGNG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392886864  190 PetTLTDVVMLADLKGYLPKMIVNQVIGRIMIMDTVTNRRHFQNLKAK 237
Cdd:pfam01852 160 P--SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 35-237 3.82e-57

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 180.71  E-value: 3.82e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864    35 VFAEVEAIFNDENYLSHAGWFKDESNNEGDVVYAKDTP---HGRMVTISTELPMPVEDVMKETWNGMEALPEWNQNINFA 111
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPgrkPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864   112 ARIAAPTSNFDIVTYGNNDVL-VVSGREFVSARIWRKVGDG-FILASRSVTVPSFKSkHKGKVRAHLHLAGARFRPNPEN 189
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSPP-ESGYVRAENLPSGLLIEPLGNG 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 392886864   190 PetTLTDVVMLADLKGYLPKMIVNQVIGRIMIMDTVTNRRHFQNLKAK 237
Cdd:smart00234 160 P--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 49-231 4.95e-27

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: 103.20  E-value: 4.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  49 LSHAGWFKDESNNEGDVVYAKDTP-HGRMVTISTELPMPVEDVMKETWNGMEALPEWNQNINFAARIAAPTSNFDIvTY- 126
Cdd:cd08868   21 LTDPGWKLEKNTTWGDVVYSRNVPgVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNPTVLECKIIQVIDDNTDI-SYq 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864 127 -----GNNdvlVVSGREFVSARIWRKVGDGFILASRSVTVPSFKSkHKGKVRAHLHLAGARFRPNPENPETTLTDVVMLA 201
Cdd:cd08868  100 vaaeaGGG---LVSPRDFVSLRHWGIRENCYLSSGVSVEHPAMPP-TKNYVRGENGPGCWILRPLPNNPNKCNFTWLLNT 175

                        170       180       190
                 ....*....|....*....|....*....|
gi 392886864 202 DLKGYLPKMIVNQVIGRIMiMDTVTNRRHF 231
Cdd:cd08868  176 DLKGWLPQYLVDQALASVL-LDFMKHLRKR 204
 
Name Accession Description Interval E-value
START pfam01852
START domain;
34-237 3.51e-63

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 196.08  E-value: 3.51e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864   34 EVFAEVEAIFNDENYLSHAGWFKDESNNEGDVVYAKDTP-HGRMVTISTELPMPVEDVMKETWNGMEALPEWNQNINFAA 112
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPdHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  113 RIAAPTSNFDIVTYGNNDVL--VVSGREFVSARIWRKVGDG-FILASRSVTVPSFKSkHKGKVRAHLHLAGARFRPNPEN 189
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWRRLGGGvYVIVDRSVTHPQFPP-SSGYVRAERLPSGYLIQPCGNG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 392886864  190 PetTLTDVVMLADLKGYLPKMIVNQVIGRIMIMDTVTNRRHFQNLKAK 237
Cdd:pfam01852 160 P--SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 35-237 3.82e-57

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 180.71  E-value: 3.82e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864    35 VFAEVEAIFNDENYLSHAGWFKDESNNEGDVVYAKDTP---HGRMVTISTELPMPVEDVMKETWNGMEALPEWNQNINFA 111
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPgrkPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864   112 ARIAAPTSNFDIVTYGNNDVL-VVSGREFVSARIWRKVGDG-FILASRSVTVPSFKSkHKGKVRAHLHLAGARFRPNPEN 189
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWREDEDGsYAVVDVSVTHPTSPP-ESGYVRAENLPSGLLIEPLGNG 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 392886864   190 PetTLTDVVMLADLKGYLPKMIVNQVIGRIMIMDTVTNRRHFQNLKAK 237
Cdd:smart00234 160 P--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 49-231 4.95e-27

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: 103.20  E-value: 4.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  49 LSHAGWFKDESNNEGDVVYAKDTP-HGRMVTISTELPMPVEDVMKETWNGMEALPEWNQNINFAARIAAPTSNFDIvTY- 126
Cdd:cd08868   21 LTDPGWKLEKNTTWGDVVYSRNVPgVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNPTVLECKIIQVIDDNTDI-SYq 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864 127 -----GNNdvlVVSGREFVSARIWRKVGDGFILASRSVTVPSFKSkHKGKVRAHLHLAGARFRPNPENPETTLTDVVMLA 201
Cdd:cd08868  100 vaaeaGGG---LVSPRDFVSLRHWGIRENCYLSSGVSVEHPAMPP-TKNYVRGENGPGCWILRPLPNNPNKCNFTWLLNT 175

                        170       180       190
                 ....*....|....*....|....*....|
gi 392886864 202 DLKGYLPKMIVNQVIGRIMiMDTVTNRRHF 231
Cdd:cd08868  176 DLKGWLPQYLVDQALASVL-LDFMKHLRKR 204
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 34-216 1.25e-25

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: 98.95  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  34 EVFAEVEAIFNDENylshaGWfKDESNNEGDVVYAKDTP--HGRMVTISTELPMPVEDVMKETWNgMEALPEWNQNINFA 111
Cdd:cd00177    2 EAIEELLELLEEPE-----GW-KLVKEKDGVKIYTKPYEdsGLKLLKAEGVIPASPEQVFELLMD-IDLRKKWDKNFEEF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864 112 ARIAAPTSNFDIVTYGNNDVLVVSGREFVSARIWRKVGDG-FILASRSVTVPSfKSKHKGKVRAHLHLAGARFRPnPENP 190
Cdd:cd00177   75 EVIEEIDEHTDIIYYKTKPPWPVSPRDFVYLRRRRKLDDGtYVIVSKSVDHDS-HPKEKGYVRAEIKLSGWIIEP-LDPG 152

                        170       180
                 ....*....|....*....|....*.
gi 392886864 191 ETTLTdVVMLADLKGYLPKMIVNQVI 216
Cdd:cd00177  153 KTKVT-YVLQVDPKGSIPKSLVNSAA 177
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 53-216 2.70e-15

Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD1 has a high affinity for cholesterol. It can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads.


Pssm-ID: 176914  Cd Length: 209  Bit Score: 72.18  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  53 GWFKDESNNEGDVVYAKDTPH-GRMVTISTELPMPVEDVMKETWNGMEALPEWNQNIN---FAARIAAPTsnfdIVTY-- 126
Cdd:cd08905   26 GWKTEIVAENGDKVLSKVVPDiGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNPNVKevkILQRIGKDT----LITHev 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864 127 -GNNDVLVVSGREFVSARIWRKVGDGFILASRSVTVPSFkSKHKGKVRAHLHLAGARFRPNPENP-ETTLTDVVMLaDLK 204
Cdd:cd08905  102 aAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLM-PEQKGFIRAENGPTCIVLRPLAGDPsKTKLTWLLSI-DLK 179

                        170
                 ....*....|..
gi 392886864 205 GYLPKMIVNQVI 216
Cdd:cd08905  180 GWLPKSIINQVL 191
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 45-221 2.71e-15

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: 72.20  E-value: 2.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  45 DENYLSHAGWFKDESNNEGDVVYAKDTP-HGRMVTISTELPMPVEDVMKETWNGMEALPEWNQNINfAARIAAPTSNFDI 123
Cdd:cd08906   18 EQILAQEENWKFEKNNDNGDTVYTLEVPfHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNKTVS-ACQVLQRVDDNTL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864 124 VTYgnnDVL------VVSGREFVSARIWRKVGDGFILASRSVTVPSFKSKHKgKVRAHLHLAGARFRPNPENPETTLTDV 197
Cdd:cd08906   97 VSY---DVAagaaggVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSK-YVRGENGPGGFVVLKSASNPSVCTFIW 172

                        170       180
                 ....*....|....*....|....
gi 392886864 198 VMLADLKGYLPKMIVNQVIGRIMI 221
Cdd:cd08906  173 ILNTDLKGRLPRYLIHQSLAATMF 196
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 48-225 1.85e-08

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: 53.03  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  48 YLSHAGWfKDESNNEGDVVYAKDTPHG--RMVTISTELPmpveDVMKETWNGMEALPE----WNQNINFAARIAAPTSNF 121
Cdd:cd08871   19 CDSTDGW-KLKYNKNNVKVWTKNPENSsiKMIKVSAIFP----DVPAETLYDVLHDPEyrktWDSNMIESFDICQLNPNN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864 122 DIVTYGNNDVLVVSGREFVSARIWRKVGDGFILASRSVTVPSFKSKhKGKVRAHLHLAGARFRPNPENpETTLTdVVMLA 201
Cdd:cd08871   94 DIGYYSAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPR-KGFVRAISLLTGYLIRPTGPK-GCTLT-YVTQN 170

                        170       180
                 ....*....|....*....|....*.
gi 392886864 202 DLKGYLPKMIVNQVIGRI--MIMDTV 225
Cdd:cd08871  171 DPKGSLPKWVVNKATTKLapKVMKKL 196
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 84-221 1.02e-03

Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD5, and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD5 is ubiquitously expressed, with highest levels in liver and kidney. STARD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy.


Pssm-ID: 176912  Cd Length: 208  Bit Score: 39.05  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  84 PMPVEDVMKETWNGMEAlpEWNQNINfaariaaptsNFDIVTYGNNDVLV------------VSGREFVSARIWRKVGDG 151
Cdd:cd08903   58 LEQVWDCLKPAAGGLRV--KWDQNVK----------DFEVVEAISDDVSVcrtvtpsaamkiISPRDFVDVVLVKRYEDG 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392886864 152 FILASRS-VTVPSFKSKhKGKVRAHLHLAGARFRPNPENPETTLTDVVMLADLKGYLPKMIVNQVIGRIMI 221
Cdd:cd08903  126 TISSNATnVEHPLCPPQ-AGFVRGFNHPCGCFCEPVPGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMA 195
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 75-221 2.84e-03

Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4, -5, and -6. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7a-hydroxycholesterol. STARD4 and STARD5 are ubiquitously expressed, with highest levels in liver and kidney. STRAD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.


Pssm-ID: 176876  Cd Length: 206  Bit Score: 37.83  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  75 RMVTISTELPMPVEDVMKETWNGMEAlpEWNQNINFAARIAAPTSNFDIVTYGNNDVLV--VSGREFVS-ARIWRKVGDG 151
Cdd:cd08867   49 RAEGIVDALPEKVIDVIIPPCGGLRL--KWDKSLKHYEVLEKISEDLCVGRTITPSAAMglISPRDFVDlVYVKRYEDNQ 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864 152 FILASRSVTVPSFKSKhKGKVRAHLHLAGARFRPNPENPETTLTDVVMLADLKGYLPKMIVNQVIGRIMI 221
Cdd:cd08867  127 WSSSGKSVDIPERPPT-PGFVRGYNHPCGYFCSPLKGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLV 195
START_STARD2_7-like cd08870
Lipid-binding START domain of mammalian STARD2, -7, and related proteins; This subfamily ...
 135-220 4.96e-03

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: 36.97  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864 135 SGREFVSAR-IWRKVGDGFILASRSVTVPSfkSKHKGKVRAHLHLAGARFRPNPENPETTLTDVVMLADLKGYLPKMIVN 213
Cdd:cd08870  111 SDREYVIARrLWESDDRSYVCVTKGVPYPS--VPRSGRKRVDDYESSLVIRAVKGDGQGSACEVTYFHNPDGGIPRELAK 188


                 ....*..
gi 392886864 214 QVIGRIM 220
Cdd:cd08870  189 LAVKRGM 195
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 52-215 6.63e-03

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: 36.48  E-value: 6.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864  52 AGWfKDESNNEGDVVYAKDTPHGRMVTIS--TELPMPVEDVMkETWNGMEALPEWNQNINfAARIAAPTSNFDIVTYGNN 129
Cdd:cd08876   17 GDW-QLVKDKDGIKVYTRDVEGSPLKEFKavAEVDASIEAFL-ALLRDTESYPQWMPNCK-ESRVLKRTDDNERSVYTVI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886864 130 DVLV-VSGREFVS-ARIWRKVGDGfILASRSVTVPSFKSKHKGKVRahLHLAGARFRPNPENPETTLTDVVMLADLKGYL 207
Cdd:cd08876   94 DLPWpVKDRDMVLrSTTEQDADDG-SVTITLEAAPEALPEQKGYVR--IKTVEGQWTFTPLGNGKTRVTYQAYADPGGSI 170


                 ....*...
gi 392886864 208 PKMIVNQV 215
Cdd:cd08876  171 PGWLANAF 178
 
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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