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Conserved domains on  [gi|7766869|pdb|1EM2|A]
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Chain A, MLN64 PROTEIN

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 18-226 8.05e-142

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: 395.00  E-value: 8.05e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       18 AQEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPER*VLWNK 97
Cdd:cd08906   1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       98 TVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLK 177
Cdd:cd08906  81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1EM2_A      178 SASNPRVCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQRISEL 226
Cdd:cd08906 161 SASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIRDL 209
 
Name Accession Description Interval E-value
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 18-226 8.05e-142

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: 395.00  E-value: 8.05e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       18 AQEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPER*VLWNK 97
Cdd:cd08906   1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       98 TVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLK 177
Cdd:cd08906  81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1EM2_A      178 SASNPRVCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQRISEL 226
Cdd:cd08906 161 SASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIRDL 209
START pfam01852
START domain;
24-229 1.77e-59

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 186.07  E-value: 1.77e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A         24 IRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPER*VLWNKTVTACQ 103
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A        104 ILQRVEDNTLISYDVSAGAAGGVVSPRDFVNV-RRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLKSASNP 182
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLrYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
1EM2_A        183 rvCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQRISELGAR 229
Cdd:pfam01852 161 --SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 25-229 1.13e-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: 166.07  E-value: 1.13e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A          25 RQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVP--FHGKTFILKTFLPCPAELVYQEVILQPER*VLWNKTVTAC 102
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPgrKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A         103 QILQRVEDNTLISYDVSAGAAgGVVSPRDFVNV-RRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLKSASN 181
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAA-GPVSPRDFVFVrYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNG 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
1EM2_A         182 PrvCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQRISELGAR 229
Cdd:smart00234 160 P--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
 
Name Accession Description Interval E-value
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 18-226 8.05e-142

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: 395.00  E-value: 8.05e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       18 AQEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPER*VLWNK 97
Cdd:cd08906   1 PQEREYVRQGKEALAVVEQILAQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       98 TVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLK 177
Cdd:cd08906  81 TVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPLSKYVRGENGPGGFVVLK 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1EM2_A      178 SASNPRVCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQRISEL 226
Cdd:cd08906 161 SASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIRDL 209
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 18-226 5.97e-108

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: 309.29  E-value: 5.97e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       18 AQEREYIRQGKEATAVVDQILAQEeNWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPER*VLWNK 97
Cdd:cd08868   1 SQELEYLKQGAEALARAWSILTDP-GWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       98 TVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLK 177
Cdd:cd08868  80 TVLECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRP 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1EM2_A      178 SASNPRVCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQRISEL 226
Cdd:cd08868 160 LPNNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIATL 208
START pfam01852
START domain;
24-229 1.77e-59

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 186.07  E-value: 1.77e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A         24 IRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPER*VLWNKTVTACQ 103
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A        104 ILQRVEDNTLISYDVSAGAAGGVVSPRDFVNV-RRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLKSASNP 182
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLrYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
1EM2_A        183 rvCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQRISELGAR 229
Cdd:pfam01852 161 --SKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 19-226 4.10e-53

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: 170.02  E-value: 4.10e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       19 QEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPER*VLWNKT 98
Cdd:cd08905   2 AEMSYIKQGEEALQKSLSILQDQEGWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNPN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       99 VTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLKS 178
Cdd:cd08905  82 VKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRPL 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
1EM2_A      179 ASNPRVCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQRISEL 226
Cdd:cd08905 162 AGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQRMASS 209
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 25-229 1.13e-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: 166.07  E-value: 1.13e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A          25 RQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVP--FHGKTFILKTFLPCPAELVYQEVILQPER*VLWNKTVTAC 102
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSPgrKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A         103 QILQRVEDNTLISYDVSAGAAgGVVSPRDFVNV-RRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLKSASN 181
Cdd:smart00234  81 ETLEVIDNGTVIYHYVSKFAA-GPVSPRDFVFVrYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNG 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
1EM2_A         182 PrvCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQRISELGAR 229
Cdd:smart00234 160 P--SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQKHCAK 205
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 28-221 4.58e-30

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: 110.12  E-value: 4.58e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       28 KEATAVVDQILAQEENWKFEKNNEyGDTVYTIEVPFHGKTFI-LKTFLPCPAELVYqEVILQPER*VLWNKTVTACQILQ 106
Cdd:cd00177   1 EEAIEELLELLEEPEGWKLVKEKD-GVKIYTKPYEDSGLKLLkAEGVIPASPEQVF-ELLMDIDLRKKWDKNFEEFEVIE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A      107 RVEDNTLISYdvSAGAAGGVVSPRDFVNVRRIERRRD-RYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLKsaSNPRVC 185
Cdd:cd00177  79 EIDEHTDIIY--YKTKPPWPVSPRDFVYLRRRRKLDDgTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEP--LDPGKT 154

                       170       180       190
                ....*....|....*....|....*....|....*.
1EM2_A      186 TFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQ 221
Cdd:cd00177 155 KVTYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLRK 190
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 41-223 1.12e-22

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: 91.37  E-value: 1.12e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       41 EENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYqEVILQP---ER*VLWNKTVTACQILQRVEDNTLISYD 117
Cdd:cd08867  21 TDGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVI-DVIIPPcggLR-LKWDKSLKHYEVLEKISEDLCVGRT 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A      118 VSAGAAGGVVSPRDFVN-VRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLKSASNPRVCTFVWILNTDLK 196
Cdd:cd08867  99 ITPSAAMGLISPRDFVDlVYVKRYEDNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPLKGSPDKSFLVLYVQTDLR 178

                       170       180
                ....*....|....*....|....*..
1EM2_A      197 GRLPRYLIHQSLAAT*FEFAFHLRQRI 223
Cdd:cd08867 179 GMIPQSLVESAMPSNLVNFYTDLVKGV 205
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 28-223 5.46e-18

Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD6 and related domains. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.


Pssm-ID: 176913  Cd Length: 204  Bit Score: 78.80  E-value: 5.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       28 KEATAVVDQILAQEEN---WKFEKNNEYGDTVYTIEVPFHGKTFILKTFLP-CPAELVyqEVILQPER*VLWNKTVTACQ 103
Cdd:cd08904   5 KIAQETSQEVLGYSRDtsgWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPeSPAKLI--QFMYQPEHRIKWDKSLQVYK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A      104 ILQRVEDNTLISYDVSAGAAGGVVSPRDFVN-VRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGG*IVLKSASNP 182
Cdd:cd08904  83 MLQRIDSDTFICHTITQSFAMGSISPRDFVDlVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPENP 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
1EM2_A      183 RVCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQRI 223
Cdd:cd08904 163 AYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGI 203
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 30-226 1.03e-13

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: 67.55  E-value: 1.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       30 ATAVVDQILA---QEENWKF-EKNNEYgdTVY-TIEVPFHGKTFILKTFLPCPAELVYQevILQPER*VL---WNKTVTA 101
Cdd:cd08903   7 AESVADKMLLyrrDESGWKTcRRTNEV--AVSwRPSAEFAGNLYKGEGIVYATLEQVWD--CLKPAAGGLrvkWDQNVKD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A      102 CQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGiAT--SHSAKPPTHKYVRGENGPGG*IVLKSA 179
Cdd:cd08903  83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSN-ATnvEHPLCPPQAGFVRGFNHPCGCFCEPVP 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
1EM2_A      180 SNPRVCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQRISEL 226
Cdd:cd08903 162 GEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKAL 208
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 95-221 1.99e-10

Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4 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. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7alpha-hydroxycholesterol. STARD4 is ubiquitously expressed, with highest levels in liver and kidney.


Pssm-ID: 176911  Cd Length: 202  Bit Score: 58.43  E-value: 1.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       95 WNKTVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPthKYVRGENGPGG*I 174
Cdd:cd08902  75 WDSLMTSMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARP--NFVRGFNHPCGWF 152

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1EM2_A      175 VLKSASNPRVCTFVWILNTDLKGRLPRYLIHQSLAAT*FEFAFHLRQ 221
Cdd:cd08902 153 CVPLKDNPSHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKK 199
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 40-204 7.21e-04

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: 39.55  E-value: 7.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A       40 QEENWKfEKNNEYGDTVYTIEVPfhGKTF-ILKTFLPC---PAELVYqEVILQPER*VLWNKTVTAC-QILQRVEDNTLI 114
Cdd:cd08871  21 STDGWK-LKYNKNNVKVWTKNPE--NSSIkMIKVSAIFpdvPAETLY-DVLHDPEYRKTWDSNMIESfDICQLNPNNDIG 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EM2_A      115 SYDVSAGAAggvVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGengpgg*IVLKS-----ASNPRVCTFVW 189
Cdd:cd08871  97 YYSAKCPKP---LKNRDFVNLRSWLEFGGEYIIFNHSVKHKKYPPRKGFVRA-------ISLLTgylirPTGPKGCTLTY 166

                       170
                ....*....|....*
1EM2_A      190 ILNTDLKGRLPRYLI 204
Cdd:cd08871 167 VTQNDPKGSLPKWVV 181
 
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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