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Conserved domains on  [gi|1972263037|ref|NP_001379724|]
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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
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 18-182 6.32e-66

Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal membrane protein, and carries this MENTAL (MLN64N-terminal) domain at its N-terminus. The domain is composed of four trans-membrane helices with three short intervening loops. The function of the domain is to capture cholesterol and pass it to the associated START domain pfam01852 for transfer to a cytosolic acceptor protein or membrane. In mammals, the MENTAL domain is involved in the localization of MLN64 and MENTHO in late endosomes, and also in homo-and of hetero-interactions of these two proteins.


:

Pssm-ID: 463097  Cd Length: 177  Bit Score: 209.07  E-value: 6.32e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  18 SKDRKRFIVITFFDTSITILLWLLCTVTRDDDWDKVFFNEINIFNpkfIRISLFDIVLLAVLRMLILGVVYGICLVKQWY 97
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINGENIKKAFEKEVLHYN---IKTSLFDIVLLAAFRFLVLLLFYALLRLNHWW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  98 TVAFTTLASSAYILMKVLFY-FNHSSSAVPPLLLIITSFTLCWSEFYLMPFQILPRERRYARRELDGI-----ENPEFST 171
Cdd:pfam10457  78 IIAITTAVSCAFLIVKVFLYdWLSSSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYLAAItsadeRAPLLQP 157

                         170
                  ....*....|.
gi 1972263037 172 DDEARSNNRHR 182
Cdd:pfam10457 158 GPEGRSNNQSD 168
START pfam01852
START domain;
246-441 8.42e-54

START domain;


:

Pssm-ID: 426476  Cd Length: 205  Bit Score: 178.75  E-value: 8.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 246 TLRECLDQVEELMRDSRLGGWKTLRS--ANPTVLQG--PDNYFLVRSEFNKFPALV-LFNIAWKDML---KWNTQVIEGK 317
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSneNGDVVLQIvePDHGEASRASGVVPMVAAlLVAELLKDMEyraQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 318 MIAHLDNATDLYYSVSAPAMRGYISSRDFLDLRKIKLDsSADVYTGYFVSVESNLCPNngNPKIVRGHNFPSMIRTLKDE 397
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRL-GGGVYVIVDRSVTHPQFPP--SSGYVRAERLPSGYLIQPCG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1972263037 398 AGVTYFEWLMKTDLKGGLP----RRLVHSGMVNYFSEHVKRMNEFAET 441
Cdd:pfam01852 158 NGPSKVTWVSHADLKGWLPswllRSLYKSGMPEGAKTWVATLQRLCEK 205
 
Name Accession Description Interval E-value
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 18-182 6.32e-66

Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal membrane protein, and carries this MENTAL (MLN64N-terminal) domain at its N-terminus. The domain is composed of four trans-membrane helices with three short intervening loops. The function of the domain is to capture cholesterol and pass it to the associated START domain pfam01852 for transfer to a cytosolic acceptor protein or membrane. In mammals, the MENTAL domain is involved in the localization of MLN64 and MENTHO in late endosomes, and also in homo-and of hetero-interactions of these two proteins.


Pssm-ID: 463097  Cd Length: 177  Bit Score: 209.07  E-value: 6.32e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  18 SKDRKRFIVITFFDTSITILLWLLCTVTRDDDWDKVFFNEINIFNpkfIRISLFDIVLLAVLRMLILGVVYGICLVKQWY 97
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINGENIKKAFEKEVLHYN---IKTSLFDIVLLAAFRFLVLLLFYALLRLNHWW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  98 TVAFTTLASSAYILMKVLFY-FNHSSSAVPPLLLIITSFTLCWSEFYLMPFQILPRERRYARRELDGI-----ENPEFST 171
Cdd:pfam10457  78 IIAITTAVSCAFLIVKVFLYdWLSSSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYLAAItsadeRAPLLQP 157

                         170
                  ....*....|.
gi 1972263037 172 DDEARSNNRHR 182
Cdd:pfam10457 158 GPEGRSNNQSD 168
START pfam01852
START domain;
246-441 8.42e-54

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 178.75  E-value: 8.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 246 TLRECLDQVEELMRDSRLGGWKTLRS--ANPTVLQG--PDNYFLVRSEFNKFPALV-LFNIAWKDML---KWNTQVIEGK 317
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSneNGDVVLQIvePDHGEASRASGVVPMVAAlLVAELLKDMEyraQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 318 MIAHLDNATDLYYSVSAPAMRGYISSRDFLDLRKIKLDsSADVYTGYFVSVESNLCPNngNPKIVRGHNFPSMIRTLKDE 397
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRL-GGGVYVIVDRSVTHPQFPP--SSGYVRAERLPSGYLIQPCG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1972263037 398 AGVTYFEWLMKTDLKGGLP----RRLVHSGMVNYFSEHVKRMNEFAET 441
Cdd:pfam01852 158 NGPSKVTWVSHADLKGWLPswllRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 198-446 2.50e-46

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 159.13  E-value: 2.50e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  198 TAVPSRVSSGVFIASDYDEFRSAAEFSSDEEARSRLL---VPPDTKRLFEITLRECLDQVEELMRDSRLggwktlrsanp 274
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSpgrKPGEAFRLVGVVPMVCADLVEELMDDLEY----------- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  275 tvlqgpdnyflvrsefnkfpalvlfniawkdMLKWNTQVIEGKMIAHLDNATDLYYSVSAPAMrGYISSRDFLDLRKIKL 354
Cdd:smart00234  70 -------------------------------RPEWDKNVAKAETLEVIDNGTVIYHYVSKFAA-GPVSPRDFVFVRYWRE 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  355 DssadVYTGYFVSVESNLCPNNG-NPKIVRGHNFPSMIRTLKDEAGVTYFEWLMKTDLKGGLPRRLVHSGMVNYFSEHVK 433
Cdd:smart00234 118 D----EDGSYAVVDVSVTHPTSPpESGYVRAENLPSGLLIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAK 193

                          250
                   ....*....|...
gi 1972263037  434 RMneFAETHYHCP 446
Cdd:smart00234 194 TL--VATLQKHCA 204
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 248-440 1.67e-27

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 108.19  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 248 RECLDQVEELMRDSRlgGWKTLRSANPTVL-----QGPDNYFL-VRSEFNKFPALVLFNIAWKD-MLKWNTQVIEGKMIA 320
Cdd:cd00177     1 EEAIEELLELLEEPE--GWKLVKEKDGVKIytkpyEDSGLKLLkAEGVIPASPEQVFELLMDIDlRKKWDKNFEEFEVIE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 321 HLDNATDL-YYSVSAPAMrgyISSRDFLDLRKIKlDSSADVYTGYFVSVESNLCPNNgnPKIVRGHNFPSMIRTLKDEAG 399
Cdd:cd00177    79 EIDEHTDIiYYKTKPPWP---VSPRDFVYLRRRR-KLDDGTYVIVSKSVDHDSHPKE--KGYVRAEIKLSGWIIEPLDPG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1972263037 400 VTYFEWLMKTDLKGGLPRRLVHSGMVNYFSEHVKRMNEFAE 440
Cdd:cd00177   153 KTKVTYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLRKAKK 193
 
Name Accession Description Interval E-value
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 18-182 6.32e-66

Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal membrane protein, and carries this MENTAL (MLN64N-terminal) domain at its N-terminus. The domain is composed of four trans-membrane helices with three short intervening loops. The function of the domain is to capture cholesterol and pass it to the associated START domain pfam01852 for transfer to a cytosolic acceptor protein or membrane. In mammals, the MENTAL domain is involved in the localization of MLN64 and MENTHO in late endosomes, and also in homo-and of hetero-interactions of these two proteins.


Pssm-ID: 463097  Cd Length: 177  Bit Score: 209.07  E-value: 6.32e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  18 SKDRKRFIVITFFDTSITILLWLLCTVTRDDDWDKVFFNEINIFNpkfIRISLFDIVLLAVLRMLILGVVYGICLVKQWY 97
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINGENIKKAFEKEVLHYN---IKTSLFDIVLLAAFRFLVLLLFYALLRLNHWW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  98 TVAFTTLASSAYILMKVLFY-FNHSSSAVPPLLLIITSFTLCWSEFYLMPFQILPRERRYARRELDGI-----ENPEFST 171
Cdd:pfam10457  78 IIAITTAVSCAFLIVKVFLYdWLSSSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYLAAItsadeRAPLLQP 157

                         170
                  ....*....|.
gi 1972263037 172 DDEARSNNRHR 182
Cdd:pfam10457 158 GPEGRSNNQSD 168
START pfam01852
START domain;
246-441 8.42e-54

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 178.75  E-value: 8.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 246 TLRECLDQVEELMRDSRLGGWKTLRS--ANPTVLQG--PDNYFLVRSEFNKFPALV-LFNIAWKDML---KWNTQVIEGK 317
Cdd:pfam01852   1 ELAEEAAQELLKLALSDEPGWVLLSSneNGDVVLQIvePDHGEASRASGVVPMVAAlLVAELLKDMEyraQWDKDVRSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 318 MIAHLDNATDLYYSVSAPAMRGYISSRDFLDLRKIKLDsSADVYTGYFVSVESNLCPNngNPKIVRGHNFPSMIRTLKDE 397
Cdd:pfam01852  81 TLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRL-GGGVYVIVDRSVTHPQFPP--SSGYVRAERLPSGYLIQPCG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1972263037 398 AGVTYFEWLMKTDLKGGLP----RRLVHSGMVNYFSEHVKRMNEFAET 441
Cdd:pfam01852 158 NGPSKVTWVSHADLKGWLPswllRSLYKSGMPEGAKTWVATLQRLCEK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 198-446 2.50e-46

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 159.13  E-value: 2.50e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  198 TAVPSRVSSGVFIASDYDEFRSAAEFSSDEEARSRLL---VPPDTKRLFEITLRECLDQVEELMRDSRLggwktlrsanp 274
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSpgrKPGEAFRLVGVVPMVCADLVEELMDDLEY----------- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  275 tvlqgpdnyflvrsefnkfpalvlfniawkdMLKWNTQVIEGKMIAHLDNATDLYYSVSAPAMrGYISSRDFLDLRKIKL 354
Cdd:smart00234  70 -------------------------------RPEWDKNVAKAETLEVIDNGTVIYHYVSKFAA-GPVSPRDFVFVRYWRE 117

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037  355 DssadVYTGYFVSVESNLCPNNG-NPKIVRGHNFPSMIRTLKDEAGVTYFEWLMKTDLKGGLPRRLVHSGMVNYFSEHVK 433
Cdd:smart00234 118 D----EDGSYAVVDVSVTHPTSPpESGYVRAENLPSGLLIEPLGNGPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAK 193

                          250
                   ....*....|...
gi 1972263037  434 RMneFAETHYHCP 446
Cdd:smart00234 194 TL--VATLQKHCA 204
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 248-440 1.67e-27

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 108.19  E-value: 1.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 248 RECLDQVEELMRDSRlgGWKTLRSANPTVL-----QGPDNYFL-VRSEFNKFPALVLFNIAWKD-MLKWNTQVIEGKMIA 320
Cdd:cd00177     1 EEAIEELLELLEEPE--GWKLVKEKDGVKIytkpyEDSGLKLLkAEGVIPASPEQVFELLMDIDlRKKWDKNFEEFEVIE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 321 HLDNATDL-YYSVSAPAMrgyISSRDFLDLRKIKlDSSADVYTGYFVSVESNLCPNNgnPKIVRGHNFPSMIRTLKDEAG 399
Cdd:cd00177    79 EIDEHTDIiYYKTKPPWP---VSPRDFVYLRRRR-KLDDGTYVIVSKSVDHDSHPKE--KGYVRAEIKLSGWIIEPLDPG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1972263037 400 VTYFEWLMKTDLKGGLPRRLVHSGMVNYFSEHVKRMNEFAE 440
Cdd:cd00177   153 KTKVTYVLQVDPKGSIPKSLVNSAAKKQLASFLKDLRKAKK 193
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 248-435 3.73e-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: 107.83  E-value: 3.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 248 RECLDQVEELMRDS----RLGGWKtLRSAN------PTV-LQGPDNYFLVRSEFNkFPALVLFNIAWKDMLK---WNTQV 313
Cdd:cd08868     4 LEYLKQGAEALARAwsilTDPGWK-LEKNTtwgdvvYSRnVPGVGKVFRLTGVLD-CPAEFLYNELVLNVESlpsWNPTV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 314 IEGKMIAHLDNATDLYYSVSAPAMRGYISSRDFLDLRKIKLDSSAdvYTGYFVSVESNLCPNngNPKIVRGHNFPS--MI 391
Cdd:cd08868    82 LECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENC--YLSSGVSVEHPAMPP--TKNYVRGENGPGcwIL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1972263037 392 RTLKDEAGVTYFEWLMKTDLKGGLPRRLVH----SGMVNY---FSEHVKRM 435
Cdd:cd08868   158 RPLPNNPNKCNFTWLLNTDLKGWLPQYLVDqalaSVLLDFmkhLRKRIATL 208
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 248-437 1.71e-17

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: 80.68  E-value: 1.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 248 RECLDQVEELMRDSRLggWKTLRS-ANPTVLQGPDNYF----LVRSEFNKFPALVLFN---IAWKDMLKWNTQVIEGKMI 319
Cdd:cd08906    11 KEALAVVEQILAQEEN--WKFEKNnDNGDTVYTLEVPFhgktFILKAFMQCPAELVYQeviLQPEKMVLWNKTVSACQVL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 320 AHLDNATDLYYSVSAPAMRGYISSRDFLDLRKIklDSSADVYTGYFVSveSNLCPNNGNPKIVRGHNFPSMIRTLKDEAG 399
Cdd:cd08906    89 QRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRI--ERRRDRYVSAGIS--TTHSHKPPLSKYVRGENGPGGFVVLKSASN 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1972263037 400 --VTYFEWLMKTDLKGGLPRRLVH----SGMVNYFSEHVKRMNE 437
Cdd:cd08906   165 psVCTFIWILNTDLKGRLPRYLIHqslaATMFEFASHLRQRIRD 208
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 235-420 7.66e-10

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: 58.81  E-value: 7.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 235 VPPDTKRLFEiTLRECLDQVEelmrdsrlgGWKTLRSANPTV--LQGPDN----YFLVRSEFNKFPALVLFniawkDML- 307
Cdd:cd08871     4 VRLPTDADFE-EFKKLCDSTD---------GWKLKYNKNNVKvwTKNPENssikMIKVSAIFPDVPAETLY-----DVLh 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 308 ------KWNTQVIEGKMIAHLDNATDL-YYSVSAPAMrgyISSRDFLDLRkikldsSADVYTGYFV----SVESNLCPNn 376
Cdd:cd08871    69 dpeyrkTWDSNMIESFDICQLNPNNDIgYYSAKCPKP---LKNRDFVNLR------SWLEFGGEYIifnhSVKHKKYPP- 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1972263037 377 gNPKIVRGHNFPS--MIRTLKDE-AGVTYFEWlmkTDLKGGLPRRLV 420
Cdd:cd08871   139 -RKGFVRAISLLTgyLIRPTGPKgCTLTYVTQ---NDPKGSLPKWVV 181
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 306-436 1.87e-09

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: 57.54  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 306 MLKWNTQVIEGKMIAHLDNATDLYYSVSAPAMRGYISSRDFLDLRKIKLDSSADVYTGyfVSVESNLCPNNGNpkIVRGH 385
Cdd:cd08905    75 MGEWNPNVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRRGSTCVLAG--MATHFGLMPEQKG--FIRAE 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972263037 386 NFPSMI--RTLKDEAGVTYFEWLMKTDLKGGLPRRLVHSGMVNY---FSEHV-KRMN 436
Cdd:cd08905   151 NGPTCIvlRPLAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTqvdFANHLrQRMA 207
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 265-433 1.71e-08

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: 54.39  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 265 GWKTLRSANP-TVLQGPDNYF---LVRSEfNKFPALV------LFNIAWKDMLKWNTQVIEGKMIAHLDNATDLYYSVSA 334
Cdd:cd08867    23 GWKVLKTVKNiTVSWKPSTEFtghLYRAE-GIVDALPekvidvIIPPCGGLRLKWDKSLKHYEVLEKISEDLCVGRTITP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 335 PAMRGYISSRDFLDLRKIK------LDSSAdvytgyfVSVE-SNLCPNNGnpkIVRGHNFPS--MIRTLKDEAGVTYFEW 405
Cdd:cd08867   102 SAAMGLISPRDFVDLVYVKryednqWSSSG-------KSVDiPERPPTPG---FVRGYNHPCgyFCSPLKGSPDKSFLVL 171

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1972263037 406 LMKTDLKGGLPRRLVHSGM----VNYFSEHVK 433
Cdd:cd08867   172 YVQTDLRGMIPQSLVESAMpsnlVNFYTDLVK 203
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 238-424 2.58e-08

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: 54.14  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 238 DTKRLFEITLRECLdqveELMRDSrlGGWKTLRSANP-TVLQGPDNYF---LVRSE--FNKFPA-LVLFNIAWKDMLKWN 310
Cdd:cd08904     2 DFKKIAQETSQEVL----GYSRDT--SGWKVVKTSKKiTVSWKPSRKYhgnLYRVEgiIPESPAkLIQFMYQPEHRIKWD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 311 TQVIEGKMIAHLDNATDLYYSVSAPAMRGYISSRDFLDLRKIKLdSSADVYTGYFVSVESNLCPNNGNpkIVRGHNFPS- 389
Cdd:cd08904    76 KSLQVYKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKR-YEGNMNIVSSVSVEYPQCPPSSN--YIRGYNHPCg 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1972263037 390 -MIRTLKDEAGVTYFEWLMKTDLKGGLPRRLVHSGM 424
Cdd:cd08904   153 yVCSPLPENPAYSKLVMFVQPELRGNLSRSVIEKTM 188
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 265-438 8.68e-06

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: 46.37  E-value: 8.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 265 GWKTLRSANPTVLqgpdnYFLVRSEFN----KFPALVLFNI--AWKDM--------LKWNTQVIEGKMIAHLDNATDLYY 330
Cdd:cd08903    23 GWKTCRRTNEVAV-----SWRPSAEFAgnlyKGEGIVYATLeqVWDCLkpaagglrVKWDQNVKDFEVVEAISDDVSVCR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972263037 331 SVSAPAMRGYISSRDFLDLRKIKLDSSADVYTGYfVSVESNLCPNngNPKIVRGHNFP--SMIRTLKDEAGVTYFEWLMK 408
Cdd:cd08903    98 TVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNA-TNVEHPLCPP--QAGFVRGFNHPcgCFCEPVPGEPDKTQLVSFFQ 174

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1972263037 409 TDLKGGLPRRLVHS----GMVNYFSEHVKRMNEF 438
Cdd:cd08903   175 TDLSGYLPQTVVDSffpaSMAEFYNNLTKAVKAL 208
 
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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