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Conserved domains on  [gi|45550514|ref|NP_611936|]
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Start1, isoform A [Drosophila melanogaster]

Protein Classification

steroidogenic acute regulatory family protein( domain architecture ID 10564580)

steroidogenic acute regulatory (StAR) family protein may bind lipids, similar to Drosophila melanogaster steroidogenic acute regulatory protein-like that may bind to and transport cholesterol and may play a role in ecdysteroid biosynthesis

CATH:  3.30.530.20
Gene Ontology:  GO:0008289
PubMed:  31927098|10322415|11276083|15718238
SCOP:  4002052

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 ...
 57-233 1.10e-96

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: 292.27  E-value: 1.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514    57 SVVRRFFCLFVTFDLVFVSLLWLICIVINGDNIFTAFHKQIVEYTIYKSLFDVVAVAICRFLVLIFFYAILYINHWSIIA 136
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINGENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514   137 LSTSGSCLFLISKVFVFDWLDSKQQVFEVILIITSFILAWGEAWFLDCRVIPQERHAQHYF--RTMTSNDRTPMEQPAIL 214
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLSSSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYlaAITSADERAPLLQPGPE 160

                         170
                  ....*....|....*....
gi 45550514   215 IEQERppQSVTDFYSLMDT 233
Cdd:pfam10457 161 GRSNN--QSDGNFYSPPES 177
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 247-571 5.40e-45

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


The actual alignment was detected with superfamily member cd08868:

Pssm-ID: 472699  Cd Length: 208  Bit Score: 158.29  E-value: 5.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 247 YTQMGLDCLRKAYEIIESSDWKVEKVNQKGDTIHSTQRDKIGKIYKLTARIKYPAKALMEDLFYRIEDCPKWNPALLESK 326
Cdd:cd08868   6 YLKQGAEALARAWSILTDPGWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNPTVLECK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 327 IVRKINSYTDITYQVSVGGGGGMVKSRDFVNLRSCRLFYNGqicdddetaqlssddgnsslnrscegsvstisdgdsntp 406
Cdd:cd08868  86 IIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENC--------------------------------------- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 407 llpssvssckatfptsskgaampfdtlgnslgakslgpivnfdeepppldqdefedakdkvdgeannmtkpnvpsvgktk 486
Cdd:cd08868     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 487 drvWVTSAVSVQYAAVPPSPKYTRGQNIVSGFAFREIVGKSDSCIVEWVLCLDLKGYIPRYVLDAALTSSMTDYISNLRK 566
Cdd:cd08868 127 ---YLSSGVSVEHPAMPPTKNYVRGENGPGCWILRPLPNNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRK 203


                ....*
gi 45550514 567 HVNEL 571
Cdd:cd08868 204 RIATL 208
 
Name Accession Description Interval E-value
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 57-233 1.10e-96

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: 292.27  E-value: 1.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514    57 SVVRRFFCLFVTFDLVFVSLLWLICIVINGDNIFTAFHKQIVEYTIYKSLFDVVAVAICRFLVLIFFYAILYINHWSIIA 136
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINGENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514   137 LSTSGSCLFLISKVFVFDWLDSKQQVFEVILIITSFILAWGEAWFLDCRVIPQERHAQHYF--RTMTSNDRTPMEQPAIL 214
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLSSSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYlaAITSADERAPLLQPGPE 160

                         170
                  ....*....|....*....
gi 45550514   215 IEQERppQSVTDFYSLMDT 233
Cdd:pfam10457 161 GRSNN--QSDGNFYSPPES 177
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 247-571 5.40e-45

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: 158.29  E-value: 5.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 247 YTQMGLDCLRKAYEIIESSDWKVEKVNQKGDTIHSTQRDKIGKIYKLTARIKYPAKALMEDLFYRIEDCPKWNPALLESK 326
Cdd:cd08868   6 YLKQGAEALARAWSILTDPGWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNPTVLECK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 327 IVRKINSYTDITYQVSVGGGGGMVKSRDFVNLRSCRLFYNGqicdddetaqlssddgnsslnrscegsvstisdgdsntp 406
Cdd:cd08868  86 IIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENC--------------------------------------- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 407 llpssvssckatfptsskgaampfdtlgnslgakslgpivnfdeepppldqdefedakdkvdgeannmtkpnvpsvgktk 486
Cdd:cd08868     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 487 drvWVTSAVSVQYAAVPPSPKYTRGQNIVSGFAFREIVGKSDSCIVEWVLCLDLKGYIPRYVLDAALTSSMTDYISNLRK 566
Cdd:cd08868 127 ---YLSSGVSVEHPAMPPTKNYVRGENGPGCWILRPLPNNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRK 203


                ....*
gi 45550514 567 HVNEL 571
Cdd:cd08868 204 RIATL 208
START pfam01852
START domain;
255-574 3.84e-12

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 65.50  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514   255 LRKAYEiiESSDWKVEKVNQKGDTIHSTQRDKIGKIYKLTARIKYPAKALMEDLFYRIEDCPKWNPALLESKIVRKINSY 334
Cdd:pfam01852  11 LKLALS--DEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAETLEVISSG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514   335 TDITYQVSVGGGGGMVKSRDFVNLRSCRlfyngqicdddetaqlssddgnsslnrscegsvsTISDGdsntpllpssvss 414
Cdd:pfam01852  89 GDLQYYVAALVAPSPLSPRDFVFLRYWR----------------------------------RLGGG------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514   415 ckatfptsskgaampfdtlgnslgakslgpivnfdeepppldqdefedakdkvdgeannmtkpnvpsvgktkdrVWVTSA 494
Cdd:pfam01852 122 --------------------------------------------------------------------------VYVIVD 127

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514   495 VSVQYAAVPPSPKYTRGQNIVSGFAFREivgKSDS-CIVEWVLCLDLKGYIPRYVLDAALTSSMTDYISNLRKHVNELRQ 573
Cdd:pfam01852 128 RSVTHPQFPPSSGYVRAERLPSGYLIQP---CGNGpSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCE 204


                  .
gi 45550514   574 K 574
Cdd:pfam01852 205 K 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 487-574 1.69e-07

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 52.05  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514    487 DRVWVTSAVSVQYAAVPPSPKYTRGQNIVSGFAFREivgKSDS-CIVEWVLCLDLKGYIPRYVLDAALTSSMTDYISNLR 565
Cdd:smart00234 120 DGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEP---LGNGpSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLV 196


                   ....*....
gi 45550514    566 KHVNELRQK 574
Cdd:smart00234 197 ATLQKHCAK 205
 
Name Accession Description Interval E-value
MENTAL pfam10457
Cholesterol-capturing domain; Human meta-static lymph node (MLN) 64 is a late endosomal ...
 57-233 1.10e-96

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: 292.27  E-value: 1.10e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514    57 SVVRRFFCLFVTFDLVFVSLLWLICIVINGDNIFTAFHKQIVEYTIYKSLFDVVAVAICRFLVLIFFYAILYINHWSIIA 136
Cdd:pfam10457   1 SDVRRFFCLFVTFDLLFTSLLWLICLVINGENIKKAFEKEVLHYNIKTSLFDIVLLAAFRFLVLLLFYALLRLNHWWIIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514   137 LSTSGSCLFLISKVFVFDWLDSKQQVFEVILIITSFILAWGEAWFLDCRVIPQERHAQHYF--RTMTSNDRTPMEQPAIL 214
Cdd:pfam10457  81 ITTAVSCAFLIVKVFLYDWLSSSQPVFGVLLIITSFVLAWIEAWFLDFKVLPQEAEAERRYlaAITSADERAPLLQPGPE 160

                         170
                  ....*....|....*....
gi 45550514   215 IEQERppQSVTDFYSLMDT 233
Cdd:pfam10457 161 GRSNN--QSDGNFYSPPES 177
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 247-571 5.40e-45

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: 158.29  E-value: 5.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 247 YTQMGLDCLRKAYEIIESSDWKVEKVNQKGDTIHSTQRDKIGKIYKLTARIKYPAKALMEDLFYRIEDCPKWNPALLESK 326
Cdd:cd08868   6 YLKQGAEALARAWSILTDPGWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDCPAEFLYNELVLNVESLPSWNPTVLECK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 327 IVRKINSYTDITYQVSVGGGGGMVKSRDFVNLRSCRLFYNGqicdddetaqlssddgnsslnrscegsvstisdgdsntp 406
Cdd:cd08868  86 IIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENC--------------------------------------- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 407 llpssvssckatfptsskgaampfdtlgnslgakslgpivnfdeepppldqdefedakdkvdgeannmtkpnvpsvgktk 486
Cdd:cd08868     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 487 drvWVTSAVSVQYAAVPPSPKYTRGQNIVSGFAFREIVGKSDSCIVEWVLCLDLKGYIPRYVLDAALTSSMTDYISNLRK 566
Cdd:cd08868 127 ---YLSSGVSVEHPAMPPTKNYVRGENGPGCWILRPLPNNPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRK 203


                ....*
gi 45550514 567 HVNEL 571
Cdd:cd08868 204 RIATL 208
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 247-362 1.92e-20

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: 89.90  E-value: 1.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 247 YTQMGLDCLRKAYEIIESSD-WKVEKVNQKGDTIHSTQRDKIGKIYKLTARIKYPAKALMEDLFYRIEDCPKWNPALLES 325
Cdd:cd08905   6 YIKQGEEALQKSLSILQDQEgWKTEIVAENGDKVLSKVVPDIGKVFRLEVVVDQPLDNLYSELVDRMEQMGEWNPNVKEV 85

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 45550514 326 KIVRKINSYTDITYQVSVGGGGGMVKSRDFVNLRSCR 362
Cdd:cd08905  86 KILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAK 122
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 247-571 5.21e-19

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: 85.68  E-value: 5.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 247 YTQMGLDCLRKAYEII-ESSDWKVEKVNQKGDTIHSTQRDKIGKIYKLTARIKYPAKALMEDLFYRIEDCPKWNPALLES 325
Cdd:cd08906   6 YVRQGKEALAVVEQILaQEENWKFEKNNDNGDTVYTLEVPFHGKTFILKAFMQCPAELVYQEVILQPEKMVLWNKTVSAC 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 326 KIVRKINSYTDITYQVSVGGGGGMVKSRDFVNLRscrlfyngqicdddetaqlssddgnsslnrscegsvstisdgdsnt 405
Cdd:cd08906  86 QVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVR---------------------------------------------- 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 406 pllpssvssckatfptsskgaampfdtlgnslgakslgpivnfdeepppldqdefedakdkvdgeannmtkpnvpSVGKT 485
Cdd:cd08906 120 ---------------------------------------------------------------------------RIERR 124

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 486 KDRvWVTSAVSVQYAAVPPSPKYTRGQNIVSGFafreIVGKSDS----CIVEWVLCLDLKGYIPRYVLDAALTSSMTDYI 561
Cdd:cd08906 125 RDR-YVSAGISTTHSHKPPLSKYVRGENGPGGF----VVLKSASnpsvCTFIWILNTDLKGRLPRYLIHQSLAATMFEFA 199

                       330
                ....*....|
gi 45550514 562 SNLRKHVNEL 571
Cdd:cd08906 200 SHLRQRIRDL 209
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 263-555 2.10e-12

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: 66.21  E-value: 2.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 263 ESSDWKVEKvNQKGDTIHST-QRDKIGKIYKLTARIKYPAKALMEdLFYRIEDCPKWNPALLESKIVRKINSYTDITYQv 341
Cdd:cd00177  13 EPEGWKLVK-EKDGVKIYTKpYEDSGLKLLKAEGVIPASPEQVFE-LLMDIDLRKKWDKNFEEFEVIEEIDEHTDIIYY- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 342 sVGGGGGMVKSRDFVNLRSCRlfyngqicdddetaqlssddgnsslnrscegsvstisdgdsntpllpssvssckatfpt 421
Cdd:cd00177  90 -KTKPPWPVSPRDFVYLRRRR----------------------------------------------------------- 109

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 422 sskgaampfdtlgnslgakslgpivnfdeepppldqdefedakdkvdgeannmtkpnvpsvgKTKDRVWVTSAVSVQYAA 501
Cdd:cd00177 110 --------------------------------------------------------------KLDDGTYVIVSKSVDHDS 127

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 45550514 502 VPPSPKYTRGQNIVSGFAFREIvgKSDSCIVEWVLCLDLKGYIPRYVLDAALTS 555
Cdd:cd00177 128 HPKEKGYVRAEIKLSGWIIEPL--DPGKTKVTYVLQVDPKGSIPKSLVNSAAKK 179
START pfam01852
START domain;
255-574 3.84e-12

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 65.50  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514   255 LRKAYEiiESSDWKVEKVNQKGDTIHSTQRDKIGKIYKLTARIKYPAKALMEDLFYRIEDCPKWNPALLESKIVRKINSY 334
Cdd:pfam01852  11 LKLALS--DEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKDMEYRAQWDKDVRSAETLEVISSG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514   335 TDITYQVSVGGGGGMVKSRDFVNLRSCRlfyngqicdddetaqlssddgnsslnrscegsvsTISDGdsntpllpssvss 414
Cdd:pfam01852  89 GDLQYYVAALVAPSPLSPRDFVFLRYWR----------------------------------RLGGG------------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514   415 ckatfptsskgaampfdtlgnslgakslgpivnfdeepppldqdefedakdkvdgeannmtkpnvpsvgktkdrVWVTSA 494
Cdd:pfam01852 122 --------------------------------------------------------------------------VYVIVD 127

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514   495 VSVQYAAVPPSPKYTRGQNIVSGFAFREivgKSDS-CIVEWVLCLDLKGYIPRYVLDAALTSSMTDYISNLRKHVNELRQ 573
Cdd:pfam01852 128 RSVTHPQFPPSSGYVRAERLPSGYLIQP---CGNGpSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCE 204


                  .
gi 45550514   574 K 574
Cdd:pfam01852 205 K 205
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 487-568 8.71e-12

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: 64.79  E-value: 8.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 487 DRVWVTSAVSVQYAAVPPSPKYTRGQNIVSGFAFREIVGKSDSCIVEWVLCLDLKGYIPRYVLDAALTSSMTDYISNLRK 566
Cdd:cd08867 124 DNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPLKGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVK 203


                ..
gi 45550514 567 HV 568
Cdd:cd08867 204 GV 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 487-574 1.69e-07

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 52.05  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514    487 DRVWVTSAVSVQYAAVPPSPKYTRGQNIVSGFAFREivgKSDS-CIVEWVLCLDLKGYIPRYVLDAALTSSMTDYISNLR 565
Cdd:smart00234 120 DGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEP---LGNGpSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLV 196


                   ....*....
gi 45550514    566 KHVNELRQK 574
Cdd:smart00234 197 ATLQKHCAK 205
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 266-374 2.04e-07

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 51.66  E-value: 2.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514    266 DWKVEKVNQKGDTIHSTQRDKI--GKIYKLTARIKYPAKALMEDLFYRIEDCPKWNPALLESKIVRKINSYTDITYQVSV 343
Cdd:smart00234  19 GWVLSSENENGDEVRSIFSPGRkpGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKAETLEVIDNGTVIYHYVSK 98

                           90       100       110
                   ....*....|....*....|....*....|.
gi 45550514    344 GGGGGMVkSRDFVNLRSCRlfyngqiCDDDE 374
Cdd:smart00234  99 FAAGPVS-PRDFVFVRYWR-------EDEDG 121
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 478-571 1.14e-05

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: 46.75  E-value: 1.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 478 NVPSVGKTKDRVWVTSAVSVQYAAVPPSPKYTRGQNIVSGFAFREIVGKSDSCIVEWVLCLDLKGYIPRYVLDAALTSSM 557
Cdd:cd08903 115 DVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPVPGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASM 194

                        90
                ....*....|....
gi 45550514 558 TDYISNLRKHVNEL 571
Cdd:cd08903 195 AEFYNNLTKAVKAL 208
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 263-358 3.84e-05

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: 44.90  E-value: 3.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550514 263 ESSDWKVEKVNQKGDTIHSTQRDKIGKIYKLTARIK-YPAKalMEDLFYRIEDCPKWNPALLESKIVRKINSYTDITYQV 341
Cdd:cd08904  20 DTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPeSPAK--LIQFMYQPEHRIKWDKSLQVYKMLQRIDSDTFICHTI 97

                        90
                ....*....|....*..
gi 45550514 342 SVGGGGGMVKSRDFVNL 358
Cdd:cd08904  98 TQSFAMGSISPRDFVDL 114
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 491-565 5.25e-04

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: 41.43  E-value: 5.25e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45550514 491 VTSAVSVQYAAVPPSPKYTRGQNIVSGFAFREIV-GKSDSCIVEWVLClDLKGYIPRYVLDAALTSSMTDYISNLR 565
Cdd:cd08904 126 IVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPeNPAYSKLVMFVQP-ELRGNLSRSVIEKTMPTNLVNLILDAK 200
 
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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