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Conserved domains on  [gi|1694459893|ref|NP_001358031|]
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stAR-related lipid transfer protein 6 isoform 2 [Homo sapiens]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 1-145 2.66e-95

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 cd08904:

Pssm-ID: 472699  Cd Length: 204  Bit Score: 274.09  E-value: 2.66e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTS-------------------------------------------------- 30
Cdd:cd08904     1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSkkitvswkpsrkyhgnlyrvegiipespakliqfmyqpehrikwdkslqv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  31 ---------DTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEE 101
Cdd:cd08904    81 ykmlqridsDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1694459893 102 NPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 145
Cdd:cd08904   161 NPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
 
Name Accession Description Interval E-value
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 1-145 2.66e-95

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: 274.09  E-value: 2.66e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTS-------------------------------------------------- 30
Cdd:cd08904     1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSkkitvswkpsrkyhgnlyrvegiipespakliqfmyqpehrikwdkslqv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  31 ---------DTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEE 101
Cdd:cd08904    81 ykmlqridsDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1694459893 102 NPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 145
Cdd:cd08904   161 NPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
START pfam01852
START domain;
29-126 2.18e-17

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 75.52  E-value: 2.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  29 TSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENpaYSKL 108
Cdd:pfam01852  86 SSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG--PSKV 163

                          90
                  ....*....|....*...
gi 1694459893 109 VMFVQTEMRGKLSPSIIE 126
Cdd:pfam01852 164 TWVSHADLKGWLPSWLLR 181
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 29-136 4.79e-17

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 74.39  E-value: 4.79e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893   29 TSDTFICHtITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPaySKL 108
Cdd:smart00234  87 DNGTVIYH-YVSKFAAGPVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGP--SKV 163

                           90       100
                   ....*....|....*....|....*...
gi 1694459893  109 VMFVQTEMRGKLSPSIIEKTMPSNLVNF 136
Cdd:smart00234 164 TWVSHADLKGWLPHWLVRSLIKSGLAEF 191
 
Name Accession Description Interval E-value
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 1-145 2.66e-95

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: 274.09  E-value: 2.66e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTS-------------------------------------------------- 30
Cdd:cd08904     1 MDFKKIAQETSQEVLGYSRDTSGWKVVKTSkkitvswkpsrkyhgnlyrvegiipespakliqfmyqpehrikwdkslqv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  31 ---------DTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEE 101
Cdd:cd08904    81 ykmlqridsDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPE 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1694459893 102 NPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 145
Cdd:cd08904   161 NPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 1-145 1.29e-76

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: 226.96  E-value: 1.29e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893   1 MDFKAIAQQTAQEVLGYNRDTSGWKVVKTS-------------------------------------------------- 30
Cdd:cd08867     1 MDFKVIAEKLANEALQYINDTDGWKVLKTVknitvswkpsteftghlyraegivdalpekvidviippcgglrlkwdksl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  31 -----------DTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPM 99
Cdd:cd08867    81 khyevlekiseDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1694459893 100 EENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 145
Cdd:cd08867   161 KGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGVK 206
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 29-146 1.80e-33

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: 117.24  E-value: 1.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  29 TSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPAYSKL 108
Cdd:cd08903    90 SDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPVPGEPDKTQL 169

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1694459893 109 VMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIKA 146
Cdd:cd08903   170 VSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKA 207
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 47-145 2.62e-24

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: 93.48  E-value: 2.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  47 ISPRDFIDLVYIKRYEGNMnIISSKSVDFPEYPPssNYIRGYNHPCGFVCSPMEENPAYSKLVMFVQTEMRGKLSPSIIE 126
Cdd:cd08902   107 ISPREFVDFSYTTQYEDGL-LSCGVSIEYEEARP--NFVRGFNHPCGWFCVPLKDNPSHSLLTGYIQTDLRGMLPQSAVD 183

                          90
                  ....*....|....*....
gi 1694459893 127 KTMPSNLVNFILNAKDGIK 145
Cdd:cd08902   184 TAMASTLVNFYSDLKKALK 202
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 17-137 3.53e-22

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: 87.39  E-value: 3.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  17 YNRDTSGWKVVKT--SDTFICHTITQSFAVgsISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGF 94
Cdd:cd00177    67 WDKNFEEFEVIEEidEHTDIIYYKTKPPWP--VSPRDFVYLRRRRKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGW 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1694459893  95 VCSPMEENpaYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFI 137
Cdd:cd00177   145 IIEPLDPG--KTKVTYVLQVDPKGSIPKSLVNSAAKKQLASFL 185
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 31-147 5.05e-21

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: 85.10  E-value: 5.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  31 DTFICHTITQSFAVGSISPRDFIDLVYIKRYEgNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPAYSKLVM 110
Cdd:cd08868    93 NTDISYQVAAEAGGGLVSPRDFVSLRHWGIRE-NCYLSSGVSVEHPAMPPTKNYVRGENGPGCWILRPLPNNPNKCNFTW 171

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1694459893 111 FVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIKAH 147
Cdd:cd08868   172 LLNTDLKGWLPQYLVDQALASVLLDFMKHLRKRIATL 208
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 12-145 3.08e-18

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: 77.59  E-value: 3.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  12 QEVLGYNRDTSGWKVVKTSD--TFICHTITQSFAVGSISPRDFIDLVYIKRYeGNMNIISSKSVDFPEYPPSSNYIRGYN 89
Cdd:cd08906    73 EKMVLWNKTVSACQVLQRVDdnTLVSYDVAAGAAGGVVSPRDFVNVRRIERR-RDRYVSAGISTTHSHKPPLSKYVRGEN 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1694459893  90 HPCGFVCSPMEENPAYSKLVMFVQTEMRGKLSPSIIEKTMPSNLVNFILNAKDGIK 145
Cdd:cd08906   152 GPGGFVVLKSASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIR 207
START pfam01852
START domain;
29-126 2.18e-17

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 75.52  E-value: 2.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  29 TSDTFICHTITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENpaYSKL 108
Cdd:pfam01852  86 SSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG--PSKV 163

                          90
                  ....*....|....*...
gi 1694459893 109 VMFVQTEMRGKLSPSIIE 126
Cdd:pfam01852 164 TWVSHADLKGWLPSWLLR 181
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 29-136 4.79e-17

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 74.39  E-value: 4.79e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893   29 TSDTFICHtITQSFAVGSISPRDFIDLVYIKRYEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPaySKL 108
Cdd:smart00234  87 DNGTVIYH-YVSKFAAGPVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGNGP--SKV 163

                           90       100
                   ....*....|....*....|....*...
gi 1694459893  109 VMFVQTEMRGKLSPSIIEKTMPSNLVNF 136
Cdd:smart00234 164 TWVSHADLKGWLPHWLVRSLIKSGLAEF 191
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 31-137 2.15e-13

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: 64.86  E-value: 2.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  31 DTFICHTITQSFAVGSISPRDFIDLVYIKRyEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPAYSKLVM 110
Cdd:cd08905    94 DTLITHEVAAETAGNVVGPRDFVSVRCAKR-RGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLRPLAGDPSKTKLTW 172

                          90       100
                  ....*....|....*....|....*..
gi 1694459893 111 FVQTEMRGKLSPSIIEKTMPSNLVNFI 137
Cdd:cd08905   173 LLSIDLKGWLPKSIINQVLSQTQVDFA 199
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 31-139 1.80e-04

Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974), STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 and STARD15/ACOT12 are type II acetyl-CoA thioesterases; they catalyze the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, STARD14 and STARD15 each have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice. Human STARD15 may have roles in cholesterol metabolism and in beta-oxidation.


Pssm-ID: 176882  Cd Length: 235  Bit Score: 40.27  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  31 DTFICHTITQSfaVGSISPRDFIDLVYIKR--YEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFV----CSPMEE--- 101
Cdd:cd08873   121 DDGIYHTTMPS--LTSEKPNDFVLLVSRRKpaTDGDPYKVAFRSVTLPRVPQTPGYSRTEVACAGFVirqdCGTCTEvsy 198

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1694459893 102 -NPAYSKLVMFVQTEMRGkLSpSIIEKTMPSnLVNFILN 139
Cdd:cd08873   199 yNETNPKLLSYVTCNLAG-LS-ALYCRTFHC-CEQFLVT 234
START_STARD14-like cd08913
Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes ...
 31-113 2.00e-03

Lipid-binding START domain of mammalian STARDT14 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974) 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. STARD14/ACOT11 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice.


Pssm-ID: 176921  Cd Length: 240  Bit Score: 37.15  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  31 DTFICHTITQSFAVGSiSPRDFIDLVYIKR--YEGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCspMEENPAYSKL 108
Cdd:cd08913   125 DDAIYHVTSPSLSGHG-KPQDFVILASRRKpcDNGDPYVIALRSVTLPTHPPTPEYTRGETLCSGFCI--WEESDQLTKV 201


                  ....*
gi 1694459893 109 VMFVQ 113
Cdd:cd08913   202 SYYNQ 206
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 47-137 3.16e-03

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: 36.47  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1694459893  47 ISPRDFIDLVYIKRYEGNMnIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEENPaySKLVMFVQTEMRGKLspsiie 126
Cdd:cd08871   106 LKNRDFVNLRSWLEFGGEY-IIFNHSVKHKKYPPRKGFVRAISLLTGYLIRPTGPKG--CTLTYVTQNDPKGSL------ 176

                          90
                  ....*....|.
gi 1694459893 127 ktmPSNLVNFI 137
Cdd:cd08871   177 ---PKWVVNKA 184
START_STARD15-like cd08914
Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes ...
 49-102 8.02e-03

Lipid-binding START domain of mammalian STARD15 and related proteins; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114) 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. STARD15/ACOT12 is a type II acetyl-CoA thioesterase; it catalyzes the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, most proteins in this subgroup have two tandem copies of the hotdog domain. Human STARD15/ACOT12 may have roles in cholesterol metabolism and in beta-oxidation.


Pssm-ID: 176922  Cd Length: 236  Bit Score: 35.64  E-value: 8.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1694459893  49 PRDFIDLVYiKRY---EGNMNIISSKSVDFPEYPPSSNYIRGYNHPCGFVCSPMEEN 102
Cdd:cd08914   138 PKDLVVLVS-RRKplkDGNTYVVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIDSN 193
 
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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