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Conserved domains on  [gi|21218432|ref|NP_075866|]
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stAR-related lipid transfer protein 5 [Mus musculus]

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 ...
 6-211 7.03e-142

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 cd08903:

Pssm-ID: 472699  Cd Length: 208  Bit Score: 394.20  E-value: 7.03e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432   6 ATQESEAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCIKPVASGLREKWDDNVSS 85
Cdd:cd08903   3 YAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPAAGGLRVKWDQNVKD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  86 FEIVQSITDMLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08903  83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPVPG 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21218432 166 DPNKTNLVTFFQTDLSGYLPQSVVDSFFPRSMAEFYPNLQKAVRKF 211
Cdd:cd08903 163 EPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKAL 208
 
Name Accession Description Interval E-value
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 6-211 7.03e-142

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: 394.20  E-value: 7.03e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432   6 ATQESEAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCIKPVASGLREKWDDNVSS 85
Cdd:cd08903   3 YAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPAAGGLRVKWDQNVKD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  86 FEIVQSITDMLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08903  83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPVPG 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21218432 166 DPNKTNLVTFFQTDLSGYLPQSVVDSFFPRSMAEFYPNLQKAVRKF 211
Cdd:cd08903 163 EPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKAL 208
START pfam01852
START domain;
11-200 5.47e-21

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 86.30  E-value: 5.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432    11 EAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTP----EEVWDcikpvASGLREKWDDNVSSF 86
Cdd:pfam01852   5 EAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAallvAELLK-----DMEYRAQWDKDVRSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432    87 EIVQSITDMLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGd 166
Cdd:pfam01852  80 ETLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGN- 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 21218432   167 pNKTNLVTFFQTDLSGYLPQSVVDSFFPRSMAEF 200
Cdd:pfam01852 159 -GPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEG 191
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 8-210 1.11e-20

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 85.56  E-value: 1.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432      8 QESEAVAEKVLRYRRDASGWKKCREGN--GVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCIKPVaSGLREKWDDNVSS 85
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENEngDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEELMDD-LEYRPEWDKNVAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432     86 FEIVQSITDMLCVSRTSTPSAAMkLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:smart00234  80 AETLEVIDNGTVIYHYVSKFAAG-PVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 21218432    166 dpNKTNLVTFFQTDLSGYLPQSVVDSFFPRSMAEFYPNLQKAVRK 210
Cdd:smart00234 159 --GPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQK 201
 
Name Accession Description Interval E-value
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 6-211 7.03e-142

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: 394.20  E-value: 7.03e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432   6 ATQESEAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCIKPVASGLREKWDDNVSS 85
Cdd:cd08903   3 YAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPAAGGLRVKWDQNVKD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  86 FEIVQSITDMLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08903  83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPVPG 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21218432 166 DPNKTNLVTFFQTDLSGYLPQSVVDSFFPRSMAEFYPNLQKAVRKF 211
Cdd:cd08903 163 EPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKAL 208
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 6-209 4.33e-113

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: 321.33  E-value: 4.33e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432   6 ATQESEAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCIKPVASGLREKWDDNVSS 85
Cdd:cd08867   3 FKVIAEKLANEALQYINDTDGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIPPCGGLRLKWDKSLKH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  86 FEIVQSITDMLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08867  83 YEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPLKG 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 21218432 166 DPNKTNLVTFFQTDLSGYLPQSVVDSFFPRSMAEFYPNLQKAVR 209
Cdd:cd08867 163 SPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGVK 206
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 10-209 1.96e-56

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: 177.79  E-value: 1.96e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  10 SEAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCIkpVASGLREKWDDNVSSFEIV 89
Cdd:cd08904   7 AQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFM--YQPEHRIKWDKSLQVYKML 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  90 QSITDMLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGDPNK 169
Cdd:cd08904  85 QRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPENPAY 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21218432 170 TNLVTFFQTDLSGYLPQSVVDSFFPRSMAEFYPNLQKAVR 209
Cdd:cd08904 165 SKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 15-213 1.21e-45

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: 149.80  E-value: 1.21e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  15 EKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCIKPVasGLREKWDDNVSSFEIVQSITD 94
Cdd:cd00177   5 EELLELLEEPEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIPASPEQVFELLMDI--DLRKKWDKNFEEFEVIEEIDE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  95 MLCVSRTSTPSaaMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLpgDPNKTNLVT 174
Cdd:cd00177  83 HTDIIYYKTKP--PWPVSPRDFVYLRRRRKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPL--DPGKTKVTY 158

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21218432 175 FFQTDLSGYLPQSVVdsffPRSMAEFYPNLQKAVRKFHH 213
Cdd:cd00177 159 VLQVDPKGSIPKSLV----NSAAKKQLASFLKDLRKAKK 193
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 27-209 3.25e-44

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: 146.64  E-value: 3.25e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  27 WKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCIKPvaSGLREKWDDNVSSFEIVQSITDMLCVSRTSTPSA 106
Cdd:cd08902  25 WRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRP--GPYRLDWDSLMTSMDIIEEFEENCCVMRYTTAGQ 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432 107 AMKLISPRDFVDLVLVKKYEDGTISSNAThVEHPlcPPKPGFVRGFNHPCGCFCEPLPGDPNKTNLVTFFQTDLSGYLPQ 186
Cdd:cd08902 103 LLNIISPREFVDFSYTTQYEDGLLSCGVS-IEYE--EARPNFVRGFNHPCGWFCVPLKDNPSHSLLTGYIQTDLRGMLPQ 179

                       170       180
                ....*....|....*....|...
gi 21218432 187 SVVDSFFPRSMAEFYPNLQKAVR 209
Cdd:cd08902 180 SAVDTAMASTLVNFYSDLKKALK 202
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 25-206 3.50e-32

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: 115.53  E-value: 3.50e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  25 SGWKK-CREGNGVSISWRpSEEFPGNLYRGEGILCGTPEEVWD--CIKPVASGLrekWDDNVSSFEIVQSITDMLCVSRT 101
Cdd:cd08868  24 PGWKLeKNTTWGDVVYSR-NVPGVGKVFRLTGVLDCPAEFLYNelVLNVESLPS---WNPTVLECKIIQVIDDNTDISYQ 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432 102 STPSAAMKLISPRDFVDLVLVKKYEDGTISSnATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGDPNKTNLVTFFQTDLS 181
Cdd:cd08868 100 VAAEAGGGLVSPRDFVSLRHWGIRENCYLSS-GVSVEHPAMPPTKNYVRGENGPGCWILRPLPNNPNKCNFTWLLNTDLK 178

                       170       180
                ....*....|....*....|....*
gi 21218432 182 GYLPQSVVDSFFPRSMAEFYPNLQK 206
Cdd:cd08868 179 GWLPQYLVDQALASVLLDFMKHLRK 203
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 1-206 7.80e-22

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: 88.74  E-value: 7.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432   1 MDPSWATQESEAVaEKVLRYRRDASGWKKcrEGNGVSISWRPSEEFP--GNLYRGEGILCGTPEEVWdcikpvaSGLREK 78
Cdd:cd08905   2 AEMSYIKQGEEAL-QKSLSILQDQEGWKT--EIVAENGDKVLSKVVPdiGKVFRLEVVVDQPLDNLY-------SELVDR 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  79 ------WDDNVSSFEIVQSITDMLCVSRTSTPSAAMKLISPRDFVDlVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGF 152
Cdd:cd08905  72 meqmgeWNPNVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVS-VRCAKRRGSTCVLAGMATHFGLMPEQKGFIRAE 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21218432 153 NHPCGCFCEPLPGDPNKTNLVTFFQTDLSGYLPQSVVDSFFPRSMAEFYPNLQK 206
Cdd:cd08905 151 NGPTCIVLRPLAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQ 204
START pfam01852
START domain;
11-200 5.47e-21

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 86.30  E-value: 5.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432    11 EAVAEKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTP----EEVWDcikpvASGLREKWDDNVSSF 86
Cdd:pfam01852   5 EAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAallvAELLK-----DMEYRAQWDKDVRSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432    87 EIVQSITDMLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGd 166
Cdd:pfam01852  80 ETLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGN- 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 21218432   167 pNKTNLVTFFQTDLSGYLPQSVVDSFFPRSMAEF 200
Cdd:pfam01852 159 -GPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEG 191
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 8-210 1.11e-20

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 85.56  E-value: 1.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432      8 QESEAVAEKVLRYRRDASGWKKCREGN--GVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCIKPVaSGLREKWDDNVSS 85
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENEngDEVRSIFSPGRKPGEAFRLVGVVPMVCADLVEELMDD-LEYRPEWDKNVAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432     86 FEIVQSITDMLCVSRTSTPSAAMkLISPRDFVDLVLVKKYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:smart00234  80 AETLEVIDNGTVIYHYVSKFAAG-PVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLIEPLGN 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 21218432    166 dpNKTNLVTFFQTDLSGYLPQSVVDSFFPRSMAEFYPNLQKAVRK 210
Cdd:smart00234 159 --GPSKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQK 201
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 79-209 5.08e-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: 81.45  E-value: 5.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  79 WDDNVSSFEIVQSITDMLCVSRTSTPSAAMKLISPRDFVDLVLVKKYEDGTISSNAThVEHPLCPPKPGFVRGFNHPCGC 158
Cdd:cd08906  78 WNKTVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGIS-TTHSHKPPLSKYVRGENGPGGF 156

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21218432 159 FCEPLPGDPNKTNLVTFFQTDLSGYLPQSVVDSFFPRSMAEFYPNLQKAVR 209
Cdd:cd08906 157 VVLKSASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIR 207
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 15-211 1.13e-14

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: 69.98  E-value: 1.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  15 EKVLRYRRDASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCG-TPEEVWDCIkpVASGLREKWDDNV-SSFEIVQsi 92
Cdd:cd08871  13 EEFKKLCDSTDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDvPAETLYDVL--HDPEYRKTWDSNMiESFDICQ-- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  93 tdmLCVSRT-STPSAAM-KLISPRDFVDLVLVKKYEDGTISSNaTHVEHPLCPPKPGFVRGFNHPCGCFCEPLPgdPNKT 170
Cdd:cd08871  89 ---LNPNNDiGYYSAKCpKPLKNRDFVNLRSWLEFGGEYIIFN-HSVKHKKYPPRKGFVRAISLLTGYLIRPTG--PKGC 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21218432 171 NLVTFFQTDLSGYLPQSVVDS----FFPRSMAefypNLQKAVRKF 211
Cdd:cd08871 163 TLTYVTQNDPKGSLPKWVVNKattkLAPKVMK----KLHKAALKY 203
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 23-209 7.68e-07

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176885  Cd Length: 195  Bit Score: 47.65  E-value: 7.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  23 DASGWKKCREGNGVSISWRPSEEFPGNLYRGEGILCGTPEEVWDCIKPVASglREKWDDNVSSFEIVQSITDM--LCVSR 100
Cdd:cd08876  15 PDGDWQLVKDKDGIKVYTRDVEGSPLKEFKAVAEVDASIEAFLALLRDTES--YPQWMPNCKESRVLKRTDDNerSVYTV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432 101 TSTPSAamklISPRDFV-DLVLVKKYEDGTISSNATHVEHPLcPPKPGFVR-----G---FNhpcgcfceplPGDPNKTN 171
Cdd:cd08876  93 IDLPWP----VKDRDMVlRSTTEQDADDGSVTITLEAAPEAL-PEQKGYVRiktveGqwtFT----------PLGNGKTR 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21218432 172 LVTFFQTDLSGYLPQSVVDSFFPRSMAEFYPNLQKAVR 209
Cdd:cd08876 158 VTYQAYADPGGSIPGWLANAFAKDAPYNTLENLRKQLK 195
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 24-195 2.32e-06

C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD9 (also known as KIAA1300), 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. Some members of this subfamily have N-terminal kinesin motor domains. STARD9 interacts with supervillin, a protein important for efficient cytokinesis, perhaps playing a role in coordinating microtubule motors with actin and myosin II functions at membranes. The human gene encoding STARD9 lies within a target region for LGMD2A, an autosomal recessive form of limb-girdle muscular dystrophy.


Pssm-ID: 176883  Cd Length: 205  Bit Score: 46.44  E-value: 2.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  24 ASGWKKCREGNGVSISWRPseeFPGNLYR--GEGILCGTPEEVWDCIKPvaSGLREKWDDNVSSFEIVQSITDMLCVSRT 101
Cdd:cd08874  21 TAGWSYQCLEKDVVIYYKV---FNGTYHGflGAGVIKAPLATVWKAVKD--PRTRFLYDTMIKTARIHKTFTEDICLVYL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432 102 STPSAAMKLISPRDFVDLVLVKKYEDGTISSnATHVEHPLCP-PKPGFVRGFNHPCGCFCEPLPGDPNKTNLVTFF-QTD 179
Cdd:cd08874  96 VHETPLCLLKQPRDFCCLQVEAKEGELSVVA-CQSVYDKSMPePGRSLVRGEILPSAWILEPVTVEGNQYTRVIYIaQVA 174

                       170
                ....*....|....*..
gi 21218432 180 LSGY-LPQSVVDSFFPR 195
Cdd:cd08874 175 LCGPdVPAQLLSSLSKR 191
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 76-182 1.67e-03

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: 38.35  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218432  76 REKWDDNVSSFEIVQSITDMLCVSRTSTPSAAMKliSPRDFVDLVLVKK-YEDGTISSNATH-VEHPLCPPKPGFVRGfN 153
Cdd:cd08873 102 RPEWDPHGRSCEEVKRVGEDDGIYHTTMPSLTSE--KPNDFVLLVSRRKpATDGDPYKVAFRsVTLPRVPQTPGYSRT-E 178

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 21218432 154 HPCGCFCEPLPGDP-------NKTN--LVTFFQTDLSG 182
Cdd:cd08873 179 VACAGFVIRQDCGTctevsyyNETNpkLLSYVTCNLAG 216
 
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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