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Conserved domains on  [gi|32526915|ref|NP_871629|]
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stAR-related lipid transfer protein 5 [Homo sapiens]

Protein Classification

StAR-related lipid transfer protein 5( domain architecture ID 10172355)

StAR-related lipid transfer protein 5 (STARD5) may be involved in the intracellular transport of sterols or other lipids

Gene Symbol:  STARD5
Gene Ontology:  GO:0008289|GO:0120020|GO:0070508
PubMed:  31927098|18922149

Graphical summary

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List of domain hits

 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 1.22e-155

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: 429.26  E-value: 1.22e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915   6 AAQMSEAVAEKMLQYRRDTAGWKICREGNGVSVSWRPSVEFPGNLYRGEGIVYGTLEEVWDCVKPAVGGLRVKWDENVTG 85
Cdd:cd08903   3 YAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPAAGGLRVKWDQNVKD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  86 FEIIQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKRYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08903  83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPVPG 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 32526915 166 EPTKTNLVTFFHTDLSGYLPQNVVDSFFPRSMTRFYANLQKAVKQF 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 1.22e-155

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: 429.26  E-value: 1.22e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915   6 AAQMSEAVAEKMLQYRRDTAGWKICREGNGVSVSWRPSVEFPGNLYRGEGIVYGTLEEVWDCVKPAVGGLRVKWDENVTG 85
Cdd:cd08903   3 YAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPAAGGLRVKWDQNVKD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  86 FEIIQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKRYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08903  83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPVPG 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 32526915 166 EPTKTNLVTFFHTDLSGYLPQNVVDSFFPRSMTRFYANLQKAVKQF 211
Cdd:cd08903 163 EPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKAL 208
START pfam01852
START domain;
11-197 1.45e-22

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 90.54  E-value: 1.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915    11 EAVAEKMLQYRRDTAGWKICREGNGVSVSWRPSVEFPGNLYRGEGIVYGT----LEEVWDcvkpaVGGLRVKWDENVTGF 86
Cdd:pfam01852   5 EAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVaallVAELLK-----DMEYRAQWDKDVRSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915    87 EIIQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKRYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGE 166
Cdd:pfam01852  80 ETLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 32526915   167 PTKTNLVTffHTDLSGYLPQNVVDSFFPRSM 197
Cdd:pfam01852 160 PSKVTWVS--HADLKGWLPSWLLRSLYKSGM 188
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 8-210 1.46e-21

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 87.87  E-value: 1.46e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915      8 QMSEAVAEKMLQYRRDTAGWKICREGN--GVSVSWRPSVEFPGNLYRGEGIVYGT----LEEVWDcvkpaVGGLRVKWDE 81
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENEngDEVRSIFSPGRKPGEAFRLVGVVPMVcadlVEELMD-----DLEYRPEWDK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915     82 NVTGFEIIQSI-TDTLCVSRTStpSAAMKLISPRDFVDLVLVKRYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFC 160
Cdd:smart00234  76 NVAKAETLEVIdNGTVIYHYVS--KFAAGPVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLI 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 32526915    161 EPLPGEPTKtnLVTFFHTDLSGYLPQNVVDSFFPRSMTRFYANLQKAVKQ 210
Cdd:smart00234 154 EPLGNGPSK--VTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQK 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 1.22e-155

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: 429.26  E-value: 1.22e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915   6 AAQMSEAVAEKMLQYRRDTAGWKICREGNGVSVSWRPSVEFPGNLYRGEGIVYGTLEEVWDCVKPAVGGLRVKWDENVTG 85
Cdd:cd08903   3 YAELAESVADKMLLYRRDESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPAAGGLRVKWDQNVKD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  86 FEIIQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKRYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08903  83 FEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGTISSNATNVEHPLCPPQAGFVRGFNHPCGCFCEPVPG 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 32526915 166 EPTKTNLVTFFHTDLSGYLPQNVVDSFFPRSMTRFYANLQKAVKQF 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 4.51e-127

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: 356.77  E-value: 4.51e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915   6 AAQMSEAVAEKMLQYRRDTAGWKICREGNGVSVSWRPSVEFPGNLYRGEGIVYGTLEEVWDCVKPAVGGLRVKWDENVTG 85
Cdd:cd08867   3 FKVIAEKLANEALQYINDTDGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIPPCGGLRLKWDKSLKH 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  86 FEIIQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKRYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08867  83 YEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNQWSSSGKSVDIPERPPTPGFVRGYNHPCGYFCSPLKG 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 32526915 166 EPTKTNLVTFFHTDLSGYLPQNVVDSFFPRSMTRFYANLQKAVK 209
Cdd:cd08867 163 SPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGVK 206
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 8-209 2.33e-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: 177.41  E-value: 2.33e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915   8 QMSEAVAEKMLQYRRDTAGWKICREGNGVSVSWRPSVEFPGNLYRGEGIVYGTLEEVWDCVkpAVGGLRVKWDENVTGFE 87
Cdd:cd08904   5 KIAQETSQEVLGYSRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFM--YQPEHRIKWDKSLQVYK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  88 IIQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKRYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGEP 167
Cdd:cd08904  83 MLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEGNMNIVSSVSVEYPQCPPSSNYIRGYNHPCGYVCSPLPENP 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 32526915 168 TKTNLVTFFHTDLSGYLPQNVVDSFFPRSMTRFYANLQKAVK 209
Cdd:cd08904 163 AYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 7-209 4.00e-46

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: 151.26  E-value: 4.00e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915   7 AQMSEAVAEKMLQYRR-DTAGWKICREGNGVSVSWRPSVEFPGNLYRGEGIVYGTLEEVWDCVKPavGGLRVKWDENVTG 85
Cdd:cd08902   4 ASKTTKLQNTLIQYHSiLEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRP--GPYRLDWDSLMTS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  86 FEIIQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKRYEDGTISSNAThVEHPlcPPKPGFVRGFNHPCGCFCEPLPG 165
Cdd:cd08902  82 MDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVS-IEYE--EARPNFVRGFNHPCGWFCVPLKD 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 32526915 166 EPTKTNLVTFFHTDLSGYLPQNVVDSFFPRSMTRFYANLQKAVK 209
Cdd:cd08902 159 NPSHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKKALK 202
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 15-213 4.75e-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: 148.26  E-value: 4.75e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  15 EKMLQYRRDTAGWKICREGNGVSVSWRPSVEFPGNLYRGEGIVYGTLEEVWDCVKPavGGLRVKWDENVTGFEIIQSITD 94
Cdd:cd00177   5 EELLELLEEPEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIPASPEQVFELLMD--IDLRKKWDKNFEEFEVIEEIDE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  95 TLCVSRTSTPSaaMKLISPRDFVDLVLVKRYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLpgEPTKTNLVT 174
Cdd:cd00177  83 HTDIIYYKTKP--PWPVSPRDFVYLRRRRKLDDGTYVIVSKSVDHDSHPKEKGYVRAEIKLSGWIIEPL--DPGKTKVTY 158

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 32526915 175 FFHTDLSGYLPQNVVdsffPRSMTRFYANLQKAVKQFHE 213
Cdd:cd00177 159 VLQVDPKGSIPKSLV----NSAAKKQLASFLKDLRKAKK 193
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 26-209 7.85e-34

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: 119.77  E-value: 7.85e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  26 GWKI-CREGNGVSVSWRpSVEFPGNLYRGEGIVYGTLEEVWDCVKPAVGGLrVKWDENVTGFEIIQSITDTLCVSRTSTP 104
Cdd:cd08868  25 GWKLeKNTTWGDVVYSR-NVPGVGKVFRLTGVLDCPAEFLYNELVLNVESL-PSWNPTVLECKIIQVIDDNTDISYQVAA 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915 105 SAAMKLISPRDFVDLVLVKRYEDGTISSnATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGEPTKTNLVTFFHTDLSGYL 184
Cdd:cd08868 103 EAGGGLVSPRDFVSLRHWGIRENCYLSS-GVSVEHPAMPPTKNYVRGENGPGCWILRPLPNNPNKCNFTWLLNTDLKGWL 181

                       170       180
                ....*....|....*....|....*
gi 32526915 185 PQNVVDSFFPRSMTRFYANLQKAVK 209
Cdd:cd08868 182 PQYLVDQALASVLLDFMKHLRKRIA 206
START pfam01852
START domain;
11-197 1.45e-22

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 90.54  E-value: 1.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915    11 EAVAEKMLQYRRDTAGWKICREGNGVSVSWRPSVEFPGNLYRGEGIVYGT----LEEVWDcvkpaVGGLRVKWDENVTGF 86
Cdd:pfam01852   5 EAAQELLKLALSDEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVaallVAELLK-----DMEYRAQWDKDVRSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915    87 EIIQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKRYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGE 166
Cdd:pfam01852  80 ETLEVISSGGDLQYYVAALVAPSPLSPRDFVFLRYWRRLGGGVYVIVDRSVTHPQFPPSSGYVRAERLPSGYLIQPCGNG 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 32526915   167 PTKTNLVTffHTDLSGYLPQNVVDSFFPRSM 197
Cdd:pfam01852 160 PSKVTWVS--HADLKGWLPSWLLRSLYKSGM 188
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 8-210 1.46e-21

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 87.87  E-value: 1.46e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915      8 QMSEAVAEKMLQYRRDTAGWKICREGN--GVSVSWRPSVEFPGNLYRGEGIVYGT----LEEVWDcvkpaVGGLRVKWDE 81
Cdd:smart00234   1 VAEEAAAELLKMAAASEEGWVLSSENEngDEVRSIFSPGRKPGEAFRLVGVVPMVcadlVEELMD-----DLEYRPEWDK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915     82 NVTGFEIIQSI-TDTLCVSRTStpSAAMKLISPRDFVDLVLVKRYEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFC 160
Cdd:smart00234  76 NVAKAETLEVIdNGTVIYHYVS--KFAAGPVSPRDFVFVRYWREDEDGSYAVVDVSVTHPTSPPESGYVRAENLPSGLLI 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 32526915    161 EPLPGEPTKtnLVTFFHTDLSGYLPQNVVDSFFPRSMTRFYANLQKAVKQ 210
Cdd:smart00234 154 EPLGNGPSK--VTWVSHADLKGWLPHWLVRSLIKSGLAEFAKTLVATLQK 201
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 77-209 3.24e-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: 81.83  E-value: 3.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  77 VKWDENVTGFEIIQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKRYEDGTISSNAThVEHPLCPPKPGFVRGFNHPC 156
Cdd:cd08906  76 VLWNKTVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGIS-TTHSHKPPLSKYVRGENGPG 154

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 32526915 157 GCFCEPLPGEPTKTNLVTFFHTDLSGYLPQNVVDSFFPRSMTRFYANLQKAVK 209
Cdd:cd08906 155 GFVVLKSASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIR 207
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 8-206 2.28e-17

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: 76.80  E-value: 2.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915   8 QMSEAVaEKMLQYRRDTAGWKicREGNGVSVSWRPSVEFP--GNLYRGEGIVYGTLE----EVWDCVKpAVGglrvKWDE 81
Cdd:cd08905   9 QGEEAL-QKSLSILQDQEGWK--TEIVAENGDKVLSKVVPdiGKVFRLEVVVDQPLDnlysELVDRME-QMG----EWNP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  82 NVTGFEIIQSITDTLCVSRTSTPSAAMKLISPRDFVDLVLVKRyEDGTISSNATHVEHPLCPPKPGFVRGFNHPCGCFCE 161
Cdd:cd08905  81 NVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKR-RGSTCVLAGMATHFGLMPEQKGFIRAENGPTCIVLR 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 32526915 162 PLPGEPTKTNLVTFFHTDLSGYLPQNVVDSFFPRSMTRFYANLQK 206
Cdd:cd08905 160 PLAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQ 204
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 23-213 1.93e-10

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).


Pssm-ID: 176880  Cd Length: 222  Bit Score: 58.04  E-value: 1.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  23 DTAGWKICREGNGVSVSWRPSVEFPGNLYRGEGIVYG-TLEEVWDCVKPAvgGLRVKWDENV-TGFEIIQsitdtLCVSR 100
Cdd:cd08871  21 STDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDvPAETLYDVLHDP--EYRKTWDSNMiESFDICQ-----LNPNN 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915 101 T-STPSAAM-KLISPRDFVDLVLVKRYEDGTISSNaTHVEHPLCPPKPGFVRGFNHPCGCFCEPLPGEPTKtnlVTFF-H 177
Cdd:cd08871  94 DiGYYSAKCpKPLKNRDFVNLRSWLEFGGEYIIFN-HSVKHKKYPPRKGFVRAISLLTGYLIRPTGPKGCT---LTYVtQ 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 32526915 178 TDLSGYLPQNVVDS----FFPRSMtrfyANLQKAVKQFHE 213
Cdd:cd08871 170 NDPKGSLPKWVVNKattkLAPKVM----KKLHKAALKYPE 205
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 24-175 5.77e-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: 45.29  E-value: 5.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  24 TAGWKICREGNGVSVSWRPsveFPGNLYR--GEGIVYGTLEEVWDCVKPAvgGLRVKWDENVTGFEIIQSITDTLCVSRT 101
Cdd:cd08874  21 TAGWSYQCLEKDVVIYYKV---FNGTYHGflGAGVIKAPLATVWKAVKDP--RTRFLYDTMIKTARIHKTFTEDICLVYL 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32526915 102 STPSAAMKLISPRDFVDLVLVKRYEDGTISSnATHVEHPLCP-PKPGFVRGFNHPCGCFCEPLPGEPTKTNLVTF 175
Cdd:cd08874  96 VHETPLCLLKQPRDFCCLQVEAKEGELSVVA-CQSVYDKSMPePGRSLVRGEILPSAWILEPVTVEGNQYTRVIY 169
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 25-209 5.02e-04

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: 39.56  E-value: 5.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  25 AGWKICREGNGVSVSWRPSVEFPGNLYRGEGIVYGTLEEVwdcvkpavggLRV--------KWDENVTGFEIIQSITDT- 95
Cdd:cd08876  17 GDWQLVKDKDGIKVYTRDVEGSPLKEFKAVAEVDASIEAF----------LALlrdtesypQWMPNCKESRVLKRTDDNe 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  96 -LCVSRTSTPSAamklISPRDfvdLVLVKRYE----DGTISSNATHVEHPLcPPKPGFVRgFNHPCGCFC-EPLPGEptK 169
Cdd:cd08876  87 rSVYTVIDLPWP----VKDRD---MVLRSTTEqdadDGSVTITLEAAPEAL-PEQKGYVR-IKTVEGQWTfTPLGNG--K 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 32526915 170 TNLVTFFHTDLSGYLPQNVVDSFFPRSMTRFYANLQKAVK 209
Cdd:cd08876 156 TRVTYQAYADPGGSIPGWLANAFAKDAPYNTLENLRKQLK 195
START_STARD14_15-like cd08873
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins; This subfamily ...
 76-182 2.14e-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: 37.96  E-value: 2.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32526915  76 RVKWDENVTGFEIIQSITDTLCVSRTSTPSAAMKliSPRDFVDLVLVKR-YEDGTISSNATH-VEHPLCPPKPGFVR--- 150
Cdd:cd08873 102 RPEWDPHGRSCEEVKRVGEDDGIYHTTMPSLTSE--KPNDFVLLVSRRKpATDGDPYKVAFRsVTLPRVPQTPGYSRtev 179

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 32526915 151 ---GF--NHPCGCFCEPLPGEPTKTNLVTFFHTDLSG 182
Cdd:cd08873 180 acaGFviRQDCGTCTEVSYYNETNPKLLSYVTCNLAG 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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