NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|25091316|sp|Q96DR4|]
View 

RecName: Full=StAR-related lipid transfer protein 4; AltName: Full=START domain-containing protein 4; Short=StARD4

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 5-205 6.44e-151

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 cd08902:

Pssm-ID: 472699  Cd Length: 202  Bit Score: 416.66  E-value: 6.44e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316   5 SDVASFATKLKNTLIQYHSIEEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMT 84
Cdd:cd08902   1 LDIASKTTKLQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  85 SLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRPEFVRGYNHPCGWFCVPLKDNP 164
Cdd:cd08902  81 SMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKDNP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 25091316 165 NQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 205
Cdd:cd08902 161 SHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKKAL 201
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 5-205 6.44e-151

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: 416.66  E-value: 6.44e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316   5 SDVASFATKLKNTLIQYHSIEEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMT 84
Cdd:cd08902   1 LDIASKTTKLQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  85 SLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRPEFVRGYNHPCGWFCVPLKDNP 164
Cdd:cd08902  81 SMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKDNP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 25091316 165 NQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 205
Cdd:cd08902 161 SHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKKAL 201
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 24-205 1.77e-13

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 66.30  E-value: 1.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316     24 IEEDKW--RVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDD----LVYSIIDHIRPgpcRLDWDSLMTSLDILENFEENCC 97
Cdd:smart00234  15 ASEEGWvlSSENENGDEVRSIFSPGRKPGEAFRLVGVVPMvcadLVEELMDDLEY---RPEWDKNVAKAETLEVIDNGTV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316     98 VMRYTTAGQlWNIISPREFVDFSYT-VGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV-PLKDNPnqSLLTGYI 173
Cdd:smart00234  92 IYHYVSKFA-AGPVSPRDFVFVRYWrEDEDGSYAVVDVSVTHPTSPPEsgYVRAENLPSG-LLIePLGNGP--SKVTWVS 167

                          170       180       190
                   ....*....|....*....|....*....|..
gi 25091316    174 QTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 205
Cdd:smart00234 168 HADLKGWLPHWLVRSLIKSGLAEFAKTLVATL 199
START pfam01852
START domain;
25-205 1.56e-11

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 60.88  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316    25 EEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVID----DLVYSIIDHirpGPCRLDWDSLMTSLDILENFEENCCVMR 100
Cdd:pfam01852  17 DEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPmvaaLLVAELLKD---MEYRAQWDKDVRSAETLEVISSGGDLQY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316   101 YTTAGQLWNIISPREFVDFSY-TVGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV-PLKDNPnqSLLTGYIQTD 176
Cdd:pfam01852  94 YVAALVAPSPLSPRDFVFLRYwRRLGGGVYVIVDRSVTHPQFPPSsgYVRAERLPSG-YLIqPCGNGP--SKVTWVSHAD 170

                         170       180
                  ....*....|....*....|....*....
gi 25091316   177 LRGMIPQSAVDTAMASTLTNFYGDLRKAL 205
Cdd:pfam01852 171 LKGWLPSWLLRSLYKSGMPEGAKTWVATL 199
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 5-205 6.44e-151

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: 416.66  E-value: 6.44e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316   5 SDVASFATKLKNTLIQYHSIEEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMT 84
Cdd:cd08902   1 LDIASKTTKLQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  85 SLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRPEFVRGYNHPCGWFCVPLKDNP 164
Cdd:cd08902  81 SMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKDNP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 25091316 165 NQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 205
Cdd:cd08902 161 SHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKKAL 201
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 5-205 1.01e-104

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: 299.76  E-value: 1.01e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316   5 SDVASFATKLKNTLIQYHSIEeDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRP--GPCRLDWDSL 82
Cdd:cd08867   1 MDFKVIAEKLANEALQYINDT-DGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIPpcGGLRLKWDKS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  83 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEG-LLSCGISLDWDEKRP--EFVRGYNHPCGWFCVP 159
Cdd:cd08867  80 LKHYEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNqWSSSGKSVDIPERPPtpGFVRGYNHPCGYFCSP 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 25091316 160 LKDNPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 205
Cdd:cd08867 160 LKGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGV 205
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 5-205 3.24e-46

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: 151.53  E-value: 3.24e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316   5 SDVASFATKLKNTLIQYHSiEEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRP--GPCRLDWDSL 82
Cdd:cd08903   1 MDYAELAESVADKMLLYRR-DESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPaaGGLRVKWDQN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  83 MTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEG-LLSCGISLDWDEKRPE--FVRGYNHPCGWFCVP 159
Cdd:cd08903  80 VKDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGtISSNATNVEHPLCPPQagFVRGFNHPCGCFCEP 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 25091316 160 LKDNPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 205
Cdd:cd08903 160 VPGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAV 205
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 25-205 1.29e-39

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: 134.00  E-value: 1.29e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  25 EEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMTSLDILENFEENCCVMRYTTA 104
Cdd:cd00177  13 EPEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHTDIIYYKTK 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316 105 GQLwnIISPREFVDFSYTVGYKEGL-LSCGISLDWD--EKRPEFVRGYNHPCGWFCVPLkdNPNQSLLTGYIQTDLRGMI 181
Cdd:cd00177  93 PPW--PVSPRDFVYLRRRRKLDDGTyVIVSKSVDHDshPKEKGYVRAEIKLSGWIIEPL--DPGKTKVTYVLQVDPKGSI 168

                       170       180
                ....*....|....*....|....
gi 25091316 182 PQSAVDTAMASTLTNFYGDLRKAL 205
Cdd:cd00177 169 PKSLVNSAAKKQLASFLKDLRKAK 192
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 29-202 4.88e-37

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: 127.72  E-value: 4.88e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  29 WRVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMTSLDILENFEENCCVMRYTTAGQLW 108
Cdd:cd08904  24 WKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQVYKMLQRIDSDTFICHTITQSFAM 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316 109 NIISPREFVDFSYtVGYKEGLLS--CGISLDWDEKRPE--FVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTDLRGMIPQS 184
Cdd:cd08904 104 GSISPRDFVDLVH-IKRYEGNMNivSSVSVEYPQCPPSsnYIRGYNHPCGYVCSPLPENPAYSKLVMFVQPELRGNLSRS 182

                       170
                ....*....|....*...
gi 25091316 185 AVDTAMASTLTNFYGDLR 202
Cdd:cd08904 183 VIEKTMPTNLVNLILDAK 200
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 10-203 1.66e-23

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: 92.80  E-value: 1.66e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  10 FATKLKNTLIQYHSIEEDK-WRVAKKTKDVTVWRKPSEEFNGYLYKAQGVID----DLVYSIIDHIRPGPcrlDWDSLMT 84
Cdd:cd08868   6 YLKQGAEALARAWSILTDPgWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDcpaeFLYNELVLNVESLP---SWNPTVL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  85 SLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDE--KRPEFVRGYNHPCGWFCVPLKD 162
Cdd:cd08868  83 ECKIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSVEHPAmpPTKNYVRGENGPGCWILRPLPN 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 25091316 163 NPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRK 203
Cdd:cd08868 163 NPNKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRK 203
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 79-205 2.70e-16

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: 73.74  E-value: 2.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  79 WDSLMTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGYKEGLLSCGISLDWDEKRP--EFVRGYNHPCGWF 156
Cdd:cd08906  78 WNKTVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPlsKYVRGENGPGGFV 157

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 25091316 157 CVPLKDNPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 205
Cdd:cd08906 158 VLKSASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRI 206
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 24-205 1.77e-13

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 66.30  E-value: 1.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316     24 IEEDKW--RVAKKTKDVTVWRKPSEEFNGYLYKAQGVIDD----LVYSIIDHIRPgpcRLDWDSLMTSLDILENFEENCC 97
Cdd:smart00234  15 ASEEGWvlSSENENGDEVRSIFSPGRKPGEAFRLVGVVPMvcadLVEELMDDLEY---RPEWDKNVAKAETLEVIDNGTV 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316     98 VMRYTTAGQlWNIISPREFVDFSYT-VGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV-PLKDNPnqSLLTGYI 173
Cdd:smart00234  92 IYHYVSKFA-AGPVSPRDFVFVRYWrEDEDGSYAVVDVSVTHPTSPPEsgYVRAENLPSG-LLIePLGNGP--SKVTWVS 167

                          170       180       190
                   ....*....|....*....|....*....|..
gi 25091316    174 QTDLRGMIPQSAVDTAMASTLTNFYGDLRKAL 205
Cdd:smart00234 168 HADLKGWLPHWLVRSLIKSGLAEFAKTLVATL 199
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 50-205 6.67e-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: 6.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  50 GYLYKAQGVID---DLVYS-IIDHIRPGPcrlDWDSLMTSLDILENFEENCCVMRYTTAGQLWNIISPREFVDFSYTVGY 125
Cdd:cd08905  48 GKVFRLEVVVDqplDNLYSeLVDRMEQMG---EWNPNVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCAKRR 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316 126 KEGLLSCGISLDWDEKRP--EFVRGYNHPCGWFCVPLKDNPNQSLLTGYIQTDLRGMIPQSAVDTAMASTLTNFYGDLRK 203
Cdd:cd08905 125 GSTCVLAGMATHFGLMPEqkGFIRAENGPTCIVLRPLAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANHLRQ 204


                ..
gi 25091316 204 AL 205
Cdd:cd08905 205 RM 206
START pfam01852
START domain;
25-205 1.56e-11

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 60.88  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316    25 EEDKWRVAKKTKDVTVWRKPSEEFNGYLYKAQGVID----DLVYSIIDHirpGPCRLDWDSLMTSLDILENFEENCCVMR 100
Cdd:pfam01852  17 DEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPmvaaLLVAELLKD---MEYRAQWDKDVRSAETLEVISSGGDLQY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316   101 YTTAGQLWNIISPREFVDFSY-TVGYKEGLLSCGISLDWDEKRPE--FVRGYNHPCGwFCV-PLKDNPnqSLLTGYIQTD 176
Cdd:pfam01852  94 YVAALVAPSPLSPRDFVFLRYwRRLGGGVYVIVDRSVTHPQFPPSsgYVRAERLPSG-YLIqPCGNGP--SKVTWVSHAD 170

                         170       180
                  ....*....|....*....|....*....
gi 25091316   177 LRGMIPQSAVDTAMASTLTNFYGDLRKAL 205
Cdd:pfam01852 171 LKGWLPSWLLRSLYKSGMPEGAKTWVATL 199
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 29-173 5.38e-04

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: 39.51  E-value: 5.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25091316  29 WRVAKKTKDVTVWRKPseeFNG--YLYKAQGVIDDLVYSIIDHIRPGPCRLDWDSLMTSLDILENFEENCCVMRYTTAGQ 106
Cdd:cd08874  24 WSYQCLEKDVVIYYKV---FNGtyHGFLGAGVIKAPLATVWKAVKDPRTRFLYDTMIKTARIHKTFTEDICLVYLVHETP 100

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25091316 107 LWNIISPREFVdfSYTVGYKEG---LLSCGISLDWDEKRP--EFVRGYNHPCGWFCVPLKDNPNQSLLTGYI 173
Cdd:cd08874 101 LCLLKQPRDFC--CLQVEAKEGelsVVACQSVYDKSMPEPgrSLVRGEILPSAWILEPVTVEGNQYTRVIYI 170
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH