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Conserved domains on  [gi|19526998|ref|NP_598535|]
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stAR-related lipid transfer protein 4 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 21-222 3.71e-162

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: 445.94  E-value: 3.71e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  21 SDVASISTKLQNTLIQYHSIEEDEWRVAKKAKDVTVWRKPSEEFNGYLYKAQGVMDDVVNNVIDHIRPGPWRLDWDRLMT 100
Cdd:cd08902   1 LDIASKTTKLQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998 101 SLDVLEHFEENCCVMRYTTAGQLLNIISPREFVDFSYTVGYEEGLLSCGVSVEWSETRPEFVRGYNHPCGWFCVPLKDSP 180
Cdd:cd08902  81 SMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKDNP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19526998 181 SQSLLTGYIQTDLRGMIPQSAVDTAMASTLANFYSDLRKGLR 222
Cdd:cd08902 161 SHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKKALK 202
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 21-222 3.71e-162

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: 445.94  E-value: 3.71e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  21 SDVASISTKLQNTLIQYHSIEEDEWRVAKKAKDVTVWRKPSEEFNGYLYKAQGVMDDVVNNVIDHIRPGPWRLDWDRLMT 100
Cdd:cd08902   1 LDIASKTTKLQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998 101 SLDVLEHFEENCCVMRYTTAGQLLNIISPREFVDFSYTVGYEEGLLSCGVSVEWSETRPEFVRGYNHPCGWFCVPLKDSP 180
Cdd:cd08902  81 SMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKDNP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19526998 181 SQSLLTGYIQTDLRGMIPQSAVDTAMASTLANFYSDLRKGLR 222
Cdd:cd08902 161 SHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKKALK 202
START pfam01852
START domain;
41-223 1.74e-15

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 72.05  E-value: 1.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998    41 EEDEWRVAKKAKDVTVWRKPSEEFNGYLYKAQGVMDDVVNNVIDHIRP-GPWRLDWDRLMTSLDVLEHFEENCCVMRYTT 119
Cdd:pfam01852  17 DEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKdMEYRAQWDKDVRSAETLEVISSGGDLQYYVA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998   120 AGQLLNIISPREFVDFSYTVGYEEG-LLSCGVSVEwSETRPE---FVRGYNHPCGwfCVPLKDSPSQSLLTGYIQTDLRG 195
Cdd:pfam01852  97 ALVAPSPLSPRDFVFLRYWRRLGGGvYVIVDRSVT-HPQFPPssgYVRAERLPSG--YLIQPCGNGPSKVTWVSHADLKG 173

                         170       180
                  ....*....|....*....|....*...
gi 19526998   196 MIPQSAVDTAMASTLANFYSDLRKGLRK 223
Cdd:pfam01852 174 WLPSWLLRSLYKSGMPEGAKTWVATLQR 201
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 40-223 1.76e-15

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 72.08  E-value: 1.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998     40 IEEDEWR-VAKKAKDVTVWRKPSEEFN-GYLYKAQGVMDDVVNNVIDHI-RPGPWRLDWDRLMTSLDVLEHFEENCCVMR 116
Cdd:smart00234  15 ASEEGWVlSSENENGDEVRSIFSPGRKpGEAFRLVGVVPMVCADLVEELmDDLEYRPEWDKNVAKAETLEVIDNGTVIYH 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998    117 YTTAGQLlNIISPREFVDFSYT-VGYEEGLLSCGVSV--EWSETRPEFVRGYNHPCGwFCV-PLKDSPSQslLTGYIQTD 192
Cdd:smart00234  95 YVSKFAA-GPVSPRDFVFVRYWrEDEDGSYAVVDVSVthPTSPPESGYVRAENLPSG-LLIePLGNGPSK--VTWVSHAD 170

                          170       180       190
                   ....*....|....*....|....*....|.
gi 19526998    193 LRGMIPQSAVDTAMASTLANFYSDLRKGLRK 223
Cdd:smart00234 171 LKGWLPHWLVRSLIKSGLAEFAKTLVATLQK 201
 
Name Accession Description Interval E-value
START_STARD4-like cd08902
Lipid-binding START domain of mammalian STARD4 and related proteins; This subgroup includes ...
 21-222 3.71e-162

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: 445.94  E-value: 3.71e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  21 SDVASISTKLQNTLIQYHSIEEDEWRVAKKAKDVTVWRKPSEEFNGYLYKAQGVMDDVVNNVIDHIRPGPWRLDWDRLMT 100
Cdd:cd08902   1 LDIASKTTKLQNTLIQYHSILEEEWRVAKKSKDVTVWRKPSEEFGGYLYKAQGVVEDVYNRIVDHIRPGPYRLDWDSLMT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998 101 SLDVLEHFEENCCVMRYTTAGQLLNIISPREFVDFSYTVGYEEGLLSCGVSVEWSETRPEFVRGYNHPCGWFCVPLKDSP 180
Cdd:cd08902  81 SMDIIEEFEENCCVMRYTTAGQLLNIISPREFVDFSYTTQYEDGLLSCGVSIEYEEARPNFVRGFNHPCGWFCVPLKDNP 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19526998 181 SQSLLTGYIQTDLRGMIPQSAVDTAMASTLANFYSDLRKGLR 222
Cdd:cd08902 161 SHSLLTGYIQTDLRGMLPQSAVDTAMASTLVNFYSDLKKALK 202
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 21-222 2.58e-116

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: 330.19  E-value: 2.58e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  21 SDVASISTKLQNTLIQYHSIEeDEWRVAKKAKDVTVWRKPSEEFNGYLYKAQGVMDDVVNNVIDHIRP--GPWRLDWDRL 98
Cdd:cd08867   1 MDFKVIAEKLANEALQYINDT-DGWKVLKTVKNITVSWKPSTEFTGHLYRAEGIVDALPEKVIDVIIPpcGGLRLKWDKS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  99 MTSLDVLEHFEENCCVMRYTTAGQLLNIISPREFVDFSYTVGYEEG-LLSCGVSVEWSETRP--EFVRGYNHPCGWFCVP 175
Cdd:cd08867  80 LKHYEVLEKISEDLCVGRTITPSAAMGLISPRDFVDLVYVKRYEDNqWSSSGKSVDIPERPPtpGFVRGYNHPCGYFCSP 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 19526998 176 LKDSPSQSLLTGYIQTDLRGMIPQSAVDTAMASTLANFYSDLRKGLR 222
Cdd:cd08867 160 LKGSPDKSFLVLYVQTDLRGMIPQSLVESAMPSNLVNFYTDLVKGVK 206
START_STARD5-like cd08903
Lipid-binding START domain of mammalian STARD5 and related proteins; This subgroup includes ...
 21-224 5.42e-49

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: 159.23  E-value: 5.42e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  21 SDVASISTKLQNTLIQYHSiEEDEWRVAKKAKDVTVWRKPSEEFNGYLYKAQGVMDDVVNNVIDHIRP--GPWRLDWDRL 98
Cdd:cd08903   1 MDYAELAESVADKMLLYRR-DESGWKTCRRTNEVAVSWRPSAEFAGNLYKGEGIVYATLEQVWDCLKPaaGGLRVKWDQN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  99 MTSLDVLEHFEENCCVMRYTTAGQLLNIISPREFVDFSYTVGYEEG-LLSCGVSVEWSETRPE--FVRGYNHPCGWFCVP 175
Cdd:cd08903  80 VKDFEVVEAISDDVSVCRTVTPSAAMKIISPRDFVDVVLVKRYEDGtISSNATNVEHPLCPPQagFVRGFNHPCGCFCEP 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 19526998 176 LKDSPSQSLLTGYIQTDLRGMIPQSAVDTAMASTLANFYSDLRKGLRKA 224
Cdd:cd08903 160 VPGEPDKTQLVSFFQTDLSGYLPQTVVDSFFPASMAEFYNNLTKAVKAL 208
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 41-219 1.18e-41

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: 140.17  E-value: 1.18e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  41 EEDEWRVAKKAKDVTVWRKPSEEFNGYLYKAQGVMDDVVNNVIDHIRPGPWRLDWDRLMTSLDVLEHFEENCCVMRYTTA 120
Cdd:cd00177  13 EPEGWKLVKEKDGVKIYTKPYEDSGLKLLKAEGVIPASPEQVFELLMDIDLRKKWDKNFEEFEVIEEIDEHTDIIYYKTK 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998 121 GQLLniISPREFVDFSYTVGYEEGL-LSCGVSVEW--SETRPEFVRGYNHPCGWFCVPLkdSPSQSLLTGYIQTDLRGMI 197
Cdd:cd00177  93 PPWP--VSPRDFVYLRRRRKLDDGTyVIVSKSVDHdsHPKEKGYVRAEIKLSGWIIEPL--DPGKTKVTYVLQVDPKGSI 168

                       170       180
                ....*....|....*....|..
gi 19526998 198 PQSAVDTAMASTLANFYSDLRK 219
Cdd:cd00177 169 PKSLVNSAAKKQLASFLKDLRK 190
START_STARD6-like cd08904
Lipid-binding START domain of mammalian STARD6 and related proteins; This subgroup includes ...
 22-222 2.32e-39

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: 134.65  E-value: 2.32e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  22 DVASISTKLQNTLIQYhSIEEDEWRVAKKAKDVTVWRKPSEEFNGYLYKAQGVMDDVVNNVIDHIRPGPWRLDWDRLMTS 101
Cdd:cd08904   2 DFKKIAQETSQEVLGY-SRDTSGWKVVKTSKKITVSWKPSRKYHGNLYRVEGIIPESPAKLIQFMYQPEHRIKWDKSLQV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998 102 LDVLEHFEENCCVMRYTTAGQLLNIISPREFVDFSYTVGYE-EGLLSCGVSVEWSETRPE--FVRGYNHPCGWFCVPLKD 178
Cdd:cd08904  81 YKMLQRIDSDTFICHTITQSFAMGSISPRDFVDLVHIKRYEgNMNIVSSVSVEYPQCPPSsnYIRGYNHPCGYVCSPLPE 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19526998 179 SPSQSLLTGYIQTDLRGMIPQSAVDTAMASTLANFYSDLRKGLR 222
Cdd:cd08904 161 NPAYSKLVMFVQPELRGNLSRSVIEKTMPTNLVNLILDAKDGIK 204
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 28-219 4.55e-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: 92.42  E-value: 4.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  28 TKLQNTLIQYHSIEEDE-WRVAKKAKDVTVWRKPSEEFNGYLYKAQGVMD----DVVNNVIDHIRPGPwrlDWDRLMTSL 102
Cdd:cd08868   8 KQGAEALARAWSILTDPgWKLEKNTTWGDVVYSRNVPGVGKVFRLTGVLDcpaeFLYNELVLNVESLP---SWNPTVLEC 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998 103 DVLEHFEENCCVMRYTTAGQLLNIISPREFVDFSYTVGYEEGLLSCGVSVEWSE--TRPEFVRGYNHPCGWFCVPLKDSP 180
Cdd:cd08868  85 KIIQVIDDNTDISYQVAAEAGGGLVSPRDFVSLRHWGIRENCYLSSGVSVEHPAmpPTKNYVRGENGPGCWILRPLPNNP 164

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19526998 181 SQSLLTGYIQTDLRGMIPQSAVDTAMASTLANFYSDLRK 219
Cdd:cd08868 165 NKCNFTWLLNTDLKGWLPQYLVDQALASVLLDFMKHLRK 203
START_STARD3-like cd08906
Cholesterol-binding START domain of mammalian STARD3 and related proteins; This subgroup ...
 95-222 7.78e-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: 72.97  E-value: 7.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  95 WDRLMTSLDVLEHFEENCCVMRYTTAGQLLNIISPREFVDFSYTVGYEEGLLSCGVSVEWSETRP--EFVRGYNHPCGWF 172
Cdd:cd08906  78 WNKTVSACQVLQRVDDNTLVSYDVAAGAAGGVVSPRDFVNVRRIERRRDRYVSAGISTTHSHKPPlsKYVRGENGPGGFV 157

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 19526998 173 CVPLKDSPSQSLLTGYIQTDLRGMIPQSAVDTAMASTLANFYSDLRKGLR 222
Cdd:cd08906 158 VLKSASNPSVCTFIWILNTDLKGRLPRYLIHQSLAATMFEFASHLRQRIR 207
START pfam01852
START domain;
41-223 1.74e-15

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 72.05  E-value: 1.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998    41 EEDEWRVAKKAKDVTVWRKPSEEFNGYLYKAQGVMDDVVNNVIDHIRP-GPWRLDWDRLMTSLDVLEHFEENCCVMRYTT 119
Cdd:pfam01852  17 DEPGWVLLSSNENGDVVLQIVEPDHGEASRASGVVPMVAALLVAELLKdMEYRAQWDKDVRSAETLEVISSGGDLQYYVA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998   120 AGQLLNIISPREFVDFSYTVGYEEG-LLSCGVSVEwSETRPE---FVRGYNHPCGwfCVPLKDSPSQSLLTGYIQTDLRG 195
Cdd:pfam01852  97 ALVAPSPLSPRDFVFLRYWRRLGGGvYVIVDRSVT-HPQFPPssgYVRAERLPSG--YLIQPCGNGPSKVTWVSHADLKG 173

                         170       180
                  ....*....|....*....|....*...
gi 19526998   196 MIPQSAVDTAMASTLANFYSDLRKGLRK 223
Cdd:pfam01852 174 WLPSWLLRSLYKSGMPEGAKTWVATLQR 201
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 40-223 1.76e-15

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 72.08  E-value: 1.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998     40 IEEDEWR-VAKKAKDVTVWRKPSEEFN-GYLYKAQGVMDDVVNNVIDHI-RPGPWRLDWDRLMTSLDVLEHFEENCCVMR 116
Cdd:smart00234  15 ASEEGWVlSSENENGDEVRSIFSPGRKpGEAFRLVGVVPMVCADLVEELmDDLEYRPEWDKNVAKAETLEVIDNGTVIYH 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998    117 YTTAGQLlNIISPREFVDFSYT-VGYEEGLLSCGVSV--EWSETRPEFVRGYNHPCGwFCV-PLKDSPSQslLTGYIQTD 192
Cdd:smart00234  95 YVSKFAA-GPVSPRDFVFVRYWrEDEDGSYAVVDVSVthPTSPPESGYVRAENLPSG-LLIePLGNGPSK--VTWVSHAD 170

                          170       180       190
                   ....*....|....*....|....*....|.
gi 19526998    193 LRGMIPQSAVDTAMASTLANFYSDLRKGLRK 223
Cdd:smart00234 171 LKGWLPHWLVRSLIKSGLAEFAKTLVATLQK 201
START_STARD1-like cd08905
Cholesterol-binding START domain of mammalian STARD1 and related proteins; This subgroup ...
 66-221 1.97e-12

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: 63.70  E-value: 1.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  66 GYLYKAQGVMDDVVNNV-------IDHIRpgpwrlDWDRLMTSLDVLEHFEENCCVMRYTTAGQLLNIISPREFVDFSYT 138
Cdd:cd08905  48 GKVFRLEVVVDQPLDNLyselvdrMEQMG------EWNPNVKEVKILQRIGKDTLITHEVAAETAGNVVGPRDFVSVRCA 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998 139 VGYEEGLLSCGVSVEWSETRP--EFVRGYNHPCGWFCVPLKDSPSQSLLTGYIQTDLRGMIPQSAVDTAMASTLANFYSD 216
Cdd:cd08905 122 KRRGSTCVLAGMATHFGLMPEqkGFIRAENGPTCIVLRPLAGDPSKTKLTWLLSIDLKGWLPKSIINQVLSQTQVDFANH 201


                ....*
gi 19526998 217 LRKGL 221
Cdd:cd08905 202 LRQRM 206
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 41-206 2.36e-04

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: 40.70  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  41 EEDEWRVAKKAKDVTVWRKPSEEFNGYLYKAQGVMDDVVNNVI-DHIRPGPWRLDWDRLMTSLDVLEHFEENCCVMRYtt 119
Cdd:cd08871  21 STDGWKLKYNKNNVKVWTKNPENSSIKMIKVSAIFPDVPAETLyDVLHDPEYRKTWDSNMIESFDICQLNPNNDIGYY-- 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998 120 AGQLLNIISPREFVDFSYTVGYEEGLLSCGVSVEWSE--TRPEFVRGYNHPCGWFCVPLkdSPSQSLLTgYI-QTDLRGM 196
Cdd:cd08871  99 SAKCPKPLKNRDFVNLRSWLEFGGEYIIFNHSVKHKKypPRKGFVRAISLLTGYLIRPT--GPKGCTLT-YVtQNDPKGS 175

                       170
                ....*....|
gi 19526998 197 IPQSAVDTAM 206
Cdd:cd08871 176 LPKWVVNKAT 185
START_STARD9-like cd08874
C-terminal START domain of mammalian STARD9, and related domains; lipid binding; This ...
 45-189 8.41e-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: 39.13  E-value: 8.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526998  45 WRVAKKAKDVTVWRKPseeFNG--YLYKAQGVMDDVVNNVIDHIR-PGPWRLdWDRLMTSLDVLEHFEENCCVMRYTTAG 121
Cdd:cd08874  24 WSYQCLEKDVVIYYKV---FNGtyHGFLGAGVIKAPLATVWKAVKdPRTRFL-YDTMIKTARIHKTFTEDICLVYLVHET 99

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19526998 122 QLLNIISPREFVdfSYTVGYEEGLLSCGV--SVEWS---ETRPEFVRGYNHPCGWFCVPLKDSPSQSLLTGYI 189
Cdd:cd08874 100 PLCLLKQPRDFC--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.
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