ID A0A287CV30_ICTTR Unreviewed; 804 AA.
AC A0A287CV30;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Very low density lipoprotein receptor {ECO:0000313|Ensembl:ENSSTOP00000025123.1};
GN Name=VLDLR {ECO:0000313|Ensembl:ENSSTOP00000025123.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000025123.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000025123.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AGTP01031842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01031843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A287CV30; -.
DR Ensembl; ENSSTOT00000034756.1; ENSSTOP00000025123.1; ENSSTOG00000006880.3.
DR GeneTree; ENSGT00940000155460; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF8; VERY LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 2.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS51120; LDLRB; 4.
PE 4: Predicted;
KW Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..804
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012335000"
FT TRANSMEM 729..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 355..390
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 440..483
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 484..526
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 527..570
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 571..615
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DISULFID 33..45
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 40..58
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 52..67
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 72..84
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 79..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 113..125
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 120..138
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 132..147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 152..164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 159..177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 198..210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 205..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 217..232
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 237..249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 244..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 256..271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 285..303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 359..369
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 804 AA; 88840 MW; 2D27B355119644B6 CRC64;
MGTSARWALW LLLALCWAPA DSGATGAGRK AKCEPSQFQC TNGRCITLLW KCDGDEDCVD
GSDEKNCVKK TCAESDFVCN NGQCVPNRWQ CDGDPDCEDG SDESPEQCRN ITCSPDEFTC
SSGRCISRNF VCNGQDDCND GSDELDCAPP TCGAHEFQCS TSSCIPISWV CDDDADCSDQ
SDESLEQCGR QPVIHTKCPA SEIQCGSGEC IHKKWRCDGD PDCKDGSDEV NCPSRTCRPD
QFECEDGGCI HGSRQCNGIR DCVDGSDEVN CKNVNQCLGP GKFKCRSGEC IDISKVCNQE
QDCRDWSDEP LKECHVNECL VNNGGCSHIC KDLVIGYECD CAAGFELIDR KTCGDIDECQ
NPGICSQICI NLKGGYKCEC SRGYQMDLAT GVCKAVGKEP SLIFTNRRDI RKIGLERKEY
IQLVEQLRNT VALDADIAAQ KLFWADLSQK AIFSASIDDK VGRHVKMIDN VYNPAAIAVD
WVYKTIYWTD AASKTISVAT LDGTKRKFLF NSDLREPASI AVDPLSGFVY WSDWGEPAKI
EKAGMNGFDR RPLVTADIQW PNGITLDLIK SRLYWLDSKL HMLSSVDLNG QDRRIVLKSL
EFLAHPLALT IFEDRVYWID GENEAVYGAN KFTGSELATL VNNLNDAQDI IVYHELVQPS
GKNWCEDDME NGGCEYLCLP APQINDHSPK YTCSCPNGYN LEENGRECQR INVTTAVSEV
SVPPKGTSAA WAILPLLLLV MAAVGGYLMW RNWQHKNMKS MNFDNPVYLK TTEEDLSIDI
GRHSASVGHT YPAISVVSTD DDLA
//
