ID F7CG52_HORSE Unreviewed; 908 AA.
AC F7CG52;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 3.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Low-density lipoprotein receptor {ECO:0000256|ARBA:ARBA00039475};
GN Name=LDLR {ECO:0000313|Ensembl:ENSECAP00000017564.3,
GN ECO:0000313|VGNC:VGNC:19621};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000017564.3, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000017564.3, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000017564.3,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000017564.3}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000017564.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Binds LDL, the major cholesterol-carrying lipoprotein of
CC plasma, and transports it into cells by endocytosis. In order to be
CC internalized, the receptor-ligand complexes must first cluster into
CC clathrin-coated pits. {ECO:0000256|ARBA:ARBA00037220}.
CC -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000256|ARBA:ARBA00004603}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; F7CG52; -.
DR Ensembl; ENSECAT00000021336.4; ENSECAP00000017564.3; ENSECAG00000019557.4.
DR VGNC; VGNC:19621; LDLR.
DR GeneTree; ENSGT00940000161046; -.
DR HOGENOM; CLU_008163_2_0_1; -.
DR OrthoDB; 3918101at2759; -.
DR TreeFam; TF351700; -.
DR Proteomes; UP000002281; Chromosome 7.
DR Bgee; ENSECAG00000019557; Expressed in chorionic villus and 23 other cell types or tissues.
DR ExpressionAtlas; F7CG52; baseline.
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:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 4.10.1220.10; EGF-type module; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 6.
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:SF21; LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 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; 3.
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; 6.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 2.
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 Coated pit {ECO:0000256|ARBA:ARBA00023176};
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 LDL {ECO:0000256|ARBA:ARBA00022710};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
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:UP000002281};
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:ARBA00022448}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..908
FT /note="Low-density lipoprotein receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040269517"
FT TRANSMEM 835..858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 355..394
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 440..486
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 487..529
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 576..619
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 620..664
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 762..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 27..39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 34..52
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 89..104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 109..121
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 116..134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 128..143
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 148..160
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 155..173
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 908 AA; 99586 MW; E33EA13B38651D9F CRC64;
MRLADWRLRW AMALLLVAAG AAAQGECGRR EFQCRDGKCI SYKWVCDGRA ECSDSSDEAP
ETCMSVTCMA GDFSCGGRVN RCIPQFWRCD GQVDCENGSD EQGCPPKTCA QDEFRCLDGK
CIAREFVCDA DRDCLDGSDE ASCPAPTCGP ASFQCNSSAC IPELWACDGD PDCKDGSDEW
PQRCGARDAA PPRDDSPCSA LEFHCSSGEC VHSSWRCDGD PDCRDKSDED NCAVATCQPD
EFQCSDGTCI HGSRQCDKEY DCKDMSDELG CVNVTLCEGP SKFKCRSGEC IPLDKVCNSA
RDCEDWSDEP LRQCGTNECL DNNGGCSHIC SDLKIGHECL CPEGFRLVDQ RRCEDIDECQ
DPDACSQLCV NLEGSYKCEC EAGFQLDPLT KACKATGTIA YLFFTNRHEV RKMTLDRSEY
TSLIPNLKNV VALDTEVASN RVYWSDLSQR KIYSTQIDRA PGFSSYDTVI GEDLQAPDGL
AVDWIHGNIY WTDSVLGTVS VADTKGLKRK TLFKEKDSKP RAIVVDPVHG KFIKDLGKRC
SACRFHSPGP DTGVNTSICS RSFLNPARAP QGAAPGFMYW TDWGTPAKIK KGGLNGVDIY
SLVTEDIQWP NGITLDLSGG RLYWVDSKLH SISSIDVNGG DRKTILEDKK KLAHPFSLAV
FEDKVFWTDI INEAIFSANR LTGSDIHLMA ENLLSPEDIV LFHNLTQPRG VNWCERTALH
NGGCQYLCLP APQINPRSPK FTCACPDGLV LAKDMRSCHT ETEAVATTRG PSTARPVASS
TVRPTGSSAV VGPKHTASSW SMASPELTTA ETVTVSHQAL GDAAGRGGEE RPRGVGALSI
VLPIALLIVL CFGTFLLWKN WRLKNVNSIH FDNPVYQKTT EDEVHICRSQ DGYTYPSRQM
VSLEDDVA
//
