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Low-density lipoprotein receptor (LDL receptor)

 LDLR_BOVIN              Reviewed;         845 AA.
P01131; F1MZ58;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
30-NOV-2016, sequence version 2.
23-MAY-2018, entry version 134.
RecName: Full=Low-density lipoprotein receptor;
Short=LDL receptor;
Flags: Precursor;
Name=LDLR;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Hereford;
PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C.,
Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S.,
Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
"A whole-genome assembly of the domestic cow, Bos taurus.";
Genome Biol. 10:R42.01-R42.10(2009).
[2]
PROTEIN SEQUENCE OF 22-37, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=6313699; DOI=10.1083/jcb.97.5.1635;
Schneider W.J., Slaughter C.J., Goldstein J.L., Anderson R.G.,
Capra J.D., Brown M.S.;
"Use of antipeptide antibodies to demonstrate external orientation of
the NH2-terminus of the low density lipoprotein receptor in the plasma
membrane of fibroblasts.";
J. Cell Biol. 97:1635-1640(1983).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 582-845.
PubMed=6327078; DOI=10.1016/0092-8674(84)90388-X;
Russell D.W., Schneider W.J., Yamamoto T., Luskey K.L., Brown M.S.,
Goldstein J.L.;
"Domain map of the LDL receptor: sequence homology with the epidermal
growth factor precursor.";
Cell 37:577-585(1984).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 644-679.
PubMed=6143315; DOI=10.1073/pnas.80.24.7501;
Russell D.W., Yamamoto T., Schneider W.J., Slaughter C.J., Brown M.S.,
Goldstein J.L.;
"cDNA cloning of the bovine low density lipoprotein receptor: feedback
regulation of a receptor mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 80:7501-7505(1983).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 644-679.
PubMed=3755212; DOI=10.1016/0076-6879(86)28113-6;
Russell D.W., Yamamoto T.;
"Molecular cloning of bovine LDL receptor cDNAs.";
Methods Enzymol. 128:895-909(1986).
-!- FUNCTION: Binds LDL, the major cholesterol-carrying lipoprotein of
plasma, and transports it into cells by endocytosis. In order to
be internalized, the receptor-ligand complexes must first cluster
into clathrin-coated pits. {ECO:0000250|UniProtKB:P01130}.
-!- SUBUNIT: Interacts (via NPXY motif) with DAB2 (via PID domain);
the interaction is impaired by tyrosine phosphorylation of the
NPXY motif. Interacts (via NPXY motif) with LDLRAP1 (via PID
domain). Interacts with ARRB1. Interacts with SNX17. Interacts
with the full-length immature form of PCSK9 (via C-terminus).
{ECO:0000250|UniProtKB:P01130}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:6313699};
Single-pass type I membrane protein {ECO:0000269|PubMed:6313699}.
Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P01130}.
Golgi apparatus {ECO:0000250|UniProtKB:P01130}. Early endosome
{ECO:0000250|UniProtKB:P01130}. Late endosome
{ECO:0000250|UniProtKB:P01130}. Lysosome
{ECO:0000250|UniProtKB:P01130}. Note=Rapidly endocytosed upon
ligand binding. {ECO:0000250|UniProtKB:P01130}.
-!- DOMAIN: The NPXY motif mediates the interaction with the clathrin
adapter DAB2 and with LDLRAP1 which are involved in receptor
internalization. A few residues outside the motif also play a role
in the interaction. {ECO:0000250|UniProtKB:P01130}.
-!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P01130}.
-!- PTM: Ubiquitinated by MYLIP leading to degradation.
{ECO:0000250|UniProtKB:P01130}.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DAAA02019482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; K01830; AAA30618.1; -; mRNA.
EMBL; K01429; AAA30620.1; -; mRNA.
EMBL; M29843; AAA30619.1; -; mRNA.
PIR; A01384; QRBOLD.
RefSeq; NP_001160002.1; NM_001166530.1.
UniGene; Bt.3562; -.
ProteinModelPortal; P01131; -.
SMR; P01131; -.
STRING; 9913.ENSBTAP00000016342; -.
PaxDb; P01131; -.
PRIDE; P01131; -.
Ensembl; ENSBTAT00000016342; ENSBTAP00000016342; ENSBTAG00000012314.
GeneID; 281276; -.
KEGG; bta:281276; -.
CTD; 3949; -.
eggNOG; ENOG410KD0U; Eukaryota.
eggNOG; ENOG410Z5FJ; LUCA.
GeneTree; ENSGT00760000118968; -.
HOGENOM; HOG000115656; -.
HOVERGEN; HBG006250; -.
InParanoid; P01131; -.
KO; K12473; -.
OMA; INVTLCE; -.
OrthoDB; EOG091G01MX; -.
TreeFam; TF351700; -.
Reactome; R-BTA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-BTA-8856828; Clathrin-mediated endocytosis.
Reactome; R-BTA-8964026; Chylomicron clearance.
Reactome; R-BTA-8964038; LDL clearance.
Proteomes; UP000009136; Chromosome 7.
Bgee; ENSBTAG00000012314; -.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0005901; C:caveola; IDA:AgBase.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; ISS:UniProtKB.
GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0005771; C:multivesicular body; IDA:AgBase.
GO; GO:1990666; C:PCSK9-LDLR complex; IEA:Ensembl.
GO; GO:0043235; C:receptor complex; IEA:Ensembl.
GO; GO:0036477; C:somatodendritic compartment; IEA:Ensembl.
GO; GO:0097443; C:sorting endosome; IEA:Ensembl.
GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IEA:Ensembl.
GO; GO:0097242; P:amyloid-beta clearance; IEA:Ensembl.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0070508; P:cholesterol import; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0030299; P:intestinal cholesterol absorption; IEA:Ensembl.
GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
GO; GO:0007616; P:long-term memory; IEA:Ensembl.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:1905907; P:negative regulation of amyloid fibril formation; IEA:Ensembl.
GO; GO:0061889; P:negative regulation of astrocyte activation; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:1903979; P:negative regulation of microglial cell activation; IEA:Ensembl.
GO; GO:0015914; P:phospholipid transport; IEA:Ensembl.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; IEA:Ensembl.
GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
GO; GO:0010986; P:positive regulation of lipoprotein particle clearance; IEA:Ensembl.
GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; IEA:Ensembl.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:Ensembl.
GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; IEA:Ensembl.
GO; GO:0090181; P:regulation of cholesterol metabolic process; IEA:Ensembl.
GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; IEA:Ensembl.
GO; GO:0061771; P:response to caloric restriction; IEA:Ensembl.
CDD; cd00112; LDLa; 6.
Gene3D; 2.120.10.30; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00057; Ldl_recept_a; 7.
Pfam; PF00058; Ldl_recept_b; 5.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 4.
SMART; SM00179; EGF_CA; 2.
SMART; SM00192; LDLa; 7.
SMART; SM00135; LY; 5.
SUPFAM; SSF57184; SSF57184; 2.
SUPFAM; SSF57424; SSF57424; 6.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS01209; LDLRA_1; 7.
PROSITE; PS50068; LDLRA_2; 7.
PROSITE; PS51120; LDLRB; 5.
1: Evidence at protein level;
Cell membrane; Cholesterol metabolism; Coated pit; Complete proteome;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Endocytosis; Endosome; Glycoprotein; Golgi apparatus; LDL;
Lipid metabolism; Lipid transport; Lysosome; Membrane; Receptor;
Reference proteome; Repeat; Signal; Steroid metabolism;
Sterol metabolism; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation.
SIGNAL 1 21 {ECO:0000269|PubMed:6313699}.
CHAIN 22 845 Low-density lipoprotein receptor.
/FTId=PRO_0000191075.
TOPO_DOM 22 774 Extracellular.
{ECO:0000269|PubMed:6313699}.
TRANSMEM 775 795 Helical. {ECO:0000255}.
TOPO_DOM 796 845 Cytoplasmic.
{ECO:0000250|UniProtKB:P01130}.
DOMAIN 26 64 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 67 105 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 108 144 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 147 185 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 198 234 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 237 273 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 277 316 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 316 355 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 356 388 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 441 487 LDL-receptor class B 1.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 488 530 LDL-receptor class B 2.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 531 574 LDL-receptor class B 3.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 575 619 LDL-receptor class B 4.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REPEAT 620 660 LDL-receptor class B 5.
{ECO:0000255|PROSITE-ProRule:PRU00461}.
REGION 712 753 Clustered O-linked oligosaccharides.
{ECO:0000255}.
REGION 796 845 Required for MYLIP-triggered down-
regulation of LDLR.
{ECO:0000250|UniProtKB:P01130}.
MOTIF 808 813 NPXY motif.
{ECO:0000250|UniProtKB:P01130}.
CARBOHYD 659 659 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 39 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 34 52 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 46 63 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 68 82 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 75 95 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 89 104 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 109 121 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 116 134 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 128 143 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 148 160 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 155 173 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 167 184 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 199 211 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 206 224 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 218 233 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 238 250 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 245 263 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 257 272 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 278 291 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 286 304 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 298 315 {ECO:0000255|PROSITE-ProRule:PRU00124}.
DISULFID 320 331 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 327 340 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 342 354 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 360 370 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 366 379 {ECO:0000255|PROSITE-ProRule:PRU00076}.
CONFLICT 760 760 I -> V (in Ref. 3; AAA30618).
{ECO:0000305}.
SEQUENCE 845 AA; 92869 MW; 5EB7D1F939DEBF10 CRC64;
MRLAGWGLRW AIALLIAVGE AAVEDNCGRN EFQCQDGKCI SYKWVCDGTA ECQDGSDESQ
ETCKSVTCKM GDFSCGGRVN RCISGSWRCD GQVDCENGSD EEGCSPKTCS QDEFRCNDGK
CIAPKFVCDL DLDCLDGSDE ASCPMPTCGP ANFQCNSSMC IPQLWACDGD PDCDDGSDEW
PKHCGTPHPS GPLQDNNPCS ALEFHCGSGE CIHSSWHCDH DPDCKDKSDE ENCAVATCRP
DEFQCSDGTC IHGSRQCDRE PDCKDLSDEL GCVNVTLCEG PNKFKCQSGE CISLDKVCNS
VRDCRDWSDE PLKDCGTNEC LDNKGGCSHI CNDLKIGYEC LCPEGFQLVG KHRCEDIDEC
QNPDTCSQLC VNLEGSYKCE CEEGFRLEPL TKACKAVGTI AYLFFTNRHE VRKMTLDRSE
YTSLIPNLKN VVALDTEVAS NRIYWSDLSQ RKIYSAQIDG APGFSSYDTV IGEDLQAPDG
LAVDWIHSNI YWTDSILGTV SVADTKGVKR KTLFQEEGSK PRAIVVDPVH GFMYWTDWGA
PAEIKKGGLN GVDVYSLVTE DIQWPNGITL DLSGGRLYWV DSKLHSISSI DVNGGNRKTV
LEDKKKLAHP FSLAIFEDKV FWTDVINEAI FSANRLTGSD ISLMAENLLS PEDIVLFHNL
TQPRGVNWCE RTALRNGGCQ YLCLPAPQIN PRSPKFTCAC PDGMLLAKDM RSCLTESESA
VTTRGPSTVS STAVGPKRTA SPELTTAESV TMSQQGQGDI ASQADTERPG SVGALYIVLP
IALLILLAFG TFLLWKNWRL KSINSINFDN PVYQKTTEDE VHICRSQDGY TYPSRQMVSL
EDDVA


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