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Low-density lipoprotein receptor (LDL receptor)

 LDLR_RAT                Reviewed;         879 AA.
P35952;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
20-DEC-2017, entry version 152.
RecName: Full=Low-density lipoprotein receptor;
Short=LDL receptor;
Flags: Precursor;
Name=Ldlr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
PubMed=2922268; DOI=10.1093/nar/17.3.1259;
Lee L.Y., Mohler W.A., Schafer B.L., Freudenberger J.S.,
Byrne-Connolly N., Eager K.B., Mosley S.T., Leighton J.K.,
Thrift R.N., Davis R.A., Tanaka R.D.;
"Nucleotide sequence of the rat low density lipoprotein receptor
cDNA.";
Nucleic Acids Res. 17:1259-1260(1989).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-717; THR-724; THR-732;
THR-733 AND SER-734, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
-!- 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 (By similarity). 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) (By similarity). {ECO:0000250|UniProtKB:P01130,
ECO:0000250|UniProtKB:P35951}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P01130}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P01131}. 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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EMBL; X13722; CAA32001.1; -; mRNA.
PIR; S03430; QRRTLD.
RefSeq; NP_786938.1; NM_175762.2.
UniGene; Rn.10483; -.
ProteinModelPortal; P35952; -.
SMR; P35952; -.
STRING; 10116.ENSRNOP00000013496; -.
iPTMnet; P35952; -.
PhosphoSitePlus; P35952; -.
PaxDb; P35952; -.
PRIDE; P35952; -.
GeneID; 300438; -.
KEGG; rno:300438; -.
UCSC; RGD:2998; rat.
CTD; 3949; -.
RGD; 2998; Ldlr.
eggNOG; ENOG410KD0U; Eukaryota.
eggNOG; ENOG410Z5FJ; LUCA.
HOGENOM; HOG000115656; -.
HOVERGEN; HBG006250; -.
InParanoid; P35952; -.
KO; K12473; -.
PhylomeDB; P35952; -.
PRO; PR:P35952; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0045177; C:apical part of cell; ISO:RGD.
GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
GO; GO:0005901; C:caveola; IDA:RGD.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0005768; C:endosome; ISO:RGD.
GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; ISO:RGD.
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:0016020; C:membrane; ISO:RGD.
GO; GO:1990666; C:PCSK9-LDLR complex; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043235; C:receptor complex; ISO:RGD.
GO; GO:0055038; C:recycling endosome membrane; IDA:RGD.
GO; GO:0036477; C:somatodendritic compartment; ISO:RGD.
GO; GO:0097443; C:sorting endosome; ISO:RGD.
GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:RGD.
GO; GO:0005041; F:low-density lipoprotein receptor activity; IMP:RGD.
GO; GO:0002020; F:protease binding; ISO:RGD.
GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; ISO:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0097242; P:amyloid-beta clearance; ISO:RGD.
GO; GO:0071398; P:cellular response to fatty acid; ISO:RGD.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISO:RGD.
GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
GO; GO:0070508; P:cholesterol import; ISO:RGD.
GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
GO; GO:0030301; P:cholesterol transport; ISO:RGD.
GO; GO:0006897; P:endocytosis; IMP:RGD.
GO; GO:0030299; P:intestinal cholesterol absorption; ISO:RGD.
GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
GO; GO:0042159; P:lipoprotein catabolic process; ISO:RGD.
GO; GO:0042157; P:lipoprotein metabolic process; ISO:RGD.
GO; GO:0007616; P:long-term memory; ISO:RGD.
GO; GO:0034383; P:low-density lipoprotein particle clearance; ISO:RGD.
GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISO:RGD.
GO; GO:0061889; P:negative regulation of astrocyte activation; ISO:RGD.
GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
GO; GO:1903979; P:negative regulation of microglial cell activation; ISO:RGD.
GO; GO:0051248; P:negative regulation of protein metabolic process; ISO:RGD.
GO; GO:0015914; P:phospholipid transport; ISO:RGD.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISO:RGD.
GO; GO:0045807; P:positive regulation of endocytosis; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
GO; GO:0010986; P:positive regulation of lipoprotein particle clearance; ISO:RGD.
GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; ISO:RGD.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISO:RGD.
GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IMP:RGD.
GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
GO; GO:0090118; P:receptor-mediated endocytosis involved in cholesterol transport; ISO:RGD.
GO; GO:2000188; P:regulation of cholesterol homeostasis; ISO:RGD.
GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:RGD.
GO; GO:0010899; P:regulation of phosphatidylcholine catabolic process; ISO:RGD.
GO; GO:0051246; P:regulation of protein metabolic process; ISO:RGD.
GO; GO:0061771; P:response to caloric restriction; ISO:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0033762; P:response to glucagon; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
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; 7.
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;
Disulfide bond; EGF-like domain; Endocytosis; Endosome; Glycoprotein;
Golgi apparatus; LDL; Lipid metabolism; Lipid transport; Lysosome;
Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat;
Signal; Steroid metabolism; Sterol metabolism; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation.
SIGNAL 1 21 {ECO:0000250|UniProtKB:P01131}.
CHAIN 22 879 Low-density lipoprotein receptor.
/FTId=PRO_0000017314.
TOPO_DOM 22 807 Extracellular.
{ECO:0000250|UniProtKB:P01131}.
TRANSMEM 808 829 Helical. {ECO:0000255}.
TOPO_DOM 830 879 Cytoplasmic.
{ECO:0000250|UniProtKB:P01130}.
DOMAIN 25 65 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 66 106 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 107 145 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 146 186 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 196 234 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 235 273 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 275 314 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 315 354 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 355 394 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 398 439 LDL-receptor class B 1.
REPEAT 440 485 LDL-receptor class B 2.
REPEAT 486 528 LDL-receptor class B 3.
REPEAT 529 572 LDL-receptor class B 4.
REPEAT 573 615 LDL-receptor class B 5.
REPEAT 616 658 LDL-receptor class B 6.
DOMAIN 663 712 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 717 788 Clustered O-linked oligosaccharides.
REGION 830 879 Required for MYLIP-triggered down-
regulation of LDLR.
{ECO:0000250|UniProtKB:P01130}.
MOTIF 842 847 NPXY motif.
{ECO:0000250|UniProtKB:P01130}.
MOD_RES 717 717 Phosphothreonine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 724 724 Phosphothreonine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 732 732 Phosphothreonine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 733 733 Phosphothreonine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 734 734 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 273 273 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 657 657 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 39 {ECO:0000250}.
DISULFID 34 52 {ECO:0000250}.
DISULFID 46 63 {ECO:0000250}.
DISULFID 68 82 {ECO:0000250}.
DISULFID 75 95 {ECO:0000250}.
DISULFID 89 104 {ECO:0000250}.
DISULFID 109 121 {ECO:0000250}.
DISULFID 116 134 {ECO:0000250}.
DISULFID 128 143 {ECO:0000250}.
DISULFID 148 160 {ECO:0000250}.
DISULFID 155 173 {ECO:0000250}.
DISULFID 167 184 {ECO:0000250}.
DISULFID 198 210 {ECO:0000250}.
DISULFID 205 223 {ECO:0000250}.
DISULFID 217 232 {ECO:0000250}.
DISULFID 237 249 {ECO:0000250}.
DISULFID 244 262 {ECO:0000250}.
DISULFID 256 271 {ECO:0000250}.
DISULFID 277 290 {ECO:0000250}.
DISULFID 285 303 {ECO:0000250}.
DISULFID 297 314 {ECO:0000250}.
DISULFID 319 330 {ECO:0000250}.
DISULFID 326 339 {ECO:0000250}.
DISULFID 341 353 {ECO:0000250}.
DISULFID 359 369 {ECO:0000250}.
DISULFID 365 378 {ECO:0000250}.
DISULFID 380 393 {ECO:0000250}.
DISULFID 667 681 {ECO:0000250}.
DISULFID 677 696 {ECO:0000250}.
DISULFID 698 711 {ECO:0000250}.
SEQUENCE 879 AA; 96622 MW; E89F354E3F7C9005 CRC64;
MSTADLMLRW AIALLLAAAG VAAEDSCGKN EFQCRDGKCI VSKWVCDGSR ECPDGSDESP
ETCMSVTCRS GEFSCGGRVS RCIPDSWRCD GRTDCENGSD ELDCSPKTCS LDEFRCQDGK
CISRQFVCDQ DWDCLDGSDE AHCAATTCGP AHFRCNSSSC IPSLWACDGD RDCDDGSDEW
PQNCGAEDTA AEVVSSPCSS LEFHCGSSEC IHRSWVCDGA ADCKDKSDEE NCAVTTCRPD
EFQCADGSCI HGSRQCDREH DCKDMSDELG CINVTQCDGP NKFKCHSGEC ISLDKVCNSA
RDCRDWSDEP IKECKTNECL DNNGGCSHIC KDLKIGYECL CPSGFRLVDG HQCEDIDECQ
EPDTCSQLCV NLEGSFKCEC RAGFHMDPHT RVCKAVGSIG FLLFTNRHEV RKMTLDRSEY
TSLIPNLKNV VALDTEVANN RIYWSDLSQR KIYSAVMDQG TSLSYDAIIS GDLHAPDGLA
VDWIHGNIYW TDSVPGTVSV ADTKGVRRRT LFREKGSRPR AIVVDPVHGF MYWTDWGTPA
KIKKGGLNGV DIYSLVTEDI QWPNGITLDL PSGRLYWVDS KLHSISSIDV NGGGRKTILE
DEKQLAHPFS LAIYEDKVYW TDVLNEAIFS ANRLTGSDVN LVAKNLMSPE DIVLFHNVTQ
PRGVNWCEAT VLPNGGCQYM CLPAPQISAH SPKFTCACPD GMLLAKDMRS CLPEVDTVPT
TQGTSTIGPV VTTSAAVSLK RKEDPSATRH KEDPSATRHN EDPSATSTSR QPGDTPELST
VESVTVSSQV QGDMAGRGDE VQRHGVGFLS IFLPIALVAL LVFGAILLWR NWRLRNINSI
NFDNPVYQKT TEDEIHICRS QDGYTYPSRQ MVSLEDDVA


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