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Protein

Low-density lipoprotein receptor

Gene

Ldlr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • low-density lipoprotein receptor activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • cholesterol metabolic process Source: UniProtKB-KW
  • endocytosis Source: RGD
  • lipid transport Source: UniProtKB-KW
  • response to estradiol Source: RGD
  • response to estrogen Source: RGD
  • response to glucagon Source: RGD
  • response to hormone Source: RGD
  • response to hypoxia Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cholesterol metabolism, Endocytosis, Lipid metabolism, Lipid transport, Steroid metabolism, Sterol metabolism, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor
Short name:
LDL receptor
Gene namesi
Name:Ldlr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2998. Ldlr.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity
  • Membraneclathrin-coated pit By similarity
  • Golgi apparatus By similarity
  • Early endosome By similarity
  • Late endosome By similarity
  • Lysosome By similarity

  • Note: Rapidly endocytosed upon ligand binding.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 807ExtracellularBy similarityAdd BLAST786
Transmembranei808 – 829HelicalSequence analysisAdd BLAST22
Topological domaini830 – 879CytoplasmicBy similarityAdd BLAST50

GO - Cellular componenti

  • caveola Source: RGD
  • cell surface Source: UniProtKB
  • clathrin-coated pit Source: UniProtKB-SubCell
  • early endosome Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • late endosome Source: UniProtKB
  • low-density lipoprotein particle Source: UniProtKB-KW
  • lysosome Source: UniProtKB
  • plasma membrane Source: RGD
  • recycling endosome membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Endosome, Golgi apparatus, LDL, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21By similarityAdd BLAST21
ChainiPRO_000001731422 – 879Low-density lipoprotein receptorAdd BLAST858

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 39By similarity
Disulfide bondi34 ↔ 52By similarity
Disulfide bondi46 ↔ 63By similarity
Disulfide bondi68 ↔ 82By similarity
Disulfide bondi75 ↔ 95By similarity
Disulfide bondi89 ↔ 104By similarity
Glycosylationi97N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi109 ↔ 121By similarity
Disulfide bondi116 ↔ 134By similarity
Disulfide bondi128 ↔ 143By similarity
Disulfide bondi148 ↔ 160By similarity
Disulfide bondi155 ↔ 173By similarity
Glycosylationi156N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi167 ↔ 184By similarity
Disulfide bondi198 ↔ 210By similarity
Disulfide bondi205 ↔ 223By similarity
Disulfide bondi217 ↔ 232By similarity
Disulfide bondi237 ↔ 249By similarity
Disulfide bondi244 ↔ 262By similarity
Disulfide bondi256 ↔ 271By similarity
Glycosylationi273N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi277 ↔ 290By similarity
Disulfide bondi285 ↔ 303By similarity
Disulfide bondi297 ↔ 314By similarity
Disulfide bondi319 ↔ 330By similarity
Disulfide bondi326 ↔ 339By similarity
Disulfide bondi341 ↔ 353By similarity
Disulfide bondi359 ↔ 369By similarity
Disulfide bondi365 ↔ 378By similarity
Disulfide bondi380 ↔ 393By similarity
Glycosylationi657N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi667 ↔ 681By similarity
Disulfide bondi677 ↔ 696By similarity
Disulfide bondi698 ↔ 711By similarity
Modified residuei717PhosphothreonineCombined sources1
Modified residuei724PhosphothreonineCombined sources1
Modified residuei732PhosphothreonineCombined sources1
Modified residuei733PhosphothreonineCombined sources1
Modified residuei734PhosphoserineCombined sources1

Post-translational modificationi

N- and O-glycosylated.By similarity
Ubiquitinated by MYLIP leading to degradation.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP35952.
PRIDEiP35952.

PTM databases

iPTMnetiP35952.
PhosphoSitePlusiP35952.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013496.

Structurei

3D structure databases

ProteinModelPortaliP35952.
SMRiP35952.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 65LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST41
Domaini66 – 106LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST41
Domaini107 – 145LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST39
Domaini146 – 186LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST41
Domaini196 – 234LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST39
Domaini235 – 273LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST39
Domaini275 – 314LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST40
Domaini315 – 354EGF-like 1PROSITE-ProRule annotationAdd BLAST40
Domaini355 – 394EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Repeati398 – 439LDL-receptor class B 1Add BLAST42
Repeati440 – 485LDL-receptor class B 2Add BLAST46
Repeati486 – 528LDL-receptor class B 3Add BLAST43
Repeati529 – 572LDL-receptor class B 4Add BLAST44
Repeati573 – 615LDL-receptor class B 5Add BLAST43
Repeati616 – 658LDL-receptor class B 6Add BLAST43
Domaini663 – 712EGF-like 3PROSITE-ProRule annotationAdd BLAST50

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni717 – 788Clustered O-linked oligosaccharidesAdd BLAST72
Regioni830 – 879Required for MYLIP-triggered down-regulation of LDLRBy similarityAdd BLAST50

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi842 – 847NPXY motifBy similarity6

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the LDLR family.Curated
Contains 3 EGF-like domains.PROSITE-ProRule annotation
Contains 7 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 6 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KD0U. Eukaryota.
ENOG410Z5FJ. LUCA.
HOGENOMiHOG000115656.
HOVERGENiHBG006250.
InParanoidiP35952.
KOiK12473.
PhylomeDBiP35952.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
4.10.400.10. 7 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 7 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 2 hits.
SM00192. LDLa. 7 hits.
SM00135. LY. 5 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 7 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS01209. LDLRA_1. 7 hits.
PS50068. LDLRA_2. 7 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35952-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTADLMLRW AIALLLAAAG VAAEDSCGKN EFQCRDGKCI VSKWVCDGSR
60 70 80 90 100
ECPDGSDESP ETCMSVTCRS GEFSCGGRVS RCIPDSWRCD GRTDCENGSD
110 120 130 140 150
ELDCSPKTCS LDEFRCQDGK CISRQFVCDQ DWDCLDGSDE AHCAATTCGP
160 170 180 190 200
AHFRCNSSSC IPSLWACDGD RDCDDGSDEW PQNCGAEDTA AEVVSSPCSS
210 220 230 240 250
LEFHCGSSEC IHRSWVCDGA ADCKDKSDEE NCAVTTCRPD EFQCADGSCI
260 270 280 290 300
HGSRQCDREH DCKDMSDELG CINVTQCDGP NKFKCHSGEC ISLDKVCNSA
310 320 330 340 350
RDCRDWSDEP IKECKTNECL DNNGGCSHIC KDLKIGYECL CPSGFRLVDG
360 370 380 390 400
HQCEDIDECQ EPDTCSQLCV NLEGSFKCEC RAGFHMDPHT RVCKAVGSIG
410 420 430 440 450
FLLFTNRHEV RKMTLDRSEY TSLIPNLKNV VALDTEVANN RIYWSDLSQR
460 470 480 490 500
KIYSAVMDQG TSLSYDAIIS GDLHAPDGLA VDWIHGNIYW TDSVPGTVSV
510 520 530 540 550
ADTKGVRRRT LFREKGSRPR AIVVDPVHGF MYWTDWGTPA KIKKGGLNGV
560 570 580 590 600
DIYSLVTEDI QWPNGITLDL PSGRLYWVDS KLHSISSIDV NGGGRKTILE
610 620 630 640 650
DEKQLAHPFS LAIYEDKVYW TDVLNEAIFS ANRLTGSDVN LVAKNLMSPE
660 670 680 690 700
DIVLFHNVTQ PRGVNWCEAT VLPNGGCQYM CLPAPQISAH SPKFTCACPD
710 720 730 740 750
GMLLAKDMRS CLPEVDTVPT TQGTSTIGPV VTTSAAVSLK RKEDPSATRH
760 770 780 790 800
KEDPSATRHN EDPSATSTSR QPGDTPELST VESVTVSSQV QGDMAGRGDE
810 820 830 840 850
VQRHGVGFLS IFLPIALVAL LVFGAILLWR NWRLRNINSI NFDNPVYQKT
860 870
TEDEIHICRS QDGYTYPSRQ MVSLEDDVA
Length:879
Mass (Da):96,622
Last modified:June 1, 1994 - v1
Checksum:iE89F354E3F7C9005
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13722 mRNA. Translation: CAA32001.1.
PIRiS03430. QRRTLD.
RefSeqiNP_786938.1. NM_175762.2.
UniGeneiRn.10483.

Genome annotation databases

GeneIDi300438.
KEGGirno:300438.
UCSCiRGD:2998. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13722 mRNA. Translation: CAA32001.1.
PIRiS03430. QRRTLD.
RefSeqiNP_786938.1. NM_175762.2.
UniGeneiRn.10483.

3D structure databases

ProteinModelPortaliP35952.
SMRiP35952.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013496.

PTM databases

iPTMnetiP35952.
PhosphoSitePlusiP35952.

Proteomic databases

PaxDbiP35952.
PRIDEiP35952.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi300438.
KEGGirno:300438.
UCSCiRGD:2998. rat.

Organism-specific databases

CTDi3949.
RGDi2998. Ldlr.

Phylogenomic databases

eggNOGiENOG410KD0U. Eukaryota.
ENOG410Z5FJ. LUCA.
HOGENOMiHOG000115656.
HOVERGENiHBG006250.
InParanoidiP35952.
KOiK12473.
PhylomeDBiP35952.

Miscellaneous databases

PROiP35952.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
4.10.400.10. 7 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 7 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 2 hits.
SM00192. LDLa. 7 hits.
SM00135. LY. 5 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 7 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS01209. LDLRA_1. 7 hits.
PS50068. LDLRA_2. 7 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLDLR_RAT
AccessioniPrimary (citable) accession number: P35952
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 30, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.