Low-density lipoprotein receptor precursor

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P35951 (LDLR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 130. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Low-density lipoprotein receptor
Short name=LDL receptor

Gene names

Name:

Ldlr

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	862 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	Interacts with LDLRAP1, ARRB1, SNX17. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Interacts with the full length immature form of PCSK9 (via C-terminus). Ref.6 Ref.7
Subcellular location	Cell membrane; Single-pass type I membrane protein. Endomembrane system; Single-pass type I membrane protein. Membrane › clathrin-coated pit; Single-pass type I membrane protein By similarity. Golgi apparatus By similarity. Early endosome By similarity. Late endosome By similarity. Cell surface By similarity. Lysosome By similarity. Note: Found distributed from the plasma membrane to intracellular compartments. Localizes to the Golgi apparatus, early and late endosomes/lysosomes and cell surface in the presence of PCSK9 By similarity.
Domain	The NPXY motif mediates the interaction with the clathrin adaptor DAB2 involved in receptor internalization. Ref.6
Post-translational modification	Ubiquitinated by MYLIP leading to degradation By similarity.
Sequence similarities	Belongs to the LDLR family. Contains 3 EGF-like domains. Contains 7 LDL-receptor class A domains. Contains 6 LDL-receptor class B repeats.

Ontologies

Keywords
Biological process	Cholesterol metabolism Endocytosis Lipid metabolism Lipid transport Steroid metabolism Sterol metabolism Transport
Cellular component	Cell membrane Coated pit Endosome Golgi apparatus LDL Lysosome Membrane
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol homeostasis Inferred from mutant phenotype PubMed 12746448 PubMed 9788969. Source: MGI cholesterol import Inferred from mutant phenotype PubMed 18175806. Source: BHF-UCL cholesterol metabolic process Inferred from mutant phenotype PubMed 17071966. Source: MGI lipoprotein catabolic process Inferred from direct assay PubMed 15741654. Source: MGI low-density lipoprotein particle clearance Inferred from mutant phenotype PubMed 18175806. Source: BHF-UCL phospholipid transport Inferred from mutant phenotype PubMed 18175806. Source: BHF-UCL positive regulation of triglyceride biosynthetic process Inferred from mutant phenotype PubMed 18175806. Source: BHF-UCL regulation of phosphatidylcholine catabolic process Inferred from mutant phenotype PubMed 18175806. Source: BHF-UCL
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB cell surface Inferred from sequence or structural similarity. Source: UniProtKB coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW late endosome Inferred from sequence or structural similarity. Source: UniProtKB low-density lipoprotein particle Inferred from electronic annotation. Source: UniProtKB-KW lysosome Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro low-density lipoprotein particle binding Inferred from direct assay PubMed 15741654 PubMed 7848292. Source: MGI low-density lipoprotein receptor activity Inferred from direct assay PubMed 12072432. Source: MGI very-low-density lipoprotein particle receptor activity Inferred from direct assay PubMed 16166565. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

By similarity

Chain

22 – 862

841

Low-density lipoprotein receptor

PRO_0000017313

Regions

Topological domain

22 – 790

769

Extracellular Potential

Transmembrane

791 – 812

Helical; Potential

Topological domain

813 – 862

Cytoplasmic Potential

Domain

25 – 65

LDL-receptor class A 1

Domain

66 – 106

LDL-receptor class A 2

Domain

107 – 145

LDL-receptor class A 3

Domain

146 – 186

LDL-receptor class A 4

Domain

196 – 234

LDL-receptor class A 5

Domain

235 – 273

LDL-receptor class A 6

Domain

275 – 314

LDL-receptor class A 7

Domain

315 – 354

EGF-like 1

Domain

355 – 394

EGF-like 2; calcium-binding Potential

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 – 713

EGF-like 3

Region

722 – 770

Clustered O-linked oligosaccharides

Region

813 – 862

Required for MYLIP-triggered down-regulation of LDLR By similarity

Motif

825 – 830

NPXY motif

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

273

N-linked (GlcNAc...) Potential

Glycosylation

462

N-linked (GlcNAc...) Potential

Disulfide bond

34 ↔ 52

By similarity

Disulfide bond

46 ↔ 63

By similarity

Disulfide bond

68 ↔ 82

By similarity

Disulfide bond

75 ↔ 95

By similarity

Disulfide bond

89 ↔ 104

By similarity

Disulfide bond

109 ↔ 121

By similarity

Disulfide bond

116 ↔ 134

By similarity

Disulfide bond

128 ↔ 143

By similarity

Disulfide bond

148 ↔ 160

By similarity

Disulfide bond

155 ↔ 173

By similarity

Disulfide bond

167 ↔ 184

By similarity

Disulfide bond

198 ↔ 210

By similarity

Disulfide bond

205 ↔ 223

By similarity

Disulfide bond

217 ↔ 232

By similarity

Disulfide bond

237 ↔ 249

By similarity

Disulfide bond

244 ↔ 262

By similarity

Disulfide bond

256 ↔ 271

By similarity

Disulfide bond

277 ↔ 290

By similarity

Disulfide bond

285 ↔ 303

By similarity

Disulfide bond

297 ↔ 314

By similarity

Disulfide bond

319 ↔ 330

By similarity

Disulfide bond

326 ↔ 339

By similarity

Disulfide bond

341 ↔ 353

By similarity

Disulfide bond

359 ↔ 369

By similarity

Disulfide bond

365 ↔ 378

By similarity

Disulfide bond

380 ↔ 393

By similarity

Disulfide bond

667 ↔ 682

By similarity

Disulfide bond

678 ↔ 697

By similarity

Disulfide bond

699 ↔ 712

By similarity

Experimental info

Sequence conflict

A → V in CAA79581. Ref.1

Sequence conflict

C → G in CAA79581. Ref.1

Sequence conflict

E → K in CAA79581. Ref.1

Sequence conflict

144

Q → P in CAA79581. Ref.1

Sequence conflict

156

N → K in CAA79581. Ref.1

Sequence conflict

178

D → H in CAA79581. Ref.1

Sequence conflict

186 – 187

GR → AE in CAA79581. Ref.1

Sequence conflict

819

N → NIT in CAA79581. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P35951 [UniParc].

Last modified February 6, 2013. Version 2.
Checksum: 43E7D6A293BE609C
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FASTA

862

94,947

        10         20         30         40         50         60 
MSTADLMRRW VIALLLAAAG VAAEDSCSRN EFQCRDGKCI ASKWVCDGSP ECPDGSDESP 

        70         80         90        100        110        120 
ETCMSVTCQS NQFSCGGRVS RCIPDSWRCD GQVDCENDSD EQGCPPKTCS QDDFRCQDGK 

       130        140        150        160        170        180 
CISPQFVCDG DRDCLDGSDE AHCQATTCGP AHFRCNSSIC IPSLWACDGD VDCVDGSDEW 

       190        200        210        220        230        240 
PQNCQGRDTA SKGVSSPCSS LEFHCGSSEC IHRSWVCDGE ADCKDKSDEE HCAVATCRPD 

       250        260        270        280        290        300 
EFQCADGSCI HGSRQCDREH DCKDMSDELG CVNVTQCDGP NKFKCHSGEC ISLDKVCDSA 

       310        320        330        340        350        360 
RDCQDWSDEP IKECKTNECL DNNGGCSHIC KDLKIGSECL CPSGFRLVDL HRCEDIDECQ 

       370        380        390        400        410        420 
EPDTCSQLCV NLEGSYKCEC QAGFHMDPHT RVCKAVGSIG YLLFTNRHEV RKMTLDRSEY 

       430        440        450        460        470        480 
TSLLPNLKNV VALDTEVTNN RIYWSDLSQK KIYSALMDQA PNLSYDTIIS EDLHAPDGLA 

       490        500        510        520        530        540 
VDWIHRNIYW TDSVPGSVSV ADTKGVKRRT LFQEAGSRPR AIVVDPVHGF MYWTDWGTPA 

       550        560        570        580        590        600 
KIKKGGLNGV DIHSLVTENI QWPNGITLDL SSGRLYWVDS KLHSISSIDV NGGNRKTILE 

       610        620        630        640        650        660 
DENRLAHPFS LAIYEDKVYW TDVINEAIFS ANRLTGSDVN LVAENLLSPE DIVLFHKVTQ 

       670        680        690        700        710        720 
PRGVNWCETT ALLPNGGCQY LCLPAPQIGP HSPKFTCACP DGMLLAKDMR SCLTEVDTVL 

       730        740        750        760        770        780 
TTQGTSAVRP VVTASATRPP KHSEDLSAPS TPRQPVDTPG LSTVASVTVS HQVQGDMAGR 

       790        800        810        820        830        840 
GNEEQPHGMR FLSIFFPIAL VALLVLGAVL LWRNWRLKNI NSINFDNPVY QKTTEDELHI 

       850        860 
CRSQDGYTYP SRQMVSLEDD VA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mouse low density lipoprotein receptor gene: cDNA sequence and exon-intron structure." Hoffer M.J.V., van Eck M.M., Petrij F., van der Zee A., de Wit E., Meijer D., Grosveld G., Havekes L.M., Hofker M.H., Frants R.R. Biochem. Biophys. Res. Commun. 191:880-886(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver.
[2]	"Molecular cloning and nucleotide sequence of cDNA encoding a functional murine low-density-lipoprotein receptor." Polvino W.J., Dichek D.A., Mason J., Anderson W.F. Somat. Cell Mol. Genet. 18:443-450(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2." Morris S.M., Cooper J.A. Traffic 2:111-123(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DAB2, DOMAIN.
[7]	"The PX-domain protein SNX17 interacts with members of the LDL receptor family and modulates endocytosis of the LDL receptor." Stockinger W., Sailler B., Strasser V., Recheis B., Fasching D., Kahr L., Schneider W.J., Nimpf J. EMBO J. 21:4259-4267(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SNX17.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z19521 mRNA. Translation: CAA79581.1. X64414 mRNA. Translation: CAA45759.1. AC161371 Genomic DNA. No translation available. CH466522 Genomic DNA. Translation: EDL25212.1. BC053041 mRNA. Translation: AAH53041.1.
IPI	IPI00312063. IPI00785217.
PIR	QRMSLD. I48623.
RefSeq	NP_001239587.1. NM_001252658.1. NP_001239588.1. NM_001252659.1. NP_034830.2. NM_010700.3.
UniGene	Mm.3213.
3D structure databases
ProteinModelPortal	P35951.
SMR	P35951. Positions 22-715.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35951. 1 interaction.
MINT	MINT-1541606.
PTM databases
PhosphoSite	P35951.
Proteomic databases
PaxDb	P35951.
PRIDE	P35951.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034713; ENSMUSP00000034713; ENSMUSG00000032193.
GeneID	16835.
KEGG	mmu:16835.
Organism-specific databases
CTD	3949.
MGI	MGI:96765. Ldlr.
Phylogenomic databases
eggNOG	NOG255913.
GeneTree	ENSGT00700000104037.
HOGENOM	HOG000115656.
HOVERGEN	HBG006250.
InParanoid	P35951.
KO	K12473.
OMA	PDTCSQL.
Gene expression databases
CleanEx	MM_LDLR.
Genevestigator	P35951.
GermOnline	ENSMUSG00000032193. Mus musculus.
Family and domain databases
Gene3D	2.120.10.30. 1 hit. 4.10.400.10. 7 hits.
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. 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]
Pfam	PF07645. EGF_CA. 1 hit. PF00057. Ldl_recept_a. 7 hits. PF00058. Ldl_recept_b. 5 hits. [Graphical view]
SMART	SM00181. EGF. 2 hits. SM00179. EGF_CA. 1 hit. SM00192. LDLa. 7 hits. SM00135. LY. 5 hits. [Graphical view]
SUPFAM	SSF57184. Grow_fac_recept. 1 hit. SSF57424. LDL_rcpt_classA_cys-rich. 7 hits.
PROSITE	PS00010. ASX_HYDROXYL. 1 hit. PS00022. EGF_1. False negative. 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]
ProtoNet	Search...
Other
NextBio	290754.
SOURCE	Search...

Entry information

Entry name

LDLR_MOUSE

Accession

Primary (citable) accession number: P35951
Secondary accession number(s): Q6GTJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	February 6, 2013
Last modified:	April 3, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents