Very low-density lipoprotein receptor precursor

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P98156 (VLDLR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 131. 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:
Very low-density lipoprotein receptor
Short name=VLDL receptor
Short name=VLDL-R

Gene names

Name:

Vldlr

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	873 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 VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binding to Reelin induces tyrosine phosphorylation of Dab1 and modulation of Tau phosphorylation.
Subunit structure	Binds to the extracellular matrix protein Reelin. Interacts with DAB1. Interacts with VLDLR. Interacts with SNX17. Interacts with PCSK9 By similarity. Ref.4 Ref.5 Ref.6
Subcellular location	Membrane; Single-pass type I membrane protein. Membrane › clathrin-coated pit; Single-pass type I membrane protein.
Tissue specificity	Abundant in heart and muscle; less in kidney, brain, ovary, testis, lung and adipose tissue.
Post-translational modification	Ubiquitinated at Lys-839 by MYLIP leading to degradation By similarity. Ref.7
Miscellaneous	LRP8 and VLVLR together are required for correct embryonic development in the brain. Targeted disruption of both genes results in a phenotype virtually indistinguishable from that seen in "reeler" and "scrambler" mice. Subtle effects of VLDLR deletion are found mainly in the cerebellum, whereas lack of LRP8 predominantly affects the positioning of the neurons in the neocortex.
Sequence similarities	Contains 3 EGF-like domains. Contains 8 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	Coated pit Membrane VLDL
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol metabolic process Inferred from electronic annotation. Source: UniProtKB-KW glycoprotein transport Inferred from electronic annotation. Source: Compara lipid transport Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 18778775. Source: BHF-UCL positive regulation of dendrite development Inferred from genetic interaction PubMed 18778775. Source: BHF-UCL positive regulation of protein kinase activity Inferred from genetic interaction PubMed 12526740. Source: MGI ventral spinal cord development Inferred from expression pattern PubMed 20711475. Source: UniProtKB very-low-density lipoprotein particle clearance Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from direct assay PubMed 15950758. Source: BHF-UCL integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from sequence orthology PubMed 15082773. Source: MGI very-low-density lipoprotein particle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro glycoprotein transporter activity Inferred from electronic annotation. Source: Compara reelin receptor activity Inferred from genetic interaction PubMed 18778775. Source: BHF-UCL very-low-density lipoprotein particle binding Inferred from electronic annotation. Source: Compara very-low-density lipoprotein particle receptor activity Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

Potential

Chain

28 – 873

846

Very low-density lipoprotein receptor

PRO_0000017344

Regions

Topological domain

28 – 797

770

Extracellular Potential

Transmembrane

798 – 819

Helical; Potential

Topological domain

820 – 873

Cytoplasmic Potential

Domain

31 – 69

LDL-receptor class A 1

Domain

70 – 110

LDL-receptor class A 2

Domain

111 – 151

LDL-receptor class A 3

Domain

152 – 190

LDL-receptor class A 4

Domain

191 – 231

LDL-receptor class A 5

Domain

237 – 275

LDL-receptor class A 6

Domain

276 – 314

LDL-receptor class A 7

Domain

316 – 355

LDL-receptor class A 8

Domain

356 – 391

EGF-like 1

Domain

396 – 431

EGF-like 2; calcium-binding Potential

Repeat

439 – 480

LDL-receptor class B 1

Repeat

481 – 524

LDL-receptor class B 2

Repeat

525 – 567

LDL-receptor class B 3

Repeat

568 – 611

LDL-receptor class B 4

Repeat

612 – 654

LDL-receptor class B 5

Repeat

655 – 697

LDL-receptor class B 6

Domain

702 – 750

EGF-like 3

Region

751 – 790

Clustered O-linked oligosaccharides

Motif

832 – 837

Endocytosis signal Potential

Amino acid modifications

Glycosylation

151

N-linked (GlcNAc...) Potential

Glycosylation

765

N-linked (GlcNAc...) Potential

Glycosylation

781

N-linked (GlcNAc...) Potential

Disulfide bond

33 ↔ 45

By similarity

Disulfide bond

40 ↔ 58

By similarity

Disulfide bond

52 ↔ 67

By similarity

Disulfide bond

72 ↔ 84

By similarity

Disulfide bond

79 ↔ 97

By similarity

Disulfide bond

91 ↔ 108

By similarity

Disulfide bond

113 ↔ 127

By similarity

Disulfide bond

120 ↔ 140

By similarity

Disulfide bond

134 ↔ 149

By similarity

Disulfide bond

154 ↔ 166

By similarity

Disulfide bond

161 ↔ 179

By similarity

Disulfide bond

173 ↔ 188

By similarity

Disulfide bond

193 ↔ 205

By similarity

Disulfide bond

200 ↔ 218

By similarity

Disulfide bond

212 ↔ 229

By similarity

Disulfide bond

239 ↔ 251

By similarity

Disulfide bond

246 ↔ 264

By similarity

Disulfide bond

258 ↔ 273

By similarity

Disulfide bond

278 ↔ 290

By similarity

Disulfide bond

285 ↔ 303

By similarity

Disulfide bond

297 ↔ 312

By similarity

Disulfide bond

318 ↔ 331

By similarity

Disulfide bond

326 ↔ 344

By similarity

Disulfide bond

338 ↔ 355

By similarity

Disulfide bond

360 ↔ 371

By similarity

Disulfide bond

367 ↔ 380

By similarity

Disulfide bond

382 ↔ 394

By similarity

Disulfide bond

400 ↔ 410

By similarity

Disulfide bond

406 ↔ 419

By similarity

Disulfide bond

421 ↔ 434

By similarity

Disulfide bond

706 ↔ 719

By similarity

Disulfide bond

715 ↔ 734

By similarity

Disulfide bond

736 ↔ 749

By similarity

Cross-link

839

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict

161

C → G in AAC37668. Ref.1

Sequence conflict

262

P → L in AAB32228. Ref.3

Sequence conflict

297

C → S in AAA59384. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P98156 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 08F09F93825195CB
Show »

FASTA

873

96,373

        10         20         30         40         50         60 
MGTSARWALW LLLALCWAPR DSGATASGKK AKCDSSQFQC TNGRCITLLW KCDGDEDCAD 

        70         80         90        100        110        120 
GSDEKNCVKK TCAESDFVCK NGQCVPNRWQ CDGDPDCEDG SDESPEQCHM RTCRINEISC 

       130        140        150        160        170        180 
GARSTQCIPV SWRCDGENDC DNGEDEENCG NITCSADEFT CSSGRCVSRN FVCNGQDDCD 

       190        200        210        220        230        240 
DGSDELDCAP PTCGAHEFQC STSSCIPLSW VCDDDADCSD QSDESLEQCG RQPVIHTKCP 

       250        260        270        280        290        300 
TSEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI 

       310        320        330        340        350        360 
RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDMSKVCDQ EQDCRDWSDE PLKECHINEC 

       370        380        390        400        410        420 
LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE 

       430        440        450        460        470        480 
CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA 

       490        500        510        520        530        540 
QKLFWADLSQ KAIFSASIDD KVGRHFKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA 

       550        560        570        580        590        600 
TLDGAKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTEDIQ 

       610        620        630        640        650        660 
WPNGITLDLV KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI 

       670        680        690        700        710        720 
DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP SGKNWCEDDM ENGGCEYLCL 

       730        740        750        760        770        780 
PAPQINDHSP KYTCSCPNGY NLEENGRECQ STSTPVTYSE TKDINTTDIL RTSGLVPGGI 

       790        800        810        820        830        840 
NVTTAVSEVS VPPKGTSAAW AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT 

       850        860        870 
TEEDLSIDIG RHSASVGHTY PAISVVSTDD DLA

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References

[1]	"Mouse very-low-density-lipoprotein receptor (VLDLR) cDNA cloning, tissue-specific expression and evolutionary relationship with the low-density-lipoprotein receptor." Oka K., Ishimura-Oka K., Chu M.J., Sullivan M., Krushkal J., Li W.H., Chan L. Eur. J. Biochem. 224:975-982(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Heart.
[2]	"Cloning of a complementary deoxyribonucleic acid encoding the murine homolog of the very low density lipoprotein/apolipoprotein-E receptor: expression pattern and assignment of the gene to mouse chromosome 19." Gafvels M.E., Paavola L.G., Boyd C.O., Nolan P.M., Wittmaack F., Chawla A., Lazar M.A., Bucan M., Angelin B.O., Strauss J.F. Endocrinology 135:387-394(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.
[3]	"The mouse very low density lipoprotein receptor (Vldlr) gene maps to chromosome 19." Naggert J.K., Mu J.L. Mamm. Genome 5:453-455(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-262.
[4]	"Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation." Hiesberger T., Trommsdorff M., Howell B.W., Goffinet A.M., Mumby M.C., Cooper J.A., Herz J. Neuron 24:481-489(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH REELIN.
[5]	"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.
[6]	"Normal sorting but defective endocytosis of the low density lipoprotein receptor in mice with autosomal recessive hypercholesterolemia." Jones C., Hammer R.E., Li W.-P., Cohen J.C., Hobbs H.H., Herz J. J. Biol. Chem. 278:29024-29030(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LDLRAP1.
[7]	"The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2." Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V., Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D., Nimpf J., van Berkel T.J., Tontonoz P., Zelcer N. J. Biol. Chem. 285:19720-19726(2010) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L33417 mRNA. Translation: AAC37668.1. U06670 mRNA. Translation: AAA59384.1. S73732 Genomic DNA. Translation: AAB32228.2.
IPI	IPI00323114.
PIR	I48952.
RefSeq	NP_001154892.1. NM_001161420.1. NP_038731.2. NM_013703.2.
UniGene	Mm.4141.
3D structure databases
ProteinModelPortal	P98156.
SMR	P98156. Positions 21-789.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-33283N.
IntAct	P98156. 1 interaction.
Proteomic databases
PaxDb	P98156.
PRIDE	P98156.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000167487; ENSMUSP00000127329; ENSMUSG00000024924.
GeneID	22359.
KEGG	mmu:22359.
UCSC	uc008hbt.2. mouse.
Organism-specific databases
CTD	7436.
MGI	MGI:98935. Vldlr.
Phylogenomic databases
eggNOG	NOG255913.
GeneTree	ENSGT00700000104037.
HOGENOM	HOG000115656.
HOVERGEN	HBG006250.
InParanoid	P98156.
OMA	SIDIGRH.
Gene expression databases
ArrayExpress	P98156.
Bgee	P98156.
CleanEx	MM_VLDLR.
Genevestigator	P98156.
GermOnline	ENSMUSG00000024924. Mus musculus.
Family and domain databases
Gene3D	2.120.10.30. 1 hit. 4.10.400.10. 8 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. 8 hits. PF00058. Ldl_recept_b. 5 hits. [Graphical view]
SMART	SM00181. EGF. 1 hit. SM00179. EGF_CA. 2 hits. SM00192. LDLa. 8 hits. SM00135. LY. 5 hits. [Graphical view]
SUPFAM	SSF57184. Grow_fac_recept. 1 hit. SSF57424. LDL_rcpt_classA_cys-rich. 8 hits.
PROSITE	PS00010. ASX_HYDROXYL. 2 hits. PS00022. EGF_1. False negative. PS01186. EGF_2. 3 hits. PS50026. EGF_3. 2 hits. PS01187. EGF_CA. 1 hit. PS01209. LDLRA_1. 8 hits. PS50068. LDLRA_2. 8 hits. PS51120. LDLRB. 5 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	302661.
SOURCE	Search...

Entry information

Entry name

VLDLR_MOUSE

Accession

Primary (citable) accession number: P98156
Secondary accession number(s): Q64022

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 131 of the entry and version 1 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

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