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P98156 (VLDLR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Very low-density lipoprotein receptor

Short name=VLDL receptor
Short name=VLDL-R
Gene names
Name:Vldlr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length873 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Membraneclathrin-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 processCholesterol metabolism
Endocytosis
Lipid metabolism
Lipid transport
Steroid metabolism
Sterol metabolism
Transport
   Cellular componentCoated pit
Membrane
VLDL
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

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

reelin-mediated signaling pathway

Inferred from genetic interaction PubMed 18778775. Source: BHF-UCL

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_componentcoated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from direct assay PubMed 15950758. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from sequence orthology PubMed 15082773. Source: MGI

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

very-low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

glycoprotein transporter activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 15249135. Source: MGI

reelin receptor activity

Inferred from genetic interaction PubMed 18778775. Source: BHF-UCL

very-low-density lipoprotein particle binding

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle receptor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 873846Very low-density lipoprotein receptor
PRO_0000017344

Regions

Topological domain28 – 797770Extracellular Potential
Transmembrane798 – 81922Helical; Potential
Topological domain820 – 87354Cytoplasmic Potential
Domain31 – 6939LDL-receptor class A 1
Domain70 – 11041LDL-receptor class A 2
Domain111 – 15141LDL-receptor class A 3
Domain152 – 19039LDL-receptor class A 4
Domain191 – 23141LDL-receptor class A 5
Domain237 – 27539LDL-receptor class A 6
Domain276 – 31439LDL-receptor class A 7
Domain316 – 35540LDL-receptor class A 8
Domain356 – 39136EGF-like 1
Domain396 – 43136EGF-like 2; calcium-binding Potential
Repeat439 – 48042LDL-receptor class B 1
Repeat481 – 52444LDL-receptor class B 2
Repeat525 – 56743LDL-receptor class B 3
Repeat568 – 61144LDL-receptor class B 4
Repeat612 – 65443LDL-receptor class B 5
Repeat655 – 69743LDL-receptor class B 6
Domain702 – 75049EGF-like 3
Region751 – 79040Clustered O-linked oligosaccharides
Motif832 – 8376Endocytosis signal Potential

Amino acid modifications

Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation7651N-linked (GlcNAc...) Potential
Glycosylation7811N-linked (GlcNAc...) Potential
Disulfide bond33 ↔ 45 By similarity
Disulfide bond40 ↔ 58 By similarity
Disulfide bond52 ↔ 67 By similarity
Disulfide bond72 ↔ 84 By similarity
Disulfide bond79 ↔ 97 By similarity
Disulfide bond91 ↔ 108 By similarity
Disulfide bond113 ↔ 127 By similarity
Disulfide bond120 ↔ 140 By similarity
Disulfide bond134 ↔ 149 By similarity
Disulfide bond154 ↔ 166 By similarity
Disulfide bond161 ↔ 179 By similarity
Disulfide bond173 ↔ 188 By similarity
Disulfide bond193 ↔ 205 By similarity
Disulfide bond200 ↔ 218 By similarity
Disulfide bond212 ↔ 229 By similarity
Disulfide bond239 ↔ 251 By similarity
Disulfide bond246 ↔ 264 By similarity
Disulfide bond258 ↔ 273 By similarity
Disulfide bond278 ↔ 290 By similarity
Disulfide bond285 ↔ 303 By similarity
Disulfide bond297 ↔ 312 By similarity
Disulfide bond318 ↔ 331 By similarity
Disulfide bond326 ↔ 344 By similarity
Disulfide bond338 ↔ 355 By similarity
Disulfide bond360 ↔ 371 By similarity
Disulfide bond367 ↔ 380 By similarity
Disulfide bond382 ↔ 394 By similarity
Disulfide bond400 ↔ 410 By similarity
Disulfide bond406 ↔ 419 By similarity
Disulfide bond421 ↔ 434 By similarity
Disulfide bond706 ↔ 719 By similarity
Disulfide bond715 ↔ 734 By similarity
Disulfide bond736 ↔ 749 By similarity
Cross-link839Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict1611C → G in AAC37668. Ref.1
Sequence conflict2621P → L in AAB32228. Ref.3
Sequence conflict2971C → S in AAA59384. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P98156 [UniParc].

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

FASTA87396,373
        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 

« Hide

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.
CCDSCCDS29721.1.
PIRI48952.
RefSeqNP_001154892.1. NM_001161420.1.
NP_038731.2. NM_013703.2.
XP_006526980.1. XM_006526917.1.
XP_006526981.1. XM_006526918.1.
UniGeneMm.4141.

3D structure databases

ProteinModelPortalP98156.
SMRP98156. Positions 21-789.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204529. 3 interactions.
DIPDIP-33283N.
IntActP98156. 2 interactions.
MINTMINT-4140012.

Proteomic databases

MaxQBP98156.
PaxDbP98156.
PRIDEP98156.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000167487; ENSMUSP00000127329; ENSMUSG00000024924.
GeneID22359.
KEGGmmu:22359.
UCSCuc008hbt.2. mouse.

Organism-specific databases

CTD7436.
MGIMGI:98935. Vldlr.

Phylogenomic databases

eggNOGNOG255913.
GeneTreeENSGT00740000114992.
HOGENOMHOG000115656.
HOVERGENHBG006250.
InParanoidP98156.
OMAMGTSARW.
PhylomeDBP98156.
TreeFamTF351700.

Gene expression databases

ArrayExpressP98156.
BgeeP98156.
CleanExMM_VLDLR.
GenevestigatorP98156.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
4.10.400.10. 8 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamPF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 2 hits.
SM00192. LDLa. 8 hits.
SM00135. LY. 5 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 8 hits.
PROSITEPS00010. ASX_HYDROXYL. 2 hits.
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]
ProtoNetSearch...

Other

NextBio302661.
PROP98156.
SOURCESearch...

Entry information

Entry nameVLDLR_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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