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P98155 (VLDLR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 By similarity.

Subunit structure

Binds to the extracellular matrix protein Reelin. Interacts with VLDLR. Interacts with SNX17 By similarity. Interacts with DAB1. Receptor for the minor-group human rhinoviruses (HRVs); binds protein VP1 through the second and third LDL-receptor class A domains. Interacts with PCSK9. Ref.9 Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein. Membraneclathrin-coated pit; Single-pass type I membrane protein.

Tissue specificity

Abundant in heart and skeletal muscle; also ovary and kidney; not in liver.

Post-translational modification

Ubiquitinated at Lys-839 by MYLIP leading to degradation. Ref.11

Involvement in disease

Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 1 (CAMRQ1) [MIM:224050]: A congenital, non-progressive cerebellar ataxia associated with disturbed equilibrium, delayed ambulation, mental retardation, cerebellar hypoplasia and mild cerebral gyral simplification. Additional features include short stature, strabismus, pes planus and, rarely, seizures.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

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
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseMental retardation
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

glycoprotein transport

Inferred from direct assay PubMed 10571240. Source: BHF-UCL

lipid transport

Inferred from electronic annotation. Source: UniProtKB-KW

memory

Traceable author statement PubMed 7550352. Source: ProtInc

negative regulation of transcription from RNA polymerase II promoter

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

nervous system development

Traceable author statement PubMed 10380922. Source: ProtInc

positive regulation of dendrite development

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

positive regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

receptor-mediated endocytosis

Inferred from direct assay PubMed 10571240. Source: BHF-UCL

reelin-mediated signaling pathway

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

signal transduction

Traceable author statement PubMed 10380922. Source: ProtInc

ventral spinal cord development

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle clearance

Inferred from direct assay PubMed 8083232. Source: BHF-UCL

   Cellular_componentcoated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 15082773. Source: MGI

plasma membrane

Traceable author statement PubMed 10380922. Source: ProtInc

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

very-low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionapolipoprotein binding

Inferred from direct assay PubMed 10571240. Source: BHF-UCL

calcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent protein binding

Inferred from physical interaction PubMed 10571240. Source: BHF-UCL

glycoprotein binding

Inferred from physical interaction PubMed 10571240. Source: BHF-UCL

glycoprotein transporter activity

Inferred from direct assay PubMed 10571240. Source: BHF-UCL

low-density lipoprotein receptor activity

Traceable author statement PubMed 10380922. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 8083232. Source: IntAct

reelin receptor activity

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

very-low-density lipoprotein particle binding

Inferred from direct assay PubMed 10571240. Source: BHF-UCL

very-low-density lipoprotein particle receptor activity

Inferred from direct assay PubMed 8083232. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRPAP1P305334EBI-9004309,EBI-715927

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P98155-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P98155-2)

The sequence of this isoform differs from the canonical sequence as follows:
     751-779: STATTVTYSETKDTNTTEISATSGLVPGG → R

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 873846Very low-density lipoprotein receptor
PRO_0000017343

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 – 39540EGF-like 1
Domain396 – 43540EGF-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
Disulfide bond120 ↔ 140
Disulfide bond134 ↔ 149
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) Ref.11

Natural variations

Alternative sequence751 – 77929STATT…LVPGG → R in isoform Short.
VSP_004304
Natural variant591V → I. Ref.5 Ref.13
Corresponds to variant rs6149 [ dbSNP | Ensembl ].
VAR_011865
Natural variant2621P → H. Ref.5
Corresponds to variant rs34761707 [ dbSNP | Ensembl ].
VAR_025063
Natural variant3791E → K. Ref.13
Corresponds to variant rs6146 [ dbSNP | Ensembl ].
VAR_011866
Natural variant4641L → I. Ref.5
Corresponds to variant rs34753566 [ dbSNP | Ensembl ].
VAR_025064
Natural variant5611I → V. Ref.5
Corresponds to variant rs35724190 [ dbSNP | Ensembl ].
VAR_025065
Natural variant6131R → H. Ref.5
Corresponds to variant rs35948251 [ dbSNP | Ensembl ].
VAR_025066
Natural variant7911V → I. Ref.5
Corresponds to variant rs35334949 [ dbSNP | Ensembl ].
VAR_025067

Experimental info

Mutagenesis8251K → R: Insensitive to MYLIP-triggered degradation; when associated with R-828 and R-839. Ref.11
Mutagenesis8281K → R: Insensitive to MYLIP-triggered degradation; when associated with R-825 and R-839. Ref.11
Mutagenesis8391K → R: Insensitive to MYLIP-triggered degradation. Insensitive to MYLIP-triggered degradation; when associated with R-825 and R-828. Ref.11
Sequence conflict91L → V in AAA53684. Ref.1
Sequence conflict131L → V in AAA61344. Ref.4
Sequence conflict4241G → A in AAA53684. Ref.1
Sequence conflict6781L → H in AAA53684. Ref.1
Sequence conflict7661T → S in AAA61344. Ref.4

Secondary structure

......... 873
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8BAC29438A78C2B8

FASTA87396,098
        10         20         30         40         50         60 
MGTSALWALW LLLALCWAPR ESGATGTGRK AKCEPSQFQC TNGRCITLLW KCDGDEDCVD 

        70         80         90        100        110        120 
GSDEKNCVKK TCAESDFVCN NGQCVPSRWK CDGDPDCEDG SDESPEQCHM RTCRIHEISC 

       130        140        150        160        170        180 
GAHSTQCIPV SWRCDGENDC DSGEDEENCG NITCSPDEFT CSSGRCISRN FVCNGQDDCS 

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

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

       310        320        330        340        350        360 
RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDISKVCNQ 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 KVGRHVKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA 

       550        560        570        580        590        600 
TLDGTKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTADIQ 

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

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

       730        740        750        760        770        780 
PAPQINDHSP KYTCSCPSGY NVEENGRDCQ STATTVTYSE TKDTNTTEIS ATSGLVPGGI 

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

       850        860        870 
TEEDLSIDIG RHSASVGHTY PAISVVSTDD DLA 

« Hide

Isoform Short [UniParc].

Checksum: 588311D7C6B2C1FD
Show »

FASTA84593,383

References

« Hide 'large scale' references
[1]"Cloning of a cDNA encoding a putative human very low density lipoprotein/apolipoprotein E receptor and assignment of the gene to chromosome 9pter-p23."
Gafvels M.E., Caird M., Britt D., Jackson C.L., Patterson D., Strauss J.F.
Somat. Cell Mol. Genet. 19:557-569(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[2]"Characterization and tissue-specific expression of the human 'very low density lipoprotein (VLDL) receptor' mRNA."
Webb J.C., Patel D.D., Jones M.D., Knight B.L., Soutar A.K.
Hum. Mol. Genet. 3:531-537(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[3]"Structure, chromosome location, and expression of the human very low density lipoprotein receptor gene."
Sakai J., Hoshino A., Takahashi S., Miura Y., Ishii H., Suzuki H., Kawarabayasi Y., Yamamoto T.
J. Biol. Chem. 269:2173-2182(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]"Human very-low-density lipoprotein receptor complementary DNA and deduced amino acid sequence and localization of its gene (VLDLR) to chromosome band 9p24 by fluorescence in situ hybridization."
Oka K., Tzung K.W., Sullivan M., Lindsay E., Baldini A., Chan L.
Genomics 20:298-300(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[5]SeattleSNPs variation discovery resource
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-59; HIS-262; ILE-464; VAL-561; HIS-613 AND ILE-791.
[6]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM LONG).
[9]"A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid."
Neumann E., Moser R., Snyers L., Blaas D., Hewat E.A.
J. Virol. 77:8504-8511(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HRV VP1.
[10]"The proprotein convertase PCSK9 induces the degradation of low density lipoprotein receptor (LDLR) and its closest family members VLDLR and ApoER2."
Poirier S., Mayer G., Benjannet S., Bergeron E., Marcinkiewicz J., Nassoury N., Mayer H., Nimpf J., Prat A., Seidah N.G.
J. Biol. Chem. 283:2363-2372(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PCSK9.
[11]"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 AT LYS-839 BY MYLIP, GLYCOSYLATION, MUTAGENESIS OF LYS-825; LYS-828 AND LYS-839.
[12]"X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein."
Verdaguer N., Fita I., Reithmayer M., Moser R., Blaas D.
Nat. Struct. Mol. Biol. 11:429-434(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 111-151 IN COMPLEX WITH HRV2.
[13]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-59 AND LYS-379.
[14]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[15]"Homozygous deletion of the very low density lipoprotein receptor gene causes autosomal recessive cerebellar hypoplasia with cerebral gyral simplification."
Boycott K.M., Flavelle S., Bureau A., Glass H.C., Fujiwara T.M., Wirrell E., Davey K., Chudley A.E., Scott J.N., McLeod D.R., Parboosingh J.S.
Am. J. Hum. Genet. 77:477-483(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CAMRQ1.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L20470 mRNA. Translation: AAA53684.1.
S73849 mRNA. Translation: AAB31735.1.
D16532 Genomic DNA. Translation: BAA03969.1.
D16493 mRNA. Translation: BAA03945.1.
D16494 mRNA. Translation: BAA03946.1.
L22431 mRNA. Translation: AAA61344.1.
DQ067198 Genomic DNA. Translation: AAY46157.1.
AL450467 Genomic DNA. Translation: CAH72454.1.
CH471071 Genomic DNA. Translation: EAW58805.1.
CH471071 Genomic DNA. Translation: EAW58806.1.
BC136562 mRNA. Translation: AAI36563.1.
CCDSCCDS34979.1. [P98155-2]
CCDS6446.1. [P98155-1]
PIRA49729.
RefSeqNP_001018066.1. NM_001018056.1. [P98155-2]
NP_003374.3. NM_003383.3. [P98155-1]
UniGeneHs.370422.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V9UX-ray3.605111-151[»]
3DPRX-ray3.50E113-151[»]
ProteinModelPortalP98155.
SMRP98155. Positions 33-753.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113277. 9 interactions.
DIPDIP-40925N.
IntActP98155. 1 interaction.
MINTMINT-111579.
STRING9606.ENSP00000371532.

PTM databases

PhosphoSiteP98155.

Polymorphism databases

DMDM1730111.

Proteomic databases

MaxQBP98155.
PaxDbP98155.
PRIDEP98155.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000382099; ENSP00000371531; ENSG00000147852. [P98155-2]
ENST00000382100; ENSP00000371532; ENSG00000147852. [P98155-1]
GeneID7436.
KEGGhsa:7436.
UCSCuc003zhk.1. human. [P98155-1]

Organism-specific databases

CTD7436.
GeneCardsGC09P002611.
GeneReviewsVLDLR.
HGNCHGNC:12698. VLDLR.
HPACAB032462.
HPA051312.
MIM192977. gene.
224050. phenotype.
neXtProtNX_P98155.
Orphanet1766. Dysequilibrium syndrome.
PharmGKBPA37317.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG255913.
HOGENOMHOG000115656.
HOVERGENHBG006250.
InParanoidP98155.
OMAMGTSARW.
OrthoDBEOG7NGQ9P.
PhylomeDBP98155.
TreeFamTF351700.

Gene expression databases

ArrayExpressP98155.
BgeeP98155.
CleanExHS_VLDLR.
GenevestigatorP98155.

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.
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]
SUPFAMSSF57424. 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

EvolutionaryTraceP98155.
GeneWikiVLDL_receptor.
GenomeRNAi7436.
NextBio29124.
PROP98155.
SOURCESearch...

Entry information

Entry nameVLDLR_HUMAN
AccessionPrimary (citable) accession number: P98155
Secondary accession number(s): B2RMZ7, D3DRH6, Q5VVF6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

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PDB cross-references

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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