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P98155

- VLDLR_HUMAN

UniProt

P98155 - VLDLR_HUMAN

Protein

Very low-density lipoprotein receptor

Gene

VLDLR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Molecular functioni

    1. apolipoprotein binding Source: BHF-UCL
    2. calcium-dependent protein binding Source: BHF-UCL
    3. calcium ion binding Source: InterPro
    4. glycoprotein binding Source: BHF-UCL
    5. glycoprotein transporter activity Source: BHF-UCL
    6. low-density lipoprotein receptor activity Source: ProtInc
    7. protein binding Source: IntAct
    8. reelin receptor activity Source: BHF-UCL
    9. very-low-density lipoprotein particle binding Source: BHF-UCL
    10. very-low-density lipoprotein particle receptor activity Source: BHF-UCL

    GO - Biological processi

    1. cholesterol metabolic process Source: UniProtKB-KW
    2. glycoprotein transport Source: BHF-UCL
    3. lipid transport Source: UniProtKB-KW
    4. memory Source: ProtInc
    5. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    6. nervous system development Source: ProtInc
    7. positive regulation of dendrite development Source: BHF-UCL
    8. positive regulation of protein kinase activity Source: Ensembl
    9. receptor-mediated endocytosis Source: BHF-UCL
    10. reelin-mediated signaling pathway Source: BHF-UCL
    11. signal transduction Source: ProtInc
    12. ventral spinal cord development Source: Ensembl
    13. very-low-density lipoprotein particle clearance Source: BHF-UCL

    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:
    Very low-density lipoprotein receptor
    Short name:
    VLDL receptor
    Short name:
    VLDL-R
    Gene namesi
    Name:VLDLR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:12698. VLDLR.

    Subcellular locationi

    GO - Cellular componenti

    1. coated pit Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: MGI
    4. plasma membrane Source: ProtInc
    5. receptor complex Source: MGI
    6. very-low-density lipoprotein particle Source: UniProtKB-KW

    Keywords - Cellular componenti

    Coated pit, Membrane, VLDL

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi825 – 8251K → R: Insensitive to MYLIP-triggered degradation; when associated with R-828 and R-839. 1 Publication
    Mutagenesisi828 – 8281K → R: Insensitive to MYLIP-triggered degradation; when associated with R-825 and R-839. 1 Publication
    Mutagenesisi839 – 8391K → R: Insensitive to MYLIP-triggered degradation. Insensitive to MYLIP-triggered degradation; when associated with R-825 and R-828. 1 Publication

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi224050. phenotype.
    Orphaneti1766. Dysequilibrium syndrome.
    PharmGKBiPA37317.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 873846Very low-density lipoprotein receptorPRO_0000017343Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi33 ↔ 45By similarity
    Disulfide bondi40 ↔ 58By similarity
    Disulfide bondi52 ↔ 67By similarity
    Disulfide bondi72 ↔ 84By similarity
    Disulfide bondi79 ↔ 97By similarity
    Disulfide bondi91 ↔ 108By similarity
    Disulfide bondi113 ↔ 127
    Disulfide bondi120 ↔ 140
    Disulfide bondi134 ↔ 149
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi154 ↔ 166By similarity
    Disulfide bondi161 ↔ 179By similarity
    Disulfide bondi173 ↔ 188By similarity
    Disulfide bondi193 ↔ 205By similarity
    Disulfide bondi200 ↔ 218By similarity
    Disulfide bondi212 ↔ 229By similarity
    Disulfide bondi239 ↔ 251By similarity
    Disulfide bondi246 ↔ 264By similarity
    Disulfide bondi258 ↔ 273By similarity
    Disulfide bondi278 ↔ 290By similarity
    Disulfide bondi285 ↔ 303By similarity
    Disulfide bondi297 ↔ 312By similarity
    Disulfide bondi318 ↔ 331By similarity
    Disulfide bondi326 ↔ 344By similarity
    Disulfide bondi338 ↔ 355By similarity
    Disulfide bondi360 ↔ 371By similarity
    Disulfide bondi367 ↔ 380By similarity
    Disulfide bondi382 ↔ 394By similarity
    Disulfide bondi400 ↔ 410By similarity
    Disulfide bondi406 ↔ 419By similarity
    Disulfide bondi421 ↔ 434By similarity
    Disulfide bondi706 ↔ 719By similarity
    Disulfide bondi715 ↔ 734By similarity
    Disulfide bondi736 ↔ 749By similarity
    Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi781 – 7811N-linked (GlcNAc...)Sequence Analysis
    Cross-linki839 – 839Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    Ubiquitinated at Lys-839 by MYLIP leading to degradation.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP98155.
    PaxDbiP98155.
    PRIDEiP98155.

    PTM databases

    PhosphoSiteiP98155.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP98155.
    BgeeiP98155.
    CleanExiHS_VLDLR.
    GenevestigatoriP98155.

    Organism-specific databases

    HPAiCAB032462.
    HPA051312.

    Interactioni

    Subunit structurei

    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.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRPAP1P305334EBI-9004309,EBI-715927
    Lrpap1Q990682EBI-9004309,EBI-919734From a different organism.
    RelnQ608414EBI-9004309,EBI-9248666From a different organism.

    Protein-protein interaction databases

    BioGridi113277. 9 interactions.
    DIPiDIP-40925N.
    IntActiP98155. 3 interactions.
    MINTiMINT-111579.
    STRINGi9606.ENSP00000371532.

    Structurei

    Secondary structure

    1
    873
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni115 – 1173
    Beta strandi121 – 1255
    Beta strandi132 – 1376
    Turni141 – 1455

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V9UX-ray3.605111-151[»]
    3DPRX-ray3.50E113-151[»]
    ProteinModelPortaliP98155.
    SMRiP98155. Positions 33-753.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP98155.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 797770ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini820 – 87354CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei798 – 81922HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 6939LDL-receptor class A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini70 – 11041LDL-receptor class A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini111 – 15141LDL-receptor class A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini152 – 19039LDL-receptor class A 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini191 – 23141LDL-receptor class A 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 27539LDL-receptor class A 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini276 – 31439LDL-receptor class A 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini316 – 35540LDL-receptor class A 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini356 – 39540EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini396 – 43540EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Repeati439 – 48042LDL-receptor class B 1Add
    BLAST
    Repeati481 – 52444LDL-receptor class B 2Add
    BLAST
    Repeati525 – 56743LDL-receptor class B 3Add
    BLAST
    Repeati568 – 61144LDL-receptor class B 4Add
    BLAST
    Repeati612 – 65443LDL-receptor class B 5Add
    BLAST
    Repeati655 – 69743LDL-receptor class B 6Add
    BLAST
    Domaini702 – 75049EGF-like 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni751 – 79040Clustered O-linked oligosaccharidesAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi832 – 8376Endocytosis signalSequence Analysis

    Sequence similaritiesi

    Contains 3 EGF-like domains.PROSITE-ProRule annotation
    Contains 8 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

    eggNOGiNOG255913.
    HOGENOMiHOG000115656.
    HOVERGENiHBG006250.
    InParanoidiP98155.
    OMAiMGTSARW.
    OrthoDBiEOG7NGQ9P.
    PhylomeDBiP98155.
    TreeFamiTF351700.

    Family and domain databases

    Gene3Di2.120.10.30. 1 hit.
    4.10.400.10. 8 hits.
    InterProiIPR011042. 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]
    PfamiPF07645. EGF_CA. 1 hit.
    PF00057. Ldl_recept_a. 8 hits.
    PF00058. Ldl_recept_b. 5 hits.
    [Graphical view]
    PRINTSiPR00261. LDLRECEPTOR.
    SMARTiSM00181. EGF. 1 hit.
    SM00179. EGF_CA. 2 hits.
    SM00192. LDLa. 8 hits.
    SM00135. LY. 5 hits.
    [Graphical view]
    SUPFAMiSSF57424. SSF57424. 8 hits.
    PROSITEiPS00010. 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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P98155-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGTSALWALW LLLALCWAPR ESGATGTGRK AKCEPSQFQC TNGRCITLLW    50
    KCDGDEDCVD GSDEKNCVKK TCAESDFVCN NGQCVPSRWK CDGDPDCEDG 100
    SDESPEQCHM RTCRIHEISC GAHSTQCIPV SWRCDGENDC DSGEDEENCG 150
    NITCSPDEFT CSSGRCISRN FVCNGQDDCS DGSDELDCAP PTCGAHEFQC 200
    STSSCIPISW VCDDDADCSD QSDESLEQCG RQPVIHTKCP ASEIQCGSGE 250
    CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI 300
    RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDISKVCNQ EQDCRDWSDE 350
    PLKECHINEC LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC 400
    QNPGICSQIC INLKGGYKCE CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD 450
    IRKIGLERKE YIQLVEQLRN TVALDADIAA QKLFWADLSQ KAIFSASIDD 500
    KVGRHVKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA TLDGTKRKFL 550
    FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTADIQ 600
    WPNGITLDLI KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL 650
    TIFEDRVYWI DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP 700
    SGKNWCEEDM ENGGCEYLCL PAPQINDHSP KYTCSCPSGY NVEENGRDCQ 750
    STATTVTYSE TKDTNTTEIS ATSGLVPGGI NVTTAVSEVS VPPKGTSAAW 800
    AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT TEEDLSIDIG 850
    RHSASVGHTY PAISVVSTDD DLA 873
    Length:873
    Mass (Da):96,098
    Last modified:October 1, 1996 - v1
    Checksum:i8BAC29438A78C2B8
    GO
    Isoform Short (identifier: P98155-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:845
    Mass (Da):93,383
    Checksum:i588311D7C6B2C1FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91L → V in AAA53684. (PubMed:8128315)Curated
    Sequence conflicti13 – 131L → V in AAA61344. (PubMed:8020981)Curated
    Sequence conflicti424 – 4241G → A in AAA53684. (PubMed:8128315)Curated
    Sequence conflicti678 – 6781L → H in AAA53684. (PubMed:8128315)Curated
    Sequence conflicti766 – 7661T → S in AAA61344. (PubMed:8020981)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591V → I.2 Publications
    Corresponds to variant rs6149 [ dbSNP | Ensembl ].
    VAR_011865
    Natural varianti262 – 2621P → H.1 Publication
    Corresponds to variant rs34761707 [ dbSNP | Ensembl ].
    VAR_025063
    Natural varianti379 – 3791E → K.1 Publication
    Corresponds to variant rs6146 [ dbSNP | Ensembl ].
    VAR_011866
    Natural varianti464 – 4641L → I.1 Publication
    Corresponds to variant rs34753566 [ dbSNP | Ensembl ].
    VAR_025064
    Natural varianti561 – 5611I → V.1 Publication
    Corresponds to variant rs35724190 [ dbSNP | Ensembl ].
    VAR_025065
    Natural varianti613 – 6131R → H.1 Publication
    Corresponds to variant rs35948251 [ dbSNP | Ensembl ].
    VAR_025066
    Natural varianti791 – 7911V → I.1 Publication
    Corresponds to variant rs35334949 [ dbSNP | Ensembl ].
    VAR_025067

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei751 – 77929STATT…LVPGG → R in isoform Short. CuratedVSP_004304Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS34979.1. [P98155-2]
    CCDS6446.1. [P98155-1]
    PIRiA49729.
    RefSeqiNP_001018066.1. NM_001018056.1. [P98155-2]
    NP_003374.3. NM_003383.3. [P98155-1]
    UniGeneiHs.370422.

    Genome annotation databases

    EnsembliENST00000382099; ENSP00000371531; ENSG00000147852. [P98155-2]
    ENST00000382100; ENSP00000371532; ENSG00000147852. [P98155-1]
    GeneIDi7436.
    KEGGihsa:7436.
    UCSCiuc003zhk.1. human. [P98155-1]

    Polymorphism databases

    DMDMi1730111.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS34979.1. [P98155-2 ]
    CCDS6446.1. [P98155-1 ]
    PIRi A49729.
    RefSeqi NP_001018066.1. NM_001018056.1. [P98155-2 ]
    NP_003374.3. NM_003383.3. [P98155-1 ]
    UniGenei Hs.370422.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1V9U X-ray 3.60 5 111-151 [» ]
    3DPR X-ray 3.50 E 113-151 [» ]
    ProteinModelPortali P98155.
    SMRi P98155. Positions 33-753.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113277. 9 interactions.
    DIPi DIP-40925N.
    IntActi P98155. 3 interactions.
    MINTi MINT-111579.
    STRINGi 9606.ENSP00000371532.

    PTM databases

    PhosphoSitei P98155.

    Polymorphism databases

    DMDMi 1730111.

    Proteomic databases

    MaxQBi P98155.
    PaxDbi P98155.
    PRIDEi P98155.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000382099 ; ENSP00000371531 ; ENSG00000147852 . [P98155-2 ]
    ENST00000382100 ; ENSP00000371532 ; ENSG00000147852 . [P98155-1 ]
    GeneIDi 7436.
    KEGGi hsa:7436.
    UCSCi uc003zhk.1. human. [P98155-1 ]

    Organism-specific databases

    CTDi 7436.
    GeneCardsi GC09P002611.
    GeneReviewsi VLDLR.
    HGNCi HGNC:12698. VLDLR.
    HPAi CAB032462.
    HPA051312.
    MIMi 192977. gene.
    224050. phenotype.
    neXtProti NX_P98155.
    Orphaneti 1766. Dysequilibrium syndrome.
    PharmGKBi PA37317.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255913.
    HOGENOMi HOG000115656.
    HOVERGENi HBG006250.
    InParanoidi P98155.
    OMAi MGTSARW.
    OrthoDBi EOG7NGQ9P.
    PhylomeDBi P98155.
    TreeFami TF351700.

    Miscellaneous databases

    EvolutionaryTracei P98155.
    GeneWikii VLDL_receptor.
    GenomeRNAii 7436.
    NextBioi 29124.
    PROi P98155.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P98155.
    Bgeei P98155.
    CleanExi HS_VLDLR.
    Genevestigatori P98155.

    Family and domain databases

    Gene3Di 2.120.10.30. 1 hit.
    4.10.400.10. 8 hits.
    InterProi IPR011042. 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 ]
    Pfami PF07645. EGF_CA. 1 hit.
    PF00057. Ldl_recept_a. 8 hits.
    PF00058. Ldl_recept_b. 5 hits.
    [Graphical view ]
    PRINTSi PR00261. LDLRECEPTOR.
    SMARTi SM00181. EGF. 1 hit.
    SM00179. EGF_CA. 2 hits.
    SM00192. LDLa. 8 hits.
    SM00135. LY. 5 hits.
    [Graphical view ]
    SUPFAMi SSF57424. SSF57424. 8 hits.
    PROSITEi PS00010. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: VARIANTS ILE-59 AND LYS-379.
    14. "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.

    Entry informationi

    Entry nameiVLDLR_HUMAN
    AccessioniPrimary (citable) accession number: P98155
    Secondary accession number(s): B2RMZ7, D3DRH6, Q5VVF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 156 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3