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P98156

- VLDLR_MOUSE

UniProt

P98156 - VLDLR_MOUSE

Protein

Very low-density lipoprotein receptor

Gene

Vldlr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (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.

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. glycoprotein transporter activity Source: Ensembl
    3. protein binding Source: MGI
    4. reelin receptor activity Source: BHF-UCL
    5. very-low-density lipoprotein particle binding Source: Ensembl
    6. very-low-density lipoprotein particle receptor activity Source: BHF-UCL

    GO - Biological processi

    1. cholesterol metabolic process Source: UniProtKB-KW
    2. lipid transport Source: UniProtKB-KW
    3. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    4. positive regulation of dendrite development Source: BHF-UCL
    5. positive regulation of protein kinase activity Source: MGI
    6. reelin-mediated signaling pathway Source: BHF-UCL
    7. ventral spinal cord development Source: UniProtKB
    8. 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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:98935. Vldlr.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Coated pit, Membrane, VLDL

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 873846Very low-density lipoprotein receptorPRO_0000017344Add
    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 ↔ 127By similarity
    Disulfide bondi120 ↔ 140By similarity
    Disulfide bondi134 ↔ 149By similarity
    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)By similarity

    Post-translational modificationi

    Ubiquitinated at Lys-839 by MYLIP leading to degradation.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP98156.
    PaxDbiP98156.
    PRIDEiP98156.

    Expressioni

    Tissue specificityi

    Abundant in heart and muscle; less in kidney, brain, ovary, testis, lung and adipose tissue.

    Gene expression databases

    ArrayExpressiP98156.
    BgeeiP98156.
    CleanExiMM_VLDLR.
    GenevestigatoriP98156.

    Interactioni

    Subunit structurei

    Binds to the extracellular matrix protein Reelin. Interacts with DAB1. Interacts with VLDLR. Interacts with SNX17. Interacts with PCSK9 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204529. 3 interactions.
    DIPiDIP-33283N.
    IntActiP98156. 2 interactions.
    MINTiMINT-4140012.

    Structurei

    3D structure databases

    ProteinModelPortaliP98156.
    SMRiP98156. Positions 21-789.
    ModBaseiSearch...
    MobiDBiSearch...

    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 – 39136EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini396 – 43136EGF-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.
    GeneTreeiENSGT00740000114992.
    HOGENOMiHOG000115656.
    HOVERGENiHBG006250.
    InParanoidiP98156.
    OMAiMGTSARW.
    PhylomeDBiP98156.
    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.
    IPR009030. Growth_fac_rcpt_N_dom.
    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]
    SUPFAMiSSF57184. SSF57184. 2 hits.
    SSF57424. 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]

    Sequencei

    Sequence statusi: Complete.

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

    P98156-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGTSARWALW LLLALCWAPR DSGATASGKK AKCDSSQFQC TNGRCITLLW    50
    KCDGDEDCAD GSDEKNCVKK TCAESDFVCK NGQCVPNRWQ CDGDPDCEDG 100
    SDESPEQCHM RTCRINEISC GARSTQCIPV SWRCDGENDC DNGEDEENCG 150
    NITCSADEFT CSSGRCVSRN FVCNGQDDCD DGSDELDCAP PTCGAHEFQC 200
    STSSCIPLSW VCDDDADCSD QSDESLEQCG RQPVIHTKCP TSEIQCGSGE 250
    CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI 300
    RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDMSKVCDQ EQDCRDWSDE 350
    PLKECHINEC LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC 400
    QNPGICSQIC INLKGGYKCE CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD 450
    IRKIGLERKE YIQLVEQLRN TVALDADIAA QKLFWADLSQ KAIFSASIDD 500
    KVGRHFKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA TLDGAKRKFL 550
    FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTEDIQ 600
    WPNGITLDLV KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL 650
    TIFEDRVYWI DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP 700
    SGKNWCEDDM ENGGCEYLCL PAPQINDHSP KYTCSCPNGY NLEENGRECQ 750
    STSTPVTYSE TKDINTTDIL RTSGLVPGGI NVTTAVSEVS VPPKGTSAAW 800
    AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT TEEDLSIDIG 850
    RHSASVGHTY PAISVVSTDD DLA 873
    Length:873
    Mass (Da):96,373
    Last modified:October 1, 1996 - v1
    Checksum:i08F09F93825195CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti161 – 1611C → G in AAC37668. (PubMed:7925422)Curated
    Sequence conflicti262 – 2621P → L in AAB32228. (PubMed:7919660)Curated
    Sequence conflicti297 – 2971C → S in AAA59384. (PubMed:8013374)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33417 mRNA. Translation: AAC37668.1.
    U06670 mRNA. Translation: AAA59384.1.
    S73732 Genomic DNA. Translation: AAB32228.2.
    CCDSiCCDS29721.1.
    PIRiI48952.
    RefSeqiNP_001154892.1. NM_001161420.1.
    NP_038731.2. NM_013703.2.
    XP_006526980.1. XM_006526917.1.
    XP_006526981.1. XM_006526918.1.
    UniGeneiMm.4141.

    Genome annotation databases

    EnsembliENSMUST00000167487; ENSMUSP00000127329; ENSMUSG00000024924.
    GeneIDi22359.
    KEGGimmu:22359.
    UCSCiuc008hbt.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L33417 mRNA. Translation: AAC37668.1 .
    U06670 mRNA. Translation: AAA59384.1 .
    S73732 Genomic DNA. Translation: AAB32228.2 .
    CCDSi CCDS29721.1.
    PIRi I48952.
    RefSeqi NP_001154892.1. NM_001161420.1.
    NP_038731.2. NM_013703.2.
    XP_006526980.1. XM_006526917.1.
    XP_006526981.1. XM_006526918.1.
    UniGenei Mm.4141.

    3D structure databases

    ProteinModelPortali P98156.
    SMRi P98156. Positions 21-789.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204529. 3 interactions.
    DIPi DIP-33283N.
    IntActi P98156. 2 interactions.
    MINTi MINT-4140012.

    Proteomic databases

    MaxQBi P98156.
    PaxDbi P98156.
    PRIDEi P98156.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000167487 ; ENSMUSP00000127329 ; ENSMUSG00000024924 .
    GeneIDi 22359.
    KEGGi mmu:22359.
    UCSCi uc008hbt.2. mouse.

    Organism-specific databases

    CTDi 7436.
    MGIi MGI:98935. Vldlr.

    Phylogenomic databases

    eggNOGi NOG255913.
    GeneTreei ENSGT00740000114992.
    HOGENOMi HOG000115656.
    HOVERGENi HBG006250.
    InParanoidi P98156.
    OMAi MGTSARW.
    PhylomeDBi P98156.
    TreeFami TF351700.

    Miscellaneous databases

    NextBioi 302661.
    PROi P98156.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P98156.
    Bgeei P98156.
    CleanExi MM_VLDLR.
    Genevestigatori P98156.

    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.
    IPR009030. Growth_fac_rcpt_N_dom.
    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 SSF57184. SSF57184. 2 hits.
    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. "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.

    Entry informationi

    Entry nameiVLDLR_MOUSE
    AccessioniPrimary (citable) accession number: P98156
    Secondary accession number(s): Q64022
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 145 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3