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Database: UniProt
Entry: P98156
LinkDB: P98156
Original site: P98156 
ID   VLDLR_MOUSE             Reviewed;         873 AA.
AC   P98156; Q64022;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   13-FEB-2019, entry version 177.
DE   RecName: Full=Very low-density lipoprotein receptor;
DE            Short=VLDL receptor;
DE            Short=VLDL-R;
DE   Flags: Precursor;
GN   Name=Vldlr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Heart;
RX   PubMed=7925422; DOI=10.1111/j.1432-1033.1994.00975.x;
RA   Oka K., Ishimura-Oka K., Chu M.J., Sullivan M., Krushkal J., Li W.H.,
RA   Chan L.;
RT   "Mouse very-low-density-lipoprotein receptor (VLDLR) cDNA cloning,
RT   tissue-specific expression and evolutionary relationship with the low-
RT   density-lipoprotein receptor.";
RL   Eur. J. Biochem. 224:975-982(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=8013374; DOI=10.1210/endo.135.1.8013374;
RA   Gafvels M.E., Paavola L.G., Boyd C.O., Nolan P.M., Wittmaack F.,
RA   Chawla A., Lazar M.A., Bucan M., Angelin B.O., Strauss J.F.;
RT   "Cloning of a complementary deoxyribonucleic acid encoding the murine
RT   homolog of the very low density lipoprotein/apolipoprotein-E receptor:
RT   expression pattern and assignment of the gene to mouse chromosome
RT   19.";
RL   Endocrinology 135:387-394(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-262.
RX   PubMed=7919660; DOI=10.1007/BF00357008;
RA   Naggert J.K., Mu J.L.;
RT   "The mouse very low density lipoprotein receptor (Vldlr) gene maps to
RT   chromosome 19.";
RL   Mamm. Genome 5:453-455(1994).
RN   [4]
RP   INTERACTION WITH REELIN.
RX   PubMed=10571241; DOI=10.1016/S0896-6273(00)80861-2;
RA   Hiesberger T., Trommsdorff M., Howell B.W., Goffinet A.M., Mumby M.C.,
RA   Cooper J.A., Herz J.;
RT   "Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces
RT   tyrosine phosphorylation of disabled-1 and modulates tau
RT   phosphorylation.";
RL   Neuron 24:481-489(1999).
RN   [5]
RP   INTERACTION WITH SNX17.
RX   PubMed=12169628; DOI=10.1093/emboj/cdf435;
RA   Stockinger W., Sailler B., Strasser V., Recheis B., Fasching D.,
RA   Kahr L., Schneider W.J., Nimpf J.;
RT   "The PX-domain protein SNX17 interacts with members of the LDL
RT   receptor family and modulates endocytosis of the LDL receptor.";
RL   EMBO J. 21:4259-4267(2002).
RN   [6]
RP   INTERACTION WITH LDLRAP1.
RX   PubMed=12746448; DOI=10.1074/jbc.M304855200;
RA   Jones C., Hammer R.E., Li W.-P., Cohen J.C., Hobbs H.H., Herz J.;
RT   "Normal sorting but defective endocytosis of the low density
RT   lipoprotein receptor in mice with autosomal recessive
RT   hypercholesterolemia.";
RL   J. Biol. Chem. 278:29024-29030(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, and Heart;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   UBIQUITINATION.
RX   PubMed=20427281; DOI=10.1074/jbc.M110.123729;
RA   Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V.,
RA   Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D.,
RA   Nimpf J., van Berkel T.J., Tontonoz P., Zelcer N.;
RT   "The E3 ubiquitin ligase IDOL induces the degradation of the low
RT   density lipoprotein receptor family members VLDLR and ApoER2.";
RL   J. Biol. Chem. 285:19720-19726(2010).
CC   -!- FUNCTION: Binds VLDL and transports it into cells by endocytosis.
CC       In order to be internalized, the receptor-ligand complexes must
CC       first cluster into clathrin-coated pits. Binding to Reelin induces
CC       tyrosine phosphorylation of Dab1 and modulation of Tau
CC       phosphorylation.
CC   -!- SUBUNIT: Binds to the extracellular matrix protein Reelin.
CC       Interacts with DAB1. Interacts with VLDLR. Interacts with SNX17.
CC       Interacts with PCSK9 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Membrane, clathrin-coated pit; Single-pass type I
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Abundant in heart and muscle; less in kidney,
CC       brain, ovary, testis, lung and adipose tissue.
CC   -!- PTM: Ubiquitinated at Lys-839 by MYLIP leading to degradation.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: LRP8 and VLVLR together are required for correct
CC       embryonic development in the brain. Targeted disruption of both
CC       genes results in a phenotype virtually indistinguishable from that
CC       seen in "reeler" and "scrambler" mice. Subtle effects of VLDLR
CC       deletion are found mainly in the cerebellum, whereas lack of LRP8
CC       predominantly affects the positioning of the neurons in the
CC       neocortex.
DR   EMBL; L33417; AAC37668.1; -; mRNA.
DR   EMBL; U06670; AAA59384.1; -; mRNA.
DR   EMBL; S73732; AAB32228.2; -; Genomic_DNA.
DR   CCDS; CCDS29721.1; -.
DR   PIR; I48952; I48952.
DR   RefSeq; NP_001154892.1; NM_001161420.1.
DR   RefSeq; NP_038731.2; NM_013703.2.
DR   RefSeq; XP_006526980.1; XM_006526917.1.
DR   RefSeq; XP_006526981.1; XM_006526918.2.
DR   UniGene; Mm.4141; -.
DR   ProteinModelPortal; P98156; -.
DR   SMR; P98156; -.
DR   BioGrid; 204529; 3.
DR   DIP; DIP-33283N; -.
DR   IntAct; P98156; 3.
DR   MINT; P98156; -.
DR   STRING; 10090.ENSMUSP00000127329; -.
DR   iPTMnet; P98156; -.
DR   PhosphoSitePlus; P98156; -.
DR   MaxQB; P98156; -.
DR   PaxDb; P98156; -.
DR   PeptideAtlas; P98156; -.
DR   PRIDE; P98156; -.
DR   Ensembl; ENSMUST00000167487; ENSMUSP00000127329; ENSMUSG00000024924.
DR   GeneID; 22359; -.
DR   KEGG; mmu:22359; -.
DR   UCSC; uc008hbt.2; mouse.
DR   CTD; 7436; -.
DR   MGI; MGI:98935; Vldlr.
DR   eggNOG; ENOG410IPT5; Eukaryota.
DR   eggNOG; ENOG410YQ6J; LUCA.
DR   GeneTree; ENSGT00940000155460; -.
DR   HOGENOM; HOG000115656; -.
DR   HOVERGEN; HBG006250; -.
DR   InParanoid; P98156; -.
DR   KO; K20053; -.
DR   OrthoDB; 359795at2759; -.
DR   PhylomeDB; P98156; -.
DR   TreeFam; TF351700; -.
DR   Reactome; R-MMU-8866376; Reelin signalling pathway.
DR   Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-MMU-8964046; VLDL clearance.
DR   PRO; PR:P98156; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   Bgee; ENSMUSG00000024924; Expressed in 323 organ(s), highest expression level in decidua.
DR   ExpressionAtlas; P98156; baseline and differential.
DR   Genevisible; P98156; MM.
DR   GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR   GO; GO:0034437; F:glycoprotein transporter activity; ISO:MGI.
DR   GO; GO:0038025; F:reelin receptor activity; IMP:CACAO.
DR   GO; GO:0034189; F:very-low-density lipoprotein particle binding; ISO:MGI.
DR   GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; ISS:BHF-UCL.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:CACAO.
DR   GO; GO:0034436; P:glycoprotein transport; ISO:MGI.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:1900006; P:positive regulation of dendrite development; IGI:BHF-UCL.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IGI:MGI.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR   GO; GO:0038026; P:reelin-mediated signaling pathway; IGI:BHF-UCL.
DR   GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
DR   GO; GO:0034447; P:very-low-density lipoprotein particle clearance; ISS:BHF-UCL.
DR   CDD; cd00112; LDLa; 8.
DR   Gene3D; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR032931; VLDLR.
DR   PANTHER; PTHR43966:SF6; PTHR43966:SF6; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00057; Ldl_recept_a; 8.
DR   Pfam; PF00058; Ldl_recept_b; 5.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00192; LDLa; 8.
DR   SMART; SM00135; LY; 5.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   SUPFAM; SSF57424; SSF57424; 8.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 8.
DR   PROSITE; PS50068; LDLRA_2; 8.
DR   PROSITE; PS51120; LDLRB; 5.
PE   1: Evidence at protein level;
KW   Cholesterol metabolism; Coated pit; Complete proteome; Disulfide bond;
KW   EGF-like domain; Endocytosis; Glycoprotein; Isopeptide bond;
KW   Lipid metabolism; Lipid transport; Membrane; Receptor;
KW   Reference proteome; Repeat; Signal; Steroid metabolism;
KW   Sterol metabolism; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation; VLDL.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28    873       Very low-density lipoprotein receptor.
FT                                /FTId=PRO_0000017344.
FT   TOPO_DOM     28    797       Extracellular. {ECO:0000255}.
FT   TRANSMEM    798    819       Helical. {ECO:0000255}.
FT   TOPO_DOM    820    873       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       31     69       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN       70    110       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      111    151       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      152    190       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      191    231       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      237    275       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      276    314       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      316    355       LDL-receptor class A 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      356    391       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      396    431       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT      439    480       LDL-receptor class B 1.
FT   REPEAT      481    524       LDL-receptor class B 2.
FT   REPEAT      525    567       LDL-receptor class B 3.
FT   REPEAT      568    611       LDL-receptor class B 4.
FT   REPEAT      612    654       LDL-receptor class B 5.
FT   REPEAT      655    697       LDL-receptor class B 6.
FT   DOMAIN      702    750       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REGION      751    790       Clustered O-linked oligosaccharides.
FT   MOTIF       832    837       Endocytosis signal. {ECO:0000255}.
FT   CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    765    765       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    781    781       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     33     45       {ECO:0000250}.
FT   DISULFID     40     58       {ECO:0000250}.
FT   DISULFID     52     67       {ECO:0000250}.
FT   DISULFID     72     84       {ECO:0000250}.
FT   DISULFID     79     97       {ECO:0000250}.
FT   DISULFID     91    108       {ECO:0000250}.
FT   DISULFID    113    127       {ECO:0000250}.
FT   DISULFID    120    140       {ECO:0000250}.
FT   DISULFID    134    149       {ECO:0000250}.
FT   DISULFID    154    166       {ECO:0000250}.
FT   DISULFID    161    179       {ECO:0000250}.
FT   DISULFID    173    188       {ECO:0000250}.
FT   DISULFID    193    205       {ECO:0000250}.
FT   DISULFID    200    218       {ECO:0000250}.
FT   DISULFID    212    229       {ECO:0000250}.
FT   DISULFID    239    251       {ECO:0000250}.
FT   DISULFID    246    264       {ECO:0000250}.
FT   DISULFID    258    273       {ECO:0000250}.
FT   DISULFID    278    290       {ECO:0000250}.
FT   DISULFID    285    303       {ECO:0000250}.
FT   DISULFID    297    312       {ECO:0000250}.
FT   DISULFID    318    331       {ECO:0000250}.
FT   DISULFID    326    344       {ECO:0000250}.
FT   DISULFID    338    355       {ECO:0000250}.
FT   DISULFID    360    371       {ECO:0000250}.
FT   DISULFID    367    380       {ECO:0000250}.
FT   DISULFID    382    394       {ECO:0000250}.
FT   DISULFID    400    410       {ECO:0000250}.
FT   DISULFID    406    419       {ECO:0000250}.
FT   DISULFID    421    434       {ECO:0000250}.
FT   DISULFID    706    719       {ECO:0000250}.
FT   DISULFID    715    734       {ECO:0000250}.
FT   DISULFID    736    749       {ECO:0000250}.
FT   CROSSLNK    839    839       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:P98155}.
FT   CONFLICT    161    161       C -> G (in Ref. 1; AAC37668).
FT                                {ECO:0000305}.
FT   CONFLICT    262    262       P -> L (in Ref. 3; AAB32228).
FT                                {ECO:0000305}.
FT   CONFLICT    297    297       C -> S (in Ref. 2; AAA59384).
FT                                {ECO:0000305}.
SQ   SEQUENCE   873 AA;  96373 MW;  08F09F93825195CB CRC64;
     MGTSARWALW LLLALCWAPR DSGATASGKK AKCDSSQFQC TNGRCITLLW KCDGDEDCAD
     GSDEKNCVKK TCAESDFVCK NGQCVPNRWQ CDGDPDCEDG SDESPEQCHM RTCRINEISC
     GARSTQCIPV SWRCDGENDC DNGEDEENCG NITCSADEFT CSSGRCVSRN FVCNGQDDCD
     DGSDELDCAP PTCGAHEFQC STSSCIPLSW VCDDDADCSD QSDESLEQCG RQPVIHTKCP
     TSEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI
     RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDMSKVCDQ EQDCRDWSDE PLKECHINEC
     LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE
     CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA
     QKLFWADLSQ KAIFSASIDD KVGRHFKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA
     TLDGAKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTEDIQ
     WPNGITLDLV KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI
     DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP SGKNWCEDDM ENGGCEYLCL
     PAPQINDHSP KYTCSCPNGY NLEENGRECQ STSTPVTYSE TKDINTTDIL RTSGLVPGGI
     NVTTAVSEVS VPPKGTSAAW AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT
     TEEDLSIDIG RHSASVGHTY PAISVVSTDD DLA
//
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