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Database: UniProt
Entry: P98155
LinkDB: P98155
Original site: P98155 
ID   VLDLR_HUMAN             Reviewed;         873 AA.
AC   P98155; B2RMZ7; D3DRH6; Q5VVF6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   13-FEB-2019, entry version 195.
DE   RecName: Full=Very low-density lipoprotein receptor;
DE            Short=VLDL receptor;
DE            Short=VLDL-R;
DE   Flags: Precursor;
GN   Name=VLDLR;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=8128315; DOI=10.1007/BF01233382;
RA   Gafvels M.E., Caird M., Britt D., Jackson C.L., Patterson D.,
RA   Strauss J.F.;
RT   "Cloning of a cDNA encoding a putative human very low density
RT   lipoprotein/apolipoprotein E receptor and assignment of the gene to
RT   chromosome 9pter-p23.";
RL   Somat. Cell Mol. Genet. 19:557-569(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=8069294; DOI=10.1093/hmg/3.4.531;
RA   Webb J.C., Patel D.D., Jones M.D., Knight B.L., Soutar A.K.;
RT   "Characterization and tissue-specific expression of the human 'very
RT   low density lipoprotein (VLDL) receptor' mRNA.";
RL   Hum. Mol. Genet. 3:531-537(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=8294473;
RA   Sakai J., Hoshino A., Takahashi S., Miura Y., Ishii H., Suzuki H.,
RA   Kawarabayasi Y., Yamamoto T.;
RT   "Structure, chromosome location, and expression of the human very low
RT   density lipoprotein receptor gene.";
RL   J. Biol. Chem. 269:2173-2182(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=8020981; DOI=10.1006/geno.1994.1171;
RA   Oka K., Tzung K.W., Sullivan M., Lindsay E., Baldini A., Chan L.;
RT   "Human very-low-density lipoprotein receptor complementary DNA and
RT   deduced amino acid sequence and localization of its gene (VLDLR) to
RT   chromosome band 9p24 by fluorescence in situ hybridization.";
RL   Genomics 20:298-300(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-59; HIS-262;
RP   ILE-464; VAL-561; HIS-613 AND ILE-791.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   INTERACTION WITH HRV VP1.
RX   PubMed=12857919; DOI=10.1128/JVI.77.15.8504-8511.2003;
RA   Neumann E., Moser R., Snyers L., Blaas D., Hewat E.A.;
RT   "A cellular receptor of human rhinovirus type 2, the very-low-density
RT   lipoprotein receptor, binds to two neighboring proteins of the viral
RT   capsid.";
RL   J. Virol. 77:8504-8511(2003).
RN   [10]
RP   INTERACTION WITH PCSK9.
RX   PubMed=18039658; DOI=10.1074/jbc.M708098200;
RA   Poirier S., Mayer G., Benjannet S., Bergeron E., Marcinkiewicz J.,
RA   Nassoury N., Mayer H., Nimpf J., Prat A., Seidah N.G.;
RT   "The proprotein convertase PCSK9 induces the degradation of low
RT   density lipoprotein receptor (LDLR) and its closest family members
RT   VLDLR and ApoER2.";
RL   J. Biol. Chem. 283:2363-2372(2008).
RN   [11]
RP   UBIQUITINATION AT LYS-839 BY MYLIP, GLYCOSYLATION, AND MUTAGENESIS OF
RP   LYS-825; LYS-828 AND LYS-839.
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).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 111-151 IN COMPLEX WITH HRV2.
RX   PubMed=15064754; DOI=10.1038/nsmb753;
RA   Verdaguer N., Fita I., Reithmayer M., Moser R., Blaas D.;
RT   "X-ray structure of a minor group human rhinovirus bound to a fragment
RT   of its cellular receptor protein.";
RL   Nat. Struct. Mol. Biol. 11:429-434(2004).
RN   [13]
RP   VARIANTS ILE-59 AND LYS-379.
RX   PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions
RT   of human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [14]
RP   ERRATUM.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
RN   [15]
RP   INVOLVEMENT IN CAMRQ1.
RX   PubMed=16080122; DOI=10.1086/444400;
RA   Boycott K.M., Flavelle S., Bureau A., Glass H.C., Fujiwara T.M.,
RA   Wirrell E., Davey K., Chudley A.E., Scott J.N., McLeod D.R.,
RA   Parboosingh J.S.;
RT   "Homozygous deletion of the very low density lipoprotein receptor gene
RT   causes autosomal recessive cerebellar hypoplasia with cerebral gyral
RT   simplification.";
RL   Am. J. Hum. Genet. 77:477-483(2005).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the extracellular matrix protein Reelin.
CC       Interacts with VLDLR. Interacts with SNX17 (By similarity).
CC       Interacts with DAB1. Receptor for the minor-group human
CC       rhinoviruses (HRVs); binds protein VP1 through the second and
CC       third LDL-receptor class A domains. Interacts with PCSK9.
CC       {ECO:0000250, ECO:0000269|PubMed:12857919,
CC       ECO:0000269|PubMed:15064754, ECO:0000269|PubMed:18039658}.
CC   -!- INTERACTION:
CC       P30533:LRPAP1; NbExp=5; IntAct=EBI-9004309, EBI-715927;
CC       Q99068:Lrpap1 (xeno); NbExp=2; IntAct=EBI-9004309, EBI-919734;
CC       Q60841:Reln (xeno); NbExp=7; IntAct=EBI-9004309, EBI-9248666;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Membrane, clathrin-coated pit; Single-pass type I
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P98155-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P98155-2; Sequence=VSP_004304;
CC   -!- TISSUE SPECIFICITY: Abundant in heart and skeletal muscle; also
CC       ovary and kidney; not in liver.
CC   -!- PTM: Ubiquitinated at Lys-839 by MYLIP leading to degradation.
CC       {ECO:0000269|PubMed:20427281}.
CC   -!- DISEASE: Cerebellar ataxia, mental retardation, and dysequilibrium
CC       syndrome 1 (CAMRQ1) [MIM:224050]: A congenital, non-progressive
CC       cerebellar ataxia associated with disturbed equilibrium, delayed
CC       ambulation, mental retardation, cerebellar hypoplasia and mild
CC       cerebral gyral simplification. Additional features include short
CC       stature, strabismus, pes planus and, rarely, seizures.
CC       {ECO:0000269|PubMed:16080122}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/vldlr/";
DR   EMBL; L20470; AAA53684.1; -; mRNA.
DR   EMBL; S73849; AAB31735.1; -; mRNA.
DR   EMBL; D16532; BAA03969.1; -; Genomic_DNA.
DR   EMBL; D16493; BAA03945.1; -; mRNA.
DR   EMBL; D16494; BAA03946.1; -; mRNA.
DR   EMBL; L22431; AAA61344.1; -; mRNA.
DR   EMBL; DQ067198; AAY46157.1; -; Genomic_DNA.
DR   EMBL; AL450467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58805.1; -; Genomic_DNA.
DR   EMBL; CH471071; EAW58806.1; -; Genomic_DNA.
DR   EMBL; BC136562; AAI36563.1; -; mRNA.
DR   CCDS; CCDS34979.1; -. [P98155-2]
DR   CCDS; CCDS6446.1; -. [P98155-1]
DR   PIR; A49729; A49729.
DR   RefSeq; NP_001018066.1; NM_001018056.2. [P98155-2]
DR   RefSeq; NP_003374.3; NM_003383.4. [P98155-1]
DR   UniGene; Hs.370422; -.
DR   PDB; 1V9U; X-ray; 3.60 A; 5=111-151.
DR   PDB; 3DPR; X-ray; 3.50 A; E=113-151.
DR   PDB; 6BYV; NMR; -; A=70-190.
DR   PDBsum; 1V9U; -.
DR   PDBsum; 3DPR; -.
DR   PDBsum; 6BYV; -.
DR   ProteinModelPortal; P98155; -.
DR   SMR; P98155; -.
DR   BioGrid; 113277; 12.
DR   DIP; DIP-40925N; -.
DR   IntAct; P98155; 5.
DR   STRING; 9606.ENSP00000371532; -.
DR   DrugBank; DB03017; Lauric Acid.
DR   iPTMnet; P98155; -.
DR   PhosphoSitePlus; P98155; -.
DR   BioMuta; VLDLR; -.
DR   DMDM; 1730111; -.
DR   EPD; P98155; -.
DR   jPOST; P98155; -.
DR   MaxQB; P98155; -.
DR   PaxDb; P98155; -.
DR   PeptideAtlas; P98155; -.
DR   PRIDE; P98155; -.
DR   ProteomicsDB; 57794; -.
DR   ProteomicsDB; 57795; -. [P98155-2]
DR   Ensembl; ENST00000382099; ENSP00000371531; ENSG00000147852. [P98155-2]
DR   Ensembl; ENST00000382100; ENSP00000371532; ENSG00000147852. [P98155-1]
DR   GeneID; 7436; -.
DR   KEGG; hsa:7436; -.
DR   UCSC; uc003zhk.2; human. [P98155-1]
DR   CTD; 7436; -.
DR   DisGeNET; 7436; -.
DR   EuPathDB; HostDB:ENSG00000147852.15; -.
DR   GeneCards; VLDLR; -.
DR   GeneReviews; VLDLR; -.
DR   HGNC; HGNC:12698; VLDLR.
DR   HPA; CAB032462; -.
DR   HPA; HPA051312; -.
DR   MalaCards; VLDLR; -.
DR   MIM; 192977; gene.
DR   MIM; 224050; phenotype.
DR   neXtProt; NX_P98155; -.
DR   OpenTargets; ENSG00000147852; -.
DR   Orphanet; 1766; Dysequilibrium syndrome.
DR   PharmGKB; PA37317; -.
DR   eggNOG; ENOG410IPT5; Eukaryota.
DR   eggNOG; ENOG410YQ6J; LUCA.
DR   GeneTree; ENSGT00940000155460; -.
DR   HOGENOM; HOG000115656; -.
DR   HOVERGEN; HBG006250; -.
DR   InParanoid; P98155; -.
DR   KO; K20053; -.
DR   OMA; PCLPHEY; -.
DR   OrthoDB; 359795at2759; -.
DR   PhylomeDB; P98155; -.
DR   TreeFam; TF351700; -.
DR   Reactome; R-HSA-8866376; Reelin signalling pathway.
DR   Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-HSA-8964046; VLDL clearance.
DR   SIGNOR; P98155; -.
DR   EvolutionaryTrace; P98155; -.
DR   GeneWiki; VLDL_receptor; -.
DR   GenomeRNAi; 7436; -.
DR   PRO; PR:P98155; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000147852; Expressed in 211 organ(s), highest expression level in female gonad.
DR   ExpressionAtlas; P98155; baseline and differential.
DR   Genevisible; P98155; HS.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0034185; F:apolipoprotein binding; IDA:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:BHF-UCL.
DR   GO; GO:0034437; F:glycoprotein transporter activity; IDA:BHF-UCL.
DR   GO; GO:0005041; F:low-density lipoprotein particle receptor activity; TAS:ProtInc.
DR   GO; GO:0038025; F:reelin receptor activity; ISS:BHF-UCL.
DR   GO; GO:0034189; F:very-low-density lipoprotein particle binding; IDA:BHF-UCL.
DR   GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IDA:BHF-UCL.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR   GO; GO:0034436; P:glycoprotein transport; IDA:BHF-UCL.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0032802; P:low-density lipoprotein particle receptor catabolic process; TAS:Reactome.
DR   GO; GO:0007613; P:memory; TAS:ProtInc.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:1900006; P:positive regulation of dendrite development; ISS:BHF-UCL.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IDA:BHF-UCL.
DR   GO; GO:0038026; P:reelin-mediated signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0021517; P:ventral spinal cord development; IEA:Ensembl.
DR   GO; GO:0034447; P:very-low-density lipoprotein particle clearance; IDA: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; 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; 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   3D-structure; Alternative splicing; Cholesterol metabolism;
KW   Coated pit; Complete proteome; Disulfide bond; EGF-like domain;
KW   Endocytosis; Glycoprotein; Isopeptide bond; Lipid metabolism;
KW   Lipid transport; Membrane; Mental retardation; Polymorphism; 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_0000017343.
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    395       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      396    435       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
FT   DISULFID    120    140
FT   DISULFID    134    149
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:0000269|PubMed:20427281}.
FT   VAR_SEQ     751    779       STATTVTYSETKDTNTTEISATSGLVPGG -> R (in
FT                                isoform Short). {ECO:0000305}.
FT                                /FTId=VSP_004304.
FT   VARIANT      59     59       V -> I (in dbSNP:rs6149).
FT                                {ECO:0000269|PubMed:10391209,
FT                                ECO:0000269|Ref.5}.
FT                                /FTId=VAR_011865.
FT   VARIANT     262    262       P -> H (in dbSNP:rs34761707).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_025063.
FT   VARIANT     379    379       E -> K (in dbSNP:rs6146).
FT                                {ECO:0000269|PubMed:10391209}.
FT                                /FTId=VAR_011866.
FT   VARIANT     464    464       L -> I (in dbSNP:rs34753566).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_025064.
FT   VARIANT     561    561       I -> V (in dbSNP:rs35724190).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_025065.
FT   VARIANT     613    613       R -> H (in dbSNP:rs35948251).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_025066.
FT   VARIANT     791    791       V -> I (in dbSNP:rs35334949).
FT                                {ECO:0000269|Ref.5}.
FT                                /FTId=VAR_025067.
FT   MUTAGEN     825    825       K->R: Insensitive to MYLIP-triggered
FT                                degradation; when associated with R-828
FT                                and R-839. {ECO:0000269|PubMed:20427281}.
FT   MUTAGEN     828    828       K->R: Insensitive to MYLIP-triggered
FT                                degradation; when associated with R-825
FT                                and R-839. {ECO:0000269|PubMed:20427281}.
FT   MUTAGEN     839    839       K->R: Insensitive to MYLIP-triggered
FT                                degradation. Insensitive to MYLIP-
FT                                triggered degradation; when associated
FT                                with R-825 and R-828.
FT                                {ECO:0000269|PubMed:20427281}.
FT   CONFLICT      9      9       L -> V (in Ref. 1; AAA53684).
FT                                {ECO:0000305}.
FT   CONFLICT     13     13       L -> V (in Ref. 4; AAA61344).
FT                                {ECO:0000305}.
FT   CONFLICT    424    424       G -> A (in Ref. 1; AAA53684).
FT                                {ECO:0000305}.
FT   CONFLICT    678    678       L -> H (in Ref. 1; AAA53684).
FT                                {ECO:0000305}.
FT   CONFLICT    766    766       T -> S (in Ref. 4; AAA61344).
FT                                {ECO:0000305}.
FT   HELIX        87     89       {ECO:0000244|PDB:6BYV}.
FT   STRAND       90     93       {ECO:0000244|PDB:6BYV}.
FT   HELIX       101    103       {ECO:0000244|PDB:6BYV}.
FT   TURN        105    107       {ECO:0000244|PDB:6BYV}.
FT   TURN        115    117       {ECO:0000244|PDB:3DPR}.
FT   STRAND      121    125       {ECO:0000244|PDB:3DPR}.
FT   STRAND      132    137       {ECO:0000244|PDB:3DPR}.
FT   TURN        141    145       {ECO:0000244|PDB:3DPR}.
FT   STRAND      158    160       {ECO:0000244|PDB:6BYV}.
FT   HELIX       169    171       {ECO:0000244|PDB:6BYV}.
FT   STRAND      174    176       {ECO:0000244|PDB:6BYV}.
FT   STRAND      179    182       {ECO:0000244|PDB:6BYV}.
FT   HELIX       183    185       {ECO:0000244|PDB:6BYV}.
SQ   SEQUENCE   873 AA;  96098 MW;  8BAC29438A78C2B8 CRC64;
     MGTSALWALW LLLALCWAPR ESGATGTGRK AKCEPSQFQC TNGRCITLLW KCDGDEDCVD
     GSDEKNCVKK TCAESDFVCN NGQCVPSRWK CDGDPDCEDG SDESPEQCHM RTCRIHEISC
     GAHSTQCIPV SWRCDGENDC DSGEDEENCG NITCSPDEFT CSSGRCISRN FVCNGQDDCS
     DGSDELDCAP PTCGAHEFQC STSSCIPISW VCDDDADCSD QSDESLEQCG RQPVIHTKCP
     ASEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI
     RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDISKVCNQ EQDCRDWSDE PLKECHINEC
     LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE
     CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA
     QKLFWADLSQ KAIFSASIDD KVGRHVKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA
     TLDGTKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTADIQ
     WPNGITLDLI KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI
     DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP SGKNWCEEDM ENGGCEYLCL
     PAPQINDHSP KYTCSCPSGY NVEENGRDCQ STATTVTYSE TKDTNTTEIS ATSGLVPGGI
     NVTTAVSEVS VPPKGTSAAW AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT
     TEEDLSIDIG RHSASVGHTY PAISVVSTDD DLA
//
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