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 11-NOV-2015, entry version 165. 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=4; IntAct=EBI-9004309, EBI-715927; CC Q99068:Lrpap1 (xeno); NbExp=2; IntAct=EBI-9004309, EBI-919734; CC Q60841:Reln (xeno); NbExp=4; 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 -!- SIMILARITY: Contains 3 EGF-like domains. {ECO:0000255|PROSITE- CC ProRule:PRU00076}. CC -!- SIMILARITY: Contains 8 LDL-receptor class A domains. CC {ECO:0000255|PROSITE-ProRule:PRU00124}. CC -!- SIMILARITY: Contains 6 LDL-receptor class B repeats. CC {ECO:0000255|PROSITE-ProRule:PRU00461}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/vldlr/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; CAH72454.1; -; 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_001018056.1. [P98155-2] DR RefSeq; NP_003374.3; NM_003383.3. [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 PDBsum; 1V9U; -. DR PDBsum; 3DPR; -. DR ProteinModelPortal; P98155; -. DR SMR; P98155; 33-753. DR BioGrid; 113277; 11. DR DIP; DIP-40925N; -. DR IntAct; P98155; 3. DR MINT; MINT-111579; -. DR STRING; 9606.ENSP00000371532; -. DR PhosphoSite; P98155; -. DR BioMuta; VLDLR; -. DR DMDM; 1730111; -. DR MaxQB; P98155; -. DR PaxDb; P98155; -. DR PRIDE; P98155; -. DR Ensembl; ENST00000382099; ENSP00000371531; ENSG00000147852. [P98155-2] DR Ensembl; ENST00000382100; ENSP00000371532; ENSG00000147852. [P98155-1] DR GeneID; 7436; -. DR KEGG; hsa:7436; -. DR UCSC; uc003zhk.1; human. [P98155-1] DR CTD; 7436; -. DR GeneCards; VLDLR; -. DR GeneReviews; VLDLR; -. DR HGNC; HGNC:12698; VLDLR. DR HPA; CAB032462; -. DR HPA; HPA051312; -. DR MIM; 192977; gene. DR MIM; 224050; phenotype. DR neXtProt; NX_P98155; -. DR Orphanet; 1766; Dysequilibrium syndrome. DR PharmGKB; PA37317; -. DR eggNOG; ENOG410IPT5; Eukaryota. DR eggNOG; ENOG410YQ6J; LUCA. DR GeneTree; ENSGT00760000118968; -. DR HOGENOM; HOG000115656; -. DR HOVERGEN; HBG006250; -. DR InParanoid; P98155; -. DR OMA; DEHTANC; -. DR OrthoDB; EOG7NGQ9P; -. DR PhylomeDB; P98155; -. DR TreeFam; TF351700; -. DR EvolutionaryTrace; P98155; -. DR GeneWiki; VLDL_receptor; -. DR GenomeRNAi; 7436; -. DR NextBio; 29124; -. DR PRO; PR:P98155; -. DR Proteomes; UP000005640; Chromosome 9. DR Bgee; P98155; -. DR CleanEx; HS_VLDLR; -. DR ExpressionAtlas; P98155; baseline and differential. DR Genevisible; P98155; HS. DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. 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:0001948; F:glycoprotein binding; IPI:BHF-UCL. DR GO; GO:0034437; F:glycoprotein transporter activity; IDA:BHF-UCL. DR GO; GO:0005041; F:low-density lipoprotein 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:0042149; P:cellular response to glucose starvation; IEA:Ensembl. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl. DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl. 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:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR GO; GO:0007613; P:memory; TAS:ProtInc. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; 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:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl. 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 Gene3D; 2.120.10.30; -; 1. DR Gene3D; 4.10.400.10; -; 8. 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; IPR023415; LDLR_class-A_CS. DR InterPro; IPR000033; LDLR_classB_rpt. DR InterPro; IPR002172; LDrepeatLR_classA_rpt. 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; 1. 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...). {ECO:0000255}. FT CARBOHYD 765 765 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 781 781 N-linked (GlcNAc...). {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 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}. 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 //