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 02-SEP-2026, entry version 234. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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., 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 low RT density lipoprotein (VLDL) receptor' mRNA."; RL Hum. Mol. Genet. 3:531-537(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=8294473; DOI=10.1016/s0021-9258(17)42151-x; 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 deduced RT amino acid sequence and localization of its gene (VLDLR) to chromosome band RT 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; ILE-464; RP 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., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., 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., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., 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., Rogers J., RA 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP INTERACTION WITH HRV VP1 (MICROBIAL INFECTION). 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 PAFAH1B3 AND PAFAH1B2. RX PubMed=17330141; DOI=10.1371/journal.pone.0000252; RA Zhang G., Assadi A.H., McNeil R.S., Beffert U., Wynshaw-Boris A., Herz J., RA Clark G.D., D'Arcangelo G.; RT "The Pafah1b complex interacts with the reelin receptor VLDLR."; RL PLoS ONE 2:e252-e252(2007). RN [11] 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 density RT lipoprotein receptor (LDLR) and its closest family members VLDLR and RT ApoER2."; RL J. Biol. Chem. 283:2363-2372(2008). RN [12] 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., Nimpf J., RA van Berkel T.J., Tontonoz P., Zelcer N.; RT "The E3 ubiquitin ligase IDOL induces the degradation of the low density RT lipoprotein receptor family members VLDLR and ApoER2."; RL J. Biol. Chem. 285:19720-19726(2010). RN [13] RP INTERACTION WITH STX5, SUBCELLULAR LOCATION, AND GLYCOSYLATION. RX PubMed=23701949; DOI=10.1016/j.yexcr.2013.05.010; RA Wagner T., Dieckmann M., Jaeger S., Weggen S., Pietrzik C.U.; RT "Stx5 is a novel interactor of VLDL-R to affect its intracellular RT trafficking and processing."; RL Exp. Cell Res. 319:1956-1972(2013). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLU. RX PubMed=24381170; DOI=10.1074/jbc.m113.529271; RA Leeb C., Eresheim C., Nimpf J.; RT "Clusterin is a ligand for apolipoprotein E receptor 2 (ApoER2) and very RT low density lipoprotein receptor (VLDLR) and signals via the Reelin- RT signaling pathway."; RL J. Biol. Chem. 289:4161-4172(2014). RN [15] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH RELN AND RP LRP8/APOER2. RX PubMed=30873003; DOI=10.3389/fnmol.2019.00053; RA Dlugosz P., Tresky R., Nimpf J.; RT "Differential Action of Reelin on Oligomerization of ApoER2 and VLDL RT Receptor in HEK293 Cells Assessed by Time-Resolved Anisotropy and RT Fluorescence Lifetime Imaging Microscopy."; RL Front. Mol. Neurosci. 12:53-53(2019). RN [16] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SEMLIKI FOREST VIRUS E2-E1 RP HETERODIMER (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=34929721; DOI=10.1038/s41586-021-04326-0; RA Clark L.E., Clark S.A., Lin C., Liu J., Coscia A., Nabel K.G., Yang P., RA Neel D.V., Lee H., Brusic V., Stryapunina I., Plante K.S., Ahmed A.A., RA Catteruccia F., Young-Pearse T.L., Chiu I.M., Llopis P.M., Weaver S.C., RA Abraham J.; RT "VLDLR and ApoER2 are receptors for multiple alphaviruses."; RL Nature 602:475-480(2022). RN [17] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH YELLOW FEVER VIRUS RP ENVELOPE PROTEIN E (MICROBIAL INFECTION). RX PubMed=41162706; DOI=10.1038/s41586-025-09689-2; RA Chong Z., Hui S., Qiu X., Palakurty S., Sariol A., Kaszuba T., Nguyen M.N., RA Li P., Raju S., Hall P.D., Nelson C.A., Baltazar-Perez I., Price D.A., RA Rothlauf P.W., Crowe J.E., Whelan S.P.J., Leung D.W., Amarasinghe G.K., RA Bailey A.L., Fremont D.H., Diamond M.S.; RT "Multiple LDLR family members act as entry receptors for yellow fever RT virus."; RL Nature 0:0-0(2025). RN [18] 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 of RT its cellular receptor protein."; RL Nat. Struct. Mol. Biol. 11:429-434(2004). RN [19] {ECO:0007744|PDB:8IHP} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 111-149 IN COMPLEX RP WITH SEMLIKI FOREST VIRUS VLP, INTERACTION WITH SEMLIKI FOREST VIRUS SPIKE RP GLYCOPROTEIN E1 (MICROBIAL INFECTION), AND MUTAGENESIS OF GLU-117; PRO-129; RP TRP-132; ASP-135; GLU-137 AND ASP-139. RX PubMed=37098345; DOI=10.1016/j.cell.2023.03.032; RA Cao D., Ma B., Cao Z., Zhang X., Xiang Y.; RT "Structure of Semliki Forest virus in complex with its receptor VLDLR."; RL Cell 186:2208-2218.e15(2023). RN [20] {ECO:0007744|PDB:8UFB} RP STRUCTURE BY ELECTRON MICROSCOPY (2.86 ANGSTROMS) OF 28-7972 IN COMPLEX RP WITH EQUINE ENCEPHALITIS VIRUS SPIKE GLYCOPROTEIN E2, AND INTERACTION WITH RP EASTERN EQUINE ENCEPHALITIS VIRUS SPIKE GLYCOPROTEIN E2 (MICROBIAL RP INFECTION). RX PubMed=38176410; DOI=10.1016/j.cell.2023.11.031; RA Adams L.J., Raju S., Ma H., Gilliland T., Reed D.S., Klimstra W.B., RA Fremont D.H., Diamond M.S.; RT "Structural and functional basis of VLDLR usage by Eastern equine RT encephalitis virus."; RL Cell 187:360-374.e19(2024). RN [21] {ECO:0007744|PDB:8UA8} RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) OF 72-108 IN COMPLEX WITH RP SEMLIKI FOREST VIRUS VLP, INTERACTION WITH SEMLIKI FOREST VIRUS SPIKE RP GLYCOPROTEIN E1 (MICROBIAL INFECTION), INTERACTION WITH EASTERN EQUINE RP ENCEPHALITIS VIRUS SPIKE GLYCOPROTEIN E2 (MICROBIAL INFECTION), AND RP MUTAGENESIS OF TRP-89; ASP-92; ASP-94 AND ASP-96. RX PubMed=39095394; DOI=10.1038/s41467-024-50887-9; RA Yang P., Li W., Fan X., Pan J., Mann C.J., Varnum H., Clark L.E., RA Clark S.A., Coscia A., Basu H., Smith K.N., Brusic V., Abraham J.; RT "Structural basis for VLDLR recognition by eastern equine encephalitis RT virus."; RL Nat. Commun. 15:6548-6548(2024). RN [22] 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 of RT human genes."; RL Nat. Genet. 22:231-238(1999). RN [23] RP ERRATUM OF PUBMED:10391209. 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 [24] 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: Multifunctional cell surface receptor that binds VLDL and CC transports it into cells by endocytosis and therefore plays an CC important role in energy metabolism. Also binds to a wide range of CC other molecules including Reelin/RELN or apolipoprotein E/APOE- CC containing ligands as well as clusterin/CLU (PubMed:24381170, CC PubMed:30873003). In the off-state of the pathway, forms homooligomers CC or heterooligomers with LRP8 (PubMed:30873003). Upon binding to CC ligands, homooligomers are rearranged to higher order receptor clusters CC that transmit the extracellular RELN signal to intracellular signaling CC processes by binding to DAB1 (PubMed:30873003). This interaction CC results in phosphorylation of DAB1 leading to the ultimate cell CC responses required for the correct positioning of newly generated CC neurons. Later, mediates a stop signal for migrating neurons, CC preventing them from entering the marginal zone (By similarity). CC {ECO:0000250|UniProtKB:P98156, ECO:0000269|PubMed:24381170, CC ECO:0000269|PubMed:30873003}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Semliki Forest CC virus. {ECO:0000269|PubMed:34929721}. CC -!- FUNCTION: (Microbial infection) Functions as a receptor for yellow CC fever virus. {ECO:0000269|PubMed:41162706}. CC -!- SUBUNIT: Homooligomer (PubMed:30873003). Binds to the extracellular CC matrix protein Reelin/RELN (PubMed:30873003). Interacts with LRP8 CC (PubMed:30873003). Interacts with LDLRAP1 (By similarity). Interacts CC with SNX17 (By similarity). Interacts with DAB1. Interacts with PCSK9. CC Interacts with PAFAH1B3 and PAFAH1B2, the catalytic complex of (PAF-AH CC (I)) heterotetrameric enzyme; these interactions may modulate the CC Reelin pathway (PubMed:17330141). Interacts with STX5; this interaction CC mediates VLDLR translocation from the endoplasmic reticulum to the CC plasma membrane (PubMed:23701949). Interacts with CLU CC (PubMed:24381170). {ECO:0000250|UniProtKB:P98156, CC ECO:0000269|PubMed:15064754, ECO:0000269|PubMed:17330141, CC ECO:0000269|PubMed:18039658, ECO:0000269|PubMed:23701949, CC ECO:0000269|PubMed:30873003}. CC -!- SUBUNIT: (Microbial infection) Interacts with protein VP1 of the minor- CC group human rhinoviruses (HRVs) through the second and third LDL- CC receptor class A domains. {ECO:0000269|PubMed:12857919}. CC -!- SUBUNIT: (Microbial infection) Interacts (via class A repeats) with CC Semliki Forest virus spike glycoprotein E1 (via DIII); this interaction CC mediates viral entry into host cell. {ECO:0000269|PubMed:37098345, CC ECO:0000305|PubMed:34929721}. CC -!- SUBUNIT: (Microbial infection) Interacts (via class A repeats) with CC Eastern equine encephalitis virus spike glycoprotein E2 (via E2-A); CC this interaction mediates viral entry into host cell. CC {ECO:0000269|PubMed:38176410, ECO:0000269|PubMed:39095394}. CC -!- SUBUNIT: (Microbial infection) Interacts with yellow fever virus CC envelope protein E; this interaction facilitates virus entry. CC {ECO:0000269|PubMed:41162706}. CC -!- INTERACTION: CC P98155; P30533: LRPAP1; NbExp=6; IntAct=EBI-9004309, EBI-715927; CC P98155; Q99068: Lrpap1; Xeno; NbExp=2; IntAct=EBI-9004309, EBI-919734; CC P98155; Q60841: Reln; Xeno; NbExp=7; IntAct=EBI-9004309, EBI-9248666; CC P98155-2; O43309: ZSCAN12; NbExp=3; IntAct=EBI-12047495, EBI-1210440; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23701949, CC ECO:0000269|PubMed:34929721}; Single-pass type I membrane protein. CC Membrane, clathrin-coated pit; Single-pass type I 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 ovary CC and kidney; not in liver. CC -!- PTM: Ubiquitinated at Lys-839 by MYLIP leading to degradation. CC {ECO:0000269|PubMed:20427281}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:23701949}. CC -!- DISEASE: Cerebellar ataxia, impaired intellectual development, and CC dysequilibrium syndrome 1 (CAMRQ1) [MIM:224050]: An autosomal CC recessive, congenital, non-progressive cerebellar ataxia associated CC with disturbed equilibrium, delayed ambulation, intellectual CC disability, cerebellar hypoplasia and mild cerebral gyral CC simplification. Additional features include short stature, strabismus, CC pes planus and, rarely, seizures. {ECO:0000269|PubMed:16080122}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. 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; -; 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_001018056.3. [P98155-2] DR RefSeq; NP_003374.3; NM_003383.5. [P98155-1] 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 PDB; 8IHP; EM; 3.00 A; M/N/O=111-149. DR PDB; 8UA4; EM; 3.58 A; R=33-68. DR PDB; 8UA8; EM; 3.70 A; R=72-108. DR PDB; 8UFB; EM; 3.89 A; R/S/T/U/V/W/X/Y=28-797. DR PDB; 8UFC; EM; 3.09 A; V/W/X/Y=31-108. DR PDB; 8X0K; EM; 3.50 A; D/H/L/P=113-149. DR PDB; 8X0L; EM; 3.50 A; D/H/L=113-149. DR PDB; 8X0M; EM; 3.50 A; D/H=113-149. DR PDB; 8XI4; EM; 3.40 A; M/N/O/P=31-113. DR PDB; 8XI5; EM; 3.40 A; M/N/O/P=191-231, Q/R/S/T=111-151. DR PDB; 8YS2; EM; 5.20 A; M/N/O/P=31-110. DR PDB; 8YS4; EM; 4.80 A; M/N/O/P=191-231, Q/R/S/T=111-151. DR PDB; 8YVZ; EM; 3.45 A; E/R/S/T=110-151. DR PDB; 8YW0; EM; 3.55 A; E/R/T=191-230. DR PDB; 8YW1; EM; 3.44 A; C=111-231. DR PDB; 8YW2; EM; 3.70 A; A=70-231. DR PDB; 9DQZ; EM; 2.90 A; M/N/O/P=33-110. DR PDB; 9E9Y; EM; 3.96 A; V/X/Y/Z=31-108. DR PDB; 9E9Z; EM; 3.95 A; V/W/X/Y=31-108. DR PDB; 9EAU; EM; 3.06 A; Y/Z=111-149. DR PDB; 9L99; EM; 3.60 A; N=31-110. DR PDB; 9L9A; EM; 3.90 A; M=70-151. DR PDB; 9UIO; EM; 3.03 A; R/S/T=32-110. DR PDB; 9WSL; EM; 3.27 A; R/S/T=32-110. DR AlphaFoldDB; P98155; -. DR EMDB; EMD-35451; -. DR EMDB; EMD-37980; -. DR EMDB; EMD-37981; -. DR EMDB; EMD-37982; -. DR EMDB; EMD-38370; -. DR EMDB; EMD-38371; -. DR EMDB; EMD-39617; -. DR EMDB; EMD-39618; -. DR EMDB; EMD-39619; -. DR EMDB; EMD-39620; -. DR EMDB; EMD-42050; -. DR EMDB; EMD-42054; -. DR EMDB; EMD-42190; -. DR EMDB; EMD-42192; -. DR EMDB; EMD-47119; -. DR EMDB; EMD-47821; -. DR EMDB; EMD-47822; -. DR EMDB; EMD-47846; -. DR EMDB; EMD-62898; -. DR EMDB; EMD-62899; -. DR EMDB; EMD-64199; -. DR EMDB; EMD-66198; -. DR SMR; P98155; -. DR BioGRID; 113277; 42. DR DIP; DIP-40925N; -. DR FunCoup; P98155; 265. DR IntAct; P98155; 20. DR NDEx; IQUERY-CP-VLDLR; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000371532; -. DR DrugBank; DB14003; alpha-Tocopherol acetate. DR DrugBank; DB06755; Beta carotene. DR DrugBank; DB06772; Cabazitaxel. DR DrugBank; DB03017; Lauric acid. DR DrugBank; DB11251; Tocopherol. DR DrugBank; DB09270; Ubidecarenone. DR GlyCosmos; P98155; 6 sites, 1 glycan. DR GlyGen; P98155; 7 sites, 2 N-linked glycans (2 sites), 2 O-linked glycans (4 sites). DR iPTMnet; P98155; -. DR PhosphoSitePlus; P98155; -. DR BioMuta; VLDLR; -. DR DMDM; 1730111; -. DR jPOST; P98155; -. DR MassIVE; P98155; -. DR PaxDb; 9606-ENSP00000371532; -. DR PeptideAtlas; P98155; -. DR ProteomicsDB; 57794; -. [P98155-1] DR ProteomicsDB; 57795; -. [P98155-2] DR Pumba; P98155; -. DR Antibodypedia; 9217; 494 antibodies from 38 providers. DR DNASU; 7436; -. DR Ensembl; ENST00000382100.8; ENSP00000371532.2; ENSG00000147852.18. [P98155-1] DR Ensembl; ENST00000681306.1; ENSP00000506072.1; ENSG00000147852.18. [P98155-2] DR GeneID; 7436; -. DR KEGG; hsa:7436; -. DR MANE-Select; ENST00000382100.8; ENSP00000371532.2; NM_003383.5; NP_003374.3. DR UCSC; uc003zhk.2; human. [P98155-1] DR AGR; HGNC:12698; -. DR ClinPGx; PA37317; -. DR CTD; 7436; -. DR DisGeNET; 7436; -. DR GeneCards; VLDLR; -. DR GeneReviews; VLDLR; -. DR HGNC; HGNC:12698; VLDLR. DR HPA; ENSG00000147852; Tissue enhanced (ovary). DR MalaCards; VLDLR; -. DR MIM; 192977; gene. DR MIM; 224050; phenotype. DR OpenTargets; ENSG00000147852; -. DR Orphanet; 1766; Dysequilibrium syndrome. DR VEuPathDB; HostDB:ENSG00000147852; -. DR eggNOG; KOG1215; Eukaryota. DR GeneTree; ENSGT00940000155460; -. DR HOGENOM; CLU_008163_2_0_1; -. DR InParanoid; P98155; -. DR OMA; ADKRNCQ; -. DR OrthoDB; 5958943at2759; -. DR PAN-GO; P98155; 2 GO annotations based on evolutionary models. DR PhylomeDB; P98155; -. DR PathwayCommons; P98155; -. 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 SignaLink; P98155; -. DR SIGNOR; P98155; -. DR Agora; ENSG00000147852; -. DR BioGRID-ORCS; 7436; 10 hits in 1147 CRISPR screens. DR ChiTaRS; VLDLR; human. DR EvolutionaryTrace; P98155; -. DR GeneWiki; VLDL_receptor; -. DR GenomeRNAi; 7436; -. DR Pharos; P98155; Tbio. DR PRO; PR:P98155; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P98155; protein. DR Bgee; ENSG00000147852; Expressed in heart right ventricle and 189 other cell types or tissues. DR ExpressionAtlas; P98155; baseline and differential. DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0043235; C:signaling receptor complex; IDA:MGI. 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:0038024; F:cargo receptor 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:0001618; F:virus receptor activity; IMP:UniProtKB. DR GO; GO:0034436; P:glycoprotein transport; IDA:BHF-UCL. DR GO; GO:0007613; P:memory; TAS:ProtInc. 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: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:0034447; P:very-low-density lipoprotein particle clearance; IDA:BHF-UCL. DR CDD; cd00054; EGF_CA; 1. DR CDD; cd00112; LDLa; 8. DR FunFam; 2.10.25.10:FF:000009; Low-density lipoprotein receptor isoform 1; 1. DR FunFam; 2.10.25.10:FF:000052; low-density lipoprotein receptor isoform X1; 1. DR FunFam; 2.120.10.30:FF:000002; low-density lipoprotein receptor isoform X1; 1. DR FunFam; 4.10.400.10:FF:000025; Very low density lipoprotein receptor; 1. DR FunFam; 4.10.400.10:FF:000038; Very low density lipoprotein receptor; 1. DR FunFam; 4.10.400.10:FF:000043; Very low density lipoprotein receptor; 1. DR FunFam; 4.10.400.10:FF:000046; Very low density lipoprotein receptor; 1. DR FunFam; 4.10.400.10:FF:000049; Very low density lipoprotein receptor; 1. DR FunFam; 4.10.400.10:FF:000051; Very low density lipoprotein receptor; 1. DR FunFam; 4.10.400.10:FF:000053; Very low density lipoprotein receptor; 1. DR FunFam; 4.10.400.10:FF:000057; Very low density lipoprotein receptor; 1. DR Gene3D; 2.10.25.10; Laminin; 3. DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8. DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR000742; EGF. DR InterPro; IPR001881; EGF-like_Ca-bd_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; IPR051221; LDLR-related. DR InterPro; IPR023415; LDLR_class-A_CS. DR InterPro; IPR000033; LDLR_classB_rpt. DR InterPro; IPR002172; LDrepeatLR_classA_rpt. DR InterPro; IPR049883; NOTCH1_EGF-like. DR PANTHER; PTHR22722:SF15; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1. DR PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1. DR Pfam; PF07645; EGF_CA; 1. DR Pfam; PF14670; FXa_inhibition; 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; SSF57196; EGF/Laminin; 3. DR SUPFAM; SSF57424; LDL receptor-like module; 8. DR SUPFAM; SSF63825; YWTD domain; 1. 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. DR PDBsum; 1V9U; -. DR PDBsum; 3DPR; -. DR PDBsum; 6BYV; -. DR PDBsum; 8IHP; -. DR PDBsum; 8UA4; -. DR PDBsum; 8UA8; -. DR PDBsum; 8UFB; -. DR PDBsum; 8UFC; -. DR PDBsum; 8X0K; -. DR PDBsum; 8X0L; -. DR PDBsum; 8X0M; -. DR PDBsum; 8XI4; -. DR PDBsum; 8XI5; -. DR PDBsum; 8YS2; -. DR PDBsum; 8YS4; -. DR PDBsum; 8YVZ; -. DR PDBsum; 8YW0; -. DR PDBsum; 8YW1; -. DR PDBsum; 8YW2; -. DR PDBsum; 9DQZ; -. DR PDBsum; 9E9Y; -. DR PDBsum; 9E9Z; -. DR PDBsum; 9EAU; -. DR PDBsum; 9L99; -. DR PDBsum; 9L9A; -. DR PDBsum; 9UIO; -. DR PDBsum; 9WSL; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cholesterol metabolism; KW Coated pit; Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; KW Host-virus interaction; Intellectual disability; Isopeptide bond; KW Lipid metabolism; Lipid transport; Membrane; Proteomics identification; KW Receptor; Reference proteome; Repeat; Signal; Steroid metabolism; KW Sterol metabolism; Transmembrane; Transmembrane helix; Transport; KW Ubl conjugation; VLDL. FT SIGNAL 1..27 FT /evidence="ECO:0000255" FT CHAIN 28..873 FT /note="Very low-density lipoprotein receptor" FT /id="PRO_0000017343" FT TOPO_DOM 28..797 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 798..819 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 820..873 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 31..69 FT /note="LDL-receptor class A 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 70..110 FT /note="LDL-receptor class A 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 111..151 FT /note="LDL-receptor class A 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 152..190 FT /note="LDL-receptor class A 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 191..231 FT /note="LDL-receptor class A 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 237..275 FT /note="LDL-receptor class A 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 276..314 FT /note="LDL-receptor class A 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 316..355 FT /note="LDL-receptor class A 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124" FT DOMAIN 356..395 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 396..435 FT /note="EGF-like 2; calcium-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REPEAT 439..480 FT /note="LDL-receptor class B 1" FT REPEAT 481..524 FT /note="LDL-receptor class B 2" FT REPEAT 525..567 FT /note="LDL-receptor class B 3" FT REPEAT 568..611 FT /note="LDL-receptor class B 4" FT REPEAT 612..654 FT /note="LDL-receptor class B 5" FT REPEAT 655..697 FT /note="LDL-receptor class B 6" FT DOMAIN 702..750 FT /note="EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT REGION 117..139 FT /note="(Microbial infection) Interaction with Semliki virus FT spike glycoprotein E1" FT /evidence="ECO:0000269|PubMed:37098345" FT REGION 751..790 FT /note="Clustered O-linked oligosaccharides" FT MOTIF 832..837 FT /note="Endocytosis signal" FT /evidence="ECO:0000255" FT CARBOHYD 151 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 765 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 781 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 33..45 FT /evidence="ECO:0000250" FT DISULFID 40..58 FT /evidence="ECO:0000250" FT DISULFID 52..67 FT /evidence="ECO:0000250" FT DISULFID 72..84 FT /evidence="ECO:0000250" FT DISULFID 79..97 FT /evidence="ECO:0000250" FT DISULFID 91..108 FT /evidence="ECO:0000250" FT DISULFID 113..127 FT DISULFID 120..140 FT DISULFID 134..149 FT DISULFID 154..166 FT /evidence="ECO:0000250" FT DISULFID 161..179 FT /evidence="ECO:0000250" FT DISULFID 173..188 FT /evidence="ECO:0000250" FT DISULFID 193..205 FT /evidence="ECO:0000250" FT DISULFID 200..218 FT /evidence="ECO:0000250" FT DISULFID 212..229 FT /evidence="ECO:0000250" FT DISULFID 239..251 FT /evidence="ECO:0000250" FT DISULFID 246..264 FT /evidence="ECO:0000250" FT DISULFID 258..273 FT /evidence="ECO:0000250" FT DISULFID 278..290 FT /evidence="ECO:0000250" FT DISULFID 285..303 FT /evidence="ECO:0000250" FT DISULFID 297..312 FT /evidence="ECO:0000250" FT DISULFID 318..331 FT /evidence="ECO:0000250" FT DISULFID 326..344 FT /evidence="ECO:0000250" FT DISULFID 338..355 FT /evidence="ECO:0000250" FT DISULFID 360..371 FT /evidence="ECO:0000250" FT DISULFID 367..380 FT /evidence="ECO:0000250" FT DISULFID 382..394 FT /evidence="ECO:0000250" FT DISULFID 400..410 FT /evidence="ECO:0000250" FT DISULFID 406..419 FT /evidence="ECO:0000250" FT DISULFID 421..434 FT /evidence="ECO:0000250" FT DISULFID 706..719 FT /evidence="ECO:0000250" FT DISULFID 715..734 FT /evidence="ECO:0000250" FT DISULFID 736..749 FT /evidence="ECO:0000250" FT CROSSLNK 839 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:20427281" FT VAR_SEQ 751..779 FT /note="STATTVTYSETKDTNTTEISATSGLVPGG -> R (in isoform FT Short)" FT /evidence="ECO:0000305" FT /id="VSP_004304" FT VARIANT 59 FT /note="V -> I (in dbSNP:rs6149)" FT /evidence="ECO:0000269|PubMed:10391209, ECO:0000269|Ref.5" FT /id="VAR_011865" FT VARIANT 262 FT /note="P -> H (in dbSNP:rs34761707)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_025063" FT VARIANT 379 FT /note="E -> K (in dbSNP:rs6146)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_011866" FT VARIANT 464 FT /note="L -> I (in dbSNP:rs34753566)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_025064" FT VARIANT 561 FT /note="I -> V (in dbSNP:rs35724190)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_025065" FT VARIANT 613 FT /note="R -> H (in dbSNP:rs35948251)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_025066" FT VARIANT 791 FT /note="V -> I (in dbSNP:rs35334949)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_025067" FT MUTAGEN 89 FT /note="W->F,R: Complete loss of entry of Semliki virus into FT the cell." FT /evidence="ECO:0000269|PubMed:39095394" FT MUTAGEN 92 FT /note="D->A: Complete loss of entry of Semliki virus into FT the cell." FT /evidence="ECO:0000269|PubMed:39095394" FT MUTAGEN 94 FT /note="D->I: Complete loss of entry of Semliki virus into FT the cell." FT /evidence="ECO:0000269|PubMed:39095394" FT MUTAGEN 96 FT /note="D->A: Complete loss of entry of Semliki virus into FT the cell." FT /evidence="ECO:0000269|PubMed:39095394" FT MUTAGEN 117 FT /note="E->A: Complete loss of interaction with Semliki FT virus spike glycoprotein E1." FT /evidence="ECO:0000269|PubMed:37098345" FT MUTAGEN 129 FT /note="P->A,H: Complete loss of interaction with Semliki FT virus spike glycoprotein E1." FT /evidence="ECO:0000269|PubMed:37098345" FT MUTAGEN 132 FT /note="W->A: Complete loss of interaction with Semliki FT virus spike glycoprotein E1." FT /evidence="ECO:0000269|PubMed:37098345" FT MUTAGEN 135 FT /note="D->A: Complete loss of interaction with Semliki FT virus spike glycoprotein E1." FT /evidence="ECO:0000269|PubMed:37098345" FT MUTAGEN 137 FT /note="E->A: Complete loss of interaction with Semliki FT virus spike glycoprotein E1." FT /evidence="ECO:0000269|PubMed:37098345" FT MUTAGEN 139 FT /note="D->A: Complete loss of interaction with Semliki FT virus spike glycoprotein E1." FT /evidence="ECO:0000269|PubMed:37098345" FT MUTAGEN 825 FT /note="K->R: Insensitive to MYLIP-triggered degradation; FT when associated with R-828 and R-839." FT /evidence="ECO:0000269|PubMed:20427281" FT MUTAGEN 828 FT /note="K->R: Insensitive to MYLIP-triggered degradation; FT when associated with R-825 and R-839." FT /evidence="ECO:0000269|PubMed:20427281" FT MUTAGEN 839 FT /note="K->R: Insensitive to MYLIP-triggered degradation. FT Insensitive to MYLIP-triggered degradation; when associated FT with R-825 and R-828." FT /evidence="ECO:0000269|PubMed:20427281" FT CONFLICT 9 FT /note="L -> V (in Ref. 1; AAA53684)" FT /evidence="ECO:0000305" FT CONFLICT 13 FT /note="L -> V (in Ref. 4; AAA61344)" FT /evidence="ECO:0000305" FT CONFLICT 424 FT /note="G -> A (in Ref. 1; AAA53684)" FT /evidence="ECO:0000305" FT CONFLICT 678 FT /note="L -> H (in Ref. 1; AAA53684)" FT /evidence="ECO:0000305" FT CONFLICT 766 FT /note="T -> S (in Ref. 4; AAA61344)" FT /evidence="ECO:0000305" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:9DQZ" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:9DQZ" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:9DQZ" FT STRAND 51..55 FT /evidence="ECO:0007829|PDB:9DQZ" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:8XI4" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:8XI4" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:9DQZ" FT HELIX 69..71 FT /evidence="ECO:0007829|PDB:8UFC" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:9DQZ" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:9DQZ" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:9DQZ" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:9DQZ" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:9DQZ" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:9DQZ" FT TURN 105..107 FT /evidence="ECO:0007829|PDB:9DQZ" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:8YW1" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:8IHP" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:8IHP" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:8IHP" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:8IHP" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:8IHP" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:8IHP" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:8IHP" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:8YW1" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:8YW1" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:8YW1" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:8YW1" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:8YW1" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:8YW1" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:8XI5" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:8XI5" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:8XI5" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:8XI5" FT STRAND 211..214 FT /evidence="ECO:0007829|PDB:8XI5" FT STRAND 218..220 FT /evidence="ECO:0007829|PDB:8XI5" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:8XI5" FT TURN 226..229 FT /evidence="ECO:0007829|PDB:8XI5" 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 //