LRP8_HUMAN
ID LRP8_HUMAN Reviewed; 963 AA.
AC Q14114; B1AMT6; B1AMT7; B1AMT8; O14968; Q86V27; Q99876; Q9BR78;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 4.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Low-density lipoprotein receptor-related protein 8;
DE Short=LRP-8;
DE AltName: Full=Apolipoprotein E receptor 2;
DE Flags: Precursor;
GN Name=LRP8; Synonyms=APOER2;
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] (ISOFORM 1), AND VARIANTS ARG-25 AND GLU-46.
RC TISSUE=Placenta;
RX PubMed=8626535; DOI=10.1074/jbc.271.14.8373;
RA Kim D.-H., Iijima H., Goto K., Sakai J., Ishii H., Kim H.-J., Suzuki H.,
RA Kondo H., Saeki S., Yamamoto T.;
RT "Human apolipoprotein E receptor 2. A novel lipoprotein receptor of the low
RT density lipoprotein receptor family predominantly expressed in brain.";
RL J. Biol. Chem. 271:8373-8380(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 4), AND VARIANTS ARG-25
RP AND GLU-46.
RC TISSUE=Peripheral blood;
RX PubMed=9079678; DOI=10.1074/jbc.272.13.8498;
RA Kim D.-H., Magoori K., Inoue T.R., Mao C.C., Kim H.-J., Suzuki H.,
RA Fujita T., Endo Y., Saeki S., Yamamoto T.T.;
RT "Exon/intron organization, chromosome localization, alternative splicing,
RT and transcription units of the human apolipoprotein E receptor 2 gene.";
RL J. Biol. Chem. 272:8498-8504(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS ARG-25 AND GLU-46.
RC TISSUE=Umbilical vein;
RX PubMed=11152697; DOI=10.1074/jbc.m011795200;
RA Korschineck I., Ziegler S., Breuss J., Lang I., Lorenz M., Kaun C.,
RA Ambros P.F., Binder B.R.;
RT "Identification of a novel exon in apolipoprotein E receptor 2 leading to
RT alternatively spliced mRNAs found in cells of the vascular wall but not in
RT neuronal tissue.";
RL J. Biol. Chem. 276:13192-13197(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 720-963 (ISOFORM 1), AND VARIANTS ARG-25 AND GLU-46.
RC TISSUE=Eye, and Lung;
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 [6]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=10218790; DOI=10.1016/s0306-4522(98)00489-8;
RA Clatworthy A.E., Stockinger W., Christie R.H., Schneider W.J., Nimpf J.,
RA Hyman B.T., Rebeck G.W.;
RT "Expression and alternate splicing of apolipoprotein E receptor 2 in
RT brain.";
RL Neuroscience 90:903-911(1999).
RN [7]
RP PHOSPHORYLATION AT TYROSINE RESIDUES.
RX PubMed=12681505; DOI=10.1016/s0014-5793(03)00261-8;
RA Sacre S.M., Stannard A.K., Owen J.S.;
RT "Apolipoprotein E (apoE) isoforms differentially induce nitric oxide
RT production in endothelial cells.";
RL FEBS Lett. 540:181-187(2003).
RN [8]
RP CHARACTERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=10508213;
RA Riddell D.R., Vinogradov D.V., Stannard A.K., Chadwick N., Owen J.S.;
RT "Identification and characterization of LRP8 (apoER2) in human blood
RT platelets.";
RL J. Lipid Res. 40:1925-1930(1999).
RN [9]
RP FUNCTION AS A RECEPTOR FOR REELIN.
RX PubMed=12899622; DOI=10.1021/bi034475p;
RA Andersen O.M., Benhayon D., Curran T., Willnow T.E.;
RT "Differential binding of ligands to the apolipoprotein E receptor 2.";
RL Biochemistry 42:9355-9364(2003).
RN [10]
RP FUNCTION AS A RECEPTOR FOR APOE.
RX PubMed=12950167; DOI=10.1021/bi027093c;
RA Li X., Kypreos K., Zanni E.E., Zannis V.;
RT "Domains of apoE required for binding to apoE receptor 2 and to
RT phospholipids: implications for the functions of apoE in the brain.";
RL Biochemistry 42:10406-10417(2003).
RN [11]
RP FUNCTION AS A RECEPTOR FOR BETA 2-GLYCOPROTEIN I.
RX PubMed=12807892; DOI=10.1074/jbc.m212655200;
RA Lutters B.C., Derksen R.H., Tekelenburg W.L., Lenting P.J., Arnout J.,
RA de Groot P.G.;
RT "Dimers of beta 2-glycoprotein I increase platelet deposition to collagen
RT via interaction with phospholipids and the apolipoprotein E receptor 2'.";
RL J. Biol. Chem. 278:33831-33838(2003).
RN [12]
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 [13]
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., 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 [14]
RP 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 VLDLR.
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] {ECO:0007744|PDB:3A7Q}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 42-83 IN COMPLEX WITH REELIN/RELN
RP AND CALCIUM, FUNCTION, AND DISULFIDE BOND.
RX PubMed=20223215; DOI=10.1016/j.str.2010.01.010;
RA Yasui N., Nogi T., Takagi J.;
RT "Structural basis for specific recognition of reelin by its receptors.";
RL Structure 18:320-331(2010).
RN [18]
RP VARIANTS GLU-46 AND GLN-952.
RX PubMed=12399018; DOI=10.1016/s0304-3940(02)00942-4;
RA Ma S.L., Ng H.K., Baum L., Pang J.C., Chiu H.F., Woo J., Tang N.L.,
RA Lam L.C.;
RT "Low-density lipoprotein receptor-related protein 8 (apolipoprotein E
RT receptor 2) gene polymorphisms in Alzheimer's disease.";
RL Neurosci. Lett. 332:216-218(2002).
RN [19]
RP VARIANT GLN-952, CHARACTERIZATION OF VARIANT GLN-952, AND ASSOCIATION WITH
RP SUSCEPTIBILITY TO MYOCARDIAL INFARCTION TYPE 1.
RX PubMed=17847002; DOI=10.1086/521581;
RA Shen G.-Q., Li L., Girelli D., Seidelmann S.B., Rao S., Fan C., Park J.E.,
RA Xi Q., Li J., Hu Y., Olivieri O., Marchant K., Barnard J., Corrocher R.,
RA Elston R., Cassano J., Henderson S., Hazen S.L., Plow E.F., Topol E.J.,
RA Wang Q.K.;
RT "An LRP8 variant is associated with familial and premature coronary artery
RT disease and myocardial infarction.";
RL Am. J. Hum. Genet. 81:780-791(2007).
CC -!- FUNCTION: Cell surface receptor for Reelin (RELN) and apolipoprotein E
CC (apoE)-containing ligands (PubMed:20223215). LRP8 participates in
CC transmitting the extracellular Reelin signal to intracellular signaling
CC processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via
CC both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine
CC phosphorylation and microtubule function in neurons. LRP8 has higher
CC affinity for Reelin than VLDLR. LRP8 is thus a key component of the
CC Reelin pathway which governs neuronal layering of the forebrain during
CC embryonic brain development. Binds the endoplasmic reticulum resident
CC receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein
CC I and may be involved in the suppression of platelet aggregation in the
CC vasculature. Highly expressed in the initial segment of the epididymis,
CC where it affects the functional expression of clusterin and
CC phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins
CC required for sperm maturation. May also function as an endocytic
CC receptor. Not required for endocytic uptake of SEPP1 in the kidney
CC which is mediated by LRP2 (By similarity). Together with its ligand,
CC apolipoprotein E (apoE), may indirectly play a role in the suppression
CC of the innate immune response by controlling the survival of myeloid-
CC derived suppressor cells (By similarity).
CC {ECO:0000250|UniProtKB:Q924X6, ECO:0000269|PubMed:12807892,
CC ECO:0000269|PubMed:12899622, ECO:0000269|PubMed:12950167,
CC ECO:0000269|PubMed:20223215, ECO:0000269|PubMed:30873003}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Semliki Forest
CC virus. {ECO:0000269|PubMed:34929721}.
CC -!- SUBUNIT: Homooligomer (PubMed:30873003). Interacts with VLDLR
CC (PubMed:30873003). Reelin associates with two or more receptor
CC molecules (PubMed:20223215). Interacts with DAB1 and JNK-interacting
CC proteins. Interacts with SNX17 (By similarity). Interacts with PCSK9.
CC Interacts with MDK; this interaction is calcium dependent (By
CC similarity). Interacts with CLU (PubMed:24381170). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q924X6, ECO:0000269|PubMed:18039658,
CC ECO:0000269|PubMed:20223215, ECO:0000269|PubMed:24381170,
CC ECO:0000269|PubMed:30873003}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Semliki Forest virus E2-
CC E1 heterodimer; this interaction mediates viral entry to host cell.
CC {ECO:0000269|PubMed:34929721}.
CC -!- INTERACTION:
CC Q14114; P25054: APC; NbExp=2; IntAct=EBI-2681187, EBI-727707;
CC Q14114; P02649: APOE; NbExp=2; IntAct=EBI-2681187, EBI-1222467;
CC Q14114; Q60841: Reln; Xeno; NbExp=10; IntAct=EBI-2681187, EBI-9248666;
CC Q14114-3; Q06481-5: APLP2; NbExp=3; IntAct=EBI-25832196, EBI-25646567;
CC Q14114-3; P02649: APOE; NbExp=3; IntAct=EBI-25832196, EBI-1222467;
CC Q14114-3; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-25832196, EBI-713677;
CC Q14114-3; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-25832196, EBI-9087876;
CC Q14114-3; P35222: CTNNB1; NbExp=3; IntAct=EBI-25832196, EBI-491549;
CC Q14114-3; Q9UJY5-5: GGA1; NbExp=3; IntAct=EBI-25832196, EBI-25903400;
CC Q14114-3; Q92993-2: KAT5; NbExp=3; IntAct=EBI-25832196, EBI-20795332;
CC Q14114-3; Q99683: MAP3K5; NbExp=3; IntAct=EBI-25832196, EBI-476263;
CC Q14114-3; Q96P71-2: NECAB3; NbExp=3; IntAct=EBI-25832196, EBI-15098952;
CC Q14114-3; I6L9F6: NEFL; NbExp=3; IntAct=EBI-25832196, EBI-10178578;
CC Q14114-3; P10599: TXN; NbExp=3; IntAct=EBI-25832196, EBI-594644;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30873003};
CC Single-pass type I membrane protein {ECO:0000250}. Secreted
CC {ECO:0000250}. Note=Isoforms that contain the exon coding for a furin-
CC type cleavage site are proteolytically processed, leading to a secreted
CC receptor fragment. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist. No differences were
CC observed in the pattern splicing between control and Alzheimer
CC brains.;
CC Name=1; Synonyms=ApoER2 922;
CC IsoId=Q14114-1; Sequence=Displayed;
CC Name=2; Synonyms=ApoER2 906;
CC IsoId=Q14114-2; Sequence=VSP_010305, VSP_010307, VSP_010308;
CC Name=3;
CC IsoId=Q14114-3; Sequence=VSP_010308;
CC Name=4; Synonyms=ApoER2delta4-7;
CC IsoId=Q14114-4; Sequence=VSP_038181, VSP_010306;
CC Name=5;
CC IsoId=Q14114-5; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed mainly in brain and placenta. Also
CC expressed in platelets and megakaryocytic cells. Not expressed in the
CC liver. {ECO:0000269|PubMed:10218790, ECO:0000269|PubMed:10508213}.
CC -!- DOMAIN: The cytoplasmic domain is involved in the binding of DAB1 and
CC in the recruitment of JNK-interacting proteins. Isoforms, which lack
CC part of the cytoplasmic domain, are unable to recruit members of the
CC family of JNK interacting proteins (JIP) to the cytoplasmic tail (By
CC similarity). {ECO:0000250}.
CC -!- PTM: O-glycosylated. Some alternatively spliced isoforms lack the O-
CC linked sugar domain (By similarity). {ECO:0000250}.
CC -!- PTM: Undergoes sequential, furin and gamma-secretase dependent,
CC proteolytic processing, resulting in the extracellular release of the
CC entire ligand-binding domain as a soluble polypeptide and in the
CC intracellular domain (ICD) release into the cytoplasm. The gamma-
CC secretase-dependent proteolytical processing occurs after the bulk of
CC the extracellular domain has been shed, in a furin-dependent manner, in
CC alternatively spliced isoforms carrying the furin cleavage site.
CC Hypoglycosylation (mainly hypo-O-glycosylation) leads to increased
CC extracellular cleavage, which in turn results in accelerating release
CC of the intracellular domain (ICD) by the gamma-secretase. The resulting
CC receptor fragment is able to inhibit Reelin signaling and in particular
CC the Reelin-induced DAB1 phosphorylation (By similarity). {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated upon apoE binding.
CC {ECO:0000269|PubMed:12681505}.
CC -!- PTM: Ubiquitinated by MYLIP leading to degradation.
CC {ECO:0000269|PubMed:20427281}.
CC -!- DISEASE: Myocardial infarction 1 (MCI1) [MIM:608446]: A condition
CC defined by the irreversible necrosis of heart muscle secondary to
CC prolonged ischemia. {ECO:0000269|PubMed:17847002}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Natural isoforms of apoE (E2, E3, E4) have similar
CC affinities for LRP8.
CC -!- MISCELLANEOUS: [Isoform 5]: Contains an insert in the extracellular
CC part which carries a furin cleavage site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA99509.1; Type=Frameshift; Evidence={ECO:0000305};
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; D50678; BAA09328.1; -; mRNA.
DR EMBL; D86407; BAA21824.1; -; Genomic_DNA.
DR EMBL; D86407; BAA21825.1; -; Genomic_DNA.
DR EMBL; Z75190; CAA99509.1; ALT_FRAME; mRNA.
DR EMBL; AL355483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006443; AAH06443.1; -; mRNA.
DR EMBL; BC051836; AAH51836.2; -; mRNA.
DR CCDS; CCDS30720.1; -. [Q14114-3]
DR CCDS; CCDS578.1; -. [Q14114-1]
DR CCDS; CCDS579.1; -. [Q14114-2]
DR CCDS; CCDS580.1; -. [Q14114-4]
DR RefSeq; NP_001018064.1; NM_001018054.2. [Q14114-3]
DR RefSeq; NP_004622.2; NM_004631.4. [Q14114-1]
DR RefSeq; NP_059992.3; NM_017522.4. [Q14114-2]
DR RefSeq; NP_150643.2; NM_033300.3. [Q14114-4]
DR PDB; 3A7Q; X-ray; 2.60 A; B=42-83.
DR PDB; 5B4X; X-ray; 3.20 A; B/D=42-736.
DR PDB; 5B4Y; X-ray; 1.90 A; B=42-124.
DR PDBsum; 3A7Q; -.
DR PDBsum; 5B4X; -.
DR PDBsum; 5B4Y; -.
DR AlphaFoldDB; Q14114; -.
DR SMR; Q14114; -.
DR BioGRID; 113579; 79.
DR DIP; DIP-48670N; -.
DR ELM; Q14114; -.
DR IntAct; Q14114; 35.
DR STRING; 9606.ENSP00000303634; -.
DR GlyGen; Q14114; 7 sites.
DR iPTMnet; Q14114; -.
DR PhosphoSitePlus; Q14114; -.
DR SwissPalm; Q14114; -.
DR BioMuta; LRP8; -.
DR DMDM; 259016389; -.
DR EPD; Q14114; -.
DR jPOST; Q14114; -.
DR MassIVE; Q14114; -.
DR MaxQB; Q14114; -.
DR PaxDb; Q14114; -.
DR PeptideAtlas; Q14114; -.
DR PRIDE; Q14114; -.
DR ProteomicsDB; 59819; -. [Q14114-1]
DR ProteomicsDB; 59820; -. [Q14114-2]
DR ProteomicsDB; 59821; -. [Q14114-3]
DR ProteomicsDB; 59822; -. [Q14114-4]
DR Antibodypedia; 33078; 410 antibodies from 33 providers.
DR DNASU; 7804; -.
DR Ensembl; ENST00000306052.12; ENSP00000303634.6; ENSG00000157193.18. [Q14114-1]
DR Ensembl; ENST00000347547.7; ENSP00000334522.2; ENSG00000157193.18. [Q14114-4]
DR Ensembl; ENST00000354412.7; ENSP00000346391.3; ENSG00000157193.18. [Q14114-2]
DR Ensembl; ENST00000371454.6; ENSP00000360509.2; ENSG00000157193.18. [Q14114-3]
DR GeneID; 7804; -.
DR KEGG; hsa:7804; -.
DR MANE-Select; ENST00000306052.12; ENSP00000303634.6; NM_004631.5; NP_004622.2.
DR UCSC; uc001cvi.4; human. [Q14114-1]
DR CTD; 7804; -.
DR DisGeNET; 7804; -.
DR GeneCards; LRP8; -.
DR HGNC; HGNC:6700; LRP8.
DR HPA; ENSG00000157193; Tissue enhanced (testis, thyroid gland).
DR MalaCards; LRP8; -.
DR MIM; 602600; gene.
DR MIM; 608446; phenotype.
DR neXtProt; NX_Q14114; -.
DR OpenTargets; ENSG00000157193; -.
DR PharmGKB; PA30457; -.
DR VEuPathDB; HostDB:ENSG00000157193; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000154819; -.
DR HOGENOM; CLU_008163_4_0_1; -.
DR InParanoid; Q14114; -.
DR OMA; PRKFQCK; -.
DR OrthoDB; 359795at2759; -.
DR PhylomeDB; Q14114; -.
DR TreeFam; TF351700; -.
DR PathwayCommons; Q14114; -.
DR Reactome; R-HSA-432142; Platelet sensitization by LDL.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; Q14114; -.
DR SIGNOR; Q14114; -.
DR BioGRID-ORCS; 7804; 34 hits in 1076 CRISPR screens.
DR EvolutionaryTrace; Q14114; -.
DR GeneWiki; Low_density_lipoprotein_receptor-related_protein_8; -.
DR GenomeRNAi; 7804; -.
DR Pharos; Q14114; Tbio.
DR PRO; PR:Q14114; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q14114; protein.
DR Bgee; ENSG00000157193; Expressed in ganglionic eminence and 177 other tissues.
DR ExpressionAtlas; Q14114; baseline and differential.
DR Genevisible; Q14114; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005901; C:caveola; IDA:BHF-UCL.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IC:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0034185; F:apolipoprotein binding; IC:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0038024; F:cargo receptor activity; NAS:ARUK-UCL.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; TAS:ARUK-UCL.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0038025; F:reelin receptor activity; ISS:BHF-UCL.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; IDA:BHF-UCL.
DR GO; GO:0021541; P:ammon gyrus development; ISS:BHF-UCL.
DR GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; NAS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:BHF-UCL.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISS:BHF-UCL.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISS:BHF-UCL.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:BHF-UCL.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; ISS:BHF-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0021517; P:ventral spinal cord development; IBA:GO_Central.
DR CDD; cd00112; LDLa; 6.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 4.10.400.10; -; 7.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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 Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 5.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57424; SSF57424; 7.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 7.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS51120; LDLRB; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Disulfide bond;
KW EGF-like domain; Endocytosis; Glycoprotein; Host-virus interaction;
KW Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..963
FT /note="Low-density lipoprotein receptor-related protein 8"
FT /id="PRO_0000017332"
FT TOPO_DOM 42..826
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 848..963
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..82
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 85..123
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 126..164
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 166..202
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 205..246
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 258..295
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 298..334
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 336..375
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 376..415
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 462..508
FT /note="LDL-receptor class B 1"
FT REPEAT 509..551
FT /note="LDL-receptor class B 2"
FT REPEAT 552..595
FT /note="LDL-receptor class B 3"
FT REPEAT 596..639
FT /note="LDL-receptor class B 4"
FT REPEAT 640..681
FT /note="LDL-receptor class B 5"
FT REGION 740..798
FT /note="Clustered O-linked oligosaccharides"
FT REGION 754..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20223215,
FT ECO:0007744|PDB:3A7Q"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20223215,
FT ECO:0007744|PDB:3A7Q"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20223215,
FT ECO:0007744|PDB:3A7Q"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20223215,
FT ECO:0007744|PDB:3A7Q"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20223215,
FT ECO:0007744|PDB:3A7Q"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20223215,
FT ECO:0007744|PDB:3A7Q"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..59
FT /evidence="ECO:0000269|PubMed:20223215,
FT ECO:0007744|PDB:3A7Q"
FT DISULFID 54..72
FT /evidence="ECO:0000269|PubMed:20223215,
FT ECO:0007744|PDB:3A7Q"
FT DISULFID 66..81
FT /evidence="ECO:0000269|PubMed:20223215,
FT ECO:0007744|PDB:3A7Q"
FT DISULFID 86..98
FT /evidence="ECO:0000250"
FT DISULFID 93..111
FT /evidence="ECO:0000250"
FT DISULFID 105..122
FT /evidence="ECO:0000250"
FT DISULFID 127..141
FT /evidence="ECO:0000250"
FT DISULFID 134..154
FT /evidence="ECO:0000250"
FT DISULFID 148..163
FT /evidence="ECO:0000250"
FT DISULFID 167..179
FT /evidence="ECO:0000250"
FT DISULFID 174..192
FT /evidence="ECO:0000250"
FT DISULFID 186..201
FT /evidence="ECO:0000250"
FT DISULFID 206..221
FT /evidence="ECO:0000250"
FT DISULFID 213..234
FT /evidence="ECO:0000250"
FT DISULFID 228..245
FT /evidence="ECO:0000250"
FT DISULFID 259..272
FT /evidence="ECO:0000250"
FT DISULFID 267..285
FT /evidence="ECO:0000250"
FT DISULFID 279..294
FT /evidence="ECO:0000250"
FT DISULFID 299..311
FT /evidence="ECO:0000250"
FT DISULFID 306..324
FT /evidence="ECO:0000250"
FT DISULFID 318..333
FT /evidence="ECO:0000250"
FT DISULFID 340..351
FT /evidence="ECO:0000250"
FT DISULFID 347..360
FT /evidence="ECO:0000250"
FT DISULFID 362..374
FT /evidence="ECO:0000250"
FT DISULFID 380..390
FT /evidence="ECO:0000250"
FT DISULFID 386..399
FT /evidence="ECO:0000250"
FT DISULFID 401..414
FT /evidence="ECO:0000250"
FT VAR_SEQ 166..295
FT /note="LCAPHEFQCGNRSCLAAVFVCDGDDDCGDGSDERGCADPACGPREFRCGGDG
FT GGACIPERWVCDRQFDCEDRSDEAAELCGRPGPGATSAPAACATASQFACRSGECVHLG
FT WRCDGDRDCKDKSDEADCP -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11152697"
FT /id="VSP_010305"
FT VAR_SEQ 166
FT /note="L -> W (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038181"
FT VAR_SEQ 167..336
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_010306"
FT VAR_SEQ 737..812
FT /note="APQSTSTTTLASTMTRTVPATTRAPGTTVHRSTYQNHSTETPSLTAAVPSSV
FT SVPRAPSISPSTLSPATSNHSQHY -> D (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11152697"
FT /id="VSP_010307"
FT VAR_SEQ 893..951
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11152697,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010308"
FT VARIANT 25
FT /note="Q -> R (in dbSNP:rs4926972)"
FT /evidence="ECO:0000269|PubMed:11152697,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8626535,
FT ECO:0000269|PubMed:9079678"
FT /id="VAR_046974"
FT VARIANT 46
FT /note="D -> E (in dbSNP:rs3820198)"
FT /evidence="ECO:0000269|PubMed:11152697,
FT ECO:0000269|PubMed:12399018, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8626535, ECO:0000269|PubMed:9079678"
FT /id="VAR_018468"
FT VARIANT 453
FT /note="V -> M (in dbSNP:rs5180)"
FT /id="VAR_037624"
FT VARIANT 466
FT /note="W -> C (in dbSNP:rs5181)"
FT /id="VAR_037625"
FT VARIANT 607
FT /note="Q -> R (in dbSNP:rs5172)"
FT /id="VAR_037626"
FT VARIANT 611
FT /note="I -> L (in dbSNP:rs5170)"
FT /id="VAR_037627"
FT VARIANT 653
FT /note="S -> T (in dbSNP:rs5171)"
FT /id="VAR_037628"
FT VARIANT 736
FT /note="R -> Q (in dbSNP:rs5172)"
FT /id="VAR_059079"
FT VARIANT 952
FT /note="R -> Q (associated with susceptibility to myocardial
FT infarction type 1; increases activation of MAPK14 by
FT oxidized low density lipoprotein; dbSNP:rs5174)"
FT /evidence="ECO:0000269|PubMed:12399018,
FT ECO:0000269|PubMed:17847002"
FT /id="VAR_018469"
FT CONFLICT 262
FT /note="A -> V (in Ref. 1; BAA09328 and 2; BAA21824)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="Y -> C (in Ref. 3; CAA99509)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="A -> G (in Ref. 1; BAA09328 and 2; BAA21824/
FT BAA21825)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="H -> Y (in Ref. 1; BAA09328, 2; BAA21824/BAA21825
FT and 3; CAA99509)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="Q -> R (in Ref. 3; CAA99509)"
FT /evidence="ECO:0000305"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5B4Y"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5B4Y"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5B4Y"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5B4Y"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:5B4Y"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:5B4Y"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:5B4Y"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5B4Y"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5B4Y"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5B4Y"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:5B4Y"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:5B4X"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:5B4X"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 385..393
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 429..439
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 442..458
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 459..462
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 469..472
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 473..478
FT /evidence="ECO:0007829|PDB:5B4X"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:5B4X"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 506..509
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 516..519
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 530..535
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 540..548
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 549..552
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 553..558
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 564..569
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 586..592
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 593..596
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 597..602
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 603..606
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 625..627
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 629..637
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 640..645
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 646..649
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 650..655
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 663..666
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 675..678
FT /evidence="ECO:0007829|PDB:5B4X"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:5B4X"
FT TURN 689..691
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 692..695
FT /evidence="ECO:0007829|PDB:5B4X"
FT HELIX 696..699
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 701..706
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 710..714
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 716..720
FT /evidence="ECO:0007829|PDB:5B4X"
FT STRAND 731..735
FT /evidence="ECO:0007829|PDB:5B4X"
SQ SEQUENCE 963 AA; 105634 MW; B10DCF72F62DE71C CRC64;
MGLPEPGPLR LLALLLLLLL LLLLQLQHLA AAAADPLLGG QGPAKDCEKD QFQCRNERCI
PSVWRCDEDD DCLDHSDEDD CPKKTCADSD FTCDNGHCIH ERWKCDGEEE CPDGSDESEA
TCTKQVCPAE KLSCGPTSHK CVPASWRCDG EKDCEGGADE AGCATLCAPH EFQCGNRSCL
AAVFVCDGDD DCGDGSDERG CADPACGPRE FRCGGDGGGA CIPERWVCDR QFDCEDRSDE
AAELCGRPGP GATSAPAACA TASQFACRSG ECVHLGWRCD GDRDCKDKSD EADCPLGTCR
GDEFQCGDGT CVLAIKHCNQ EQDCPDGSDE AGCLQGLNEC LHNNGGCSHI CTDLKIGFEC
TCPAGFQLLD QKTCGDIDEC KDPDACSQIC VNYKGYFKCE CYPGYEMDLL TKNCKAAAGK
SPSLIFTNRH EVRRIDLVKR NYSRLIPMLK NVVALDVEVA TNRIYWCDLS YRKIYSAYMD
KASDPKEQEV LIDEQLHSPE GLAVDWVHKH IYWTDSGNKT ISVATVDGGR RRTLFSRNLS
EPRAIAVDPL RGFMYWSDWG DQAKIEKSGL NGVDRQTLVS DNIEWPNGIT LDLLSQRLYW
VDSKLHQLSS IDFSGGNRKT LISSTDFLSH PFGIAVFEDK VFWTDLENEA IFSANRLNGL
EISILAENLN NPHDIVIFHE LKQPRAPDAC ELSVQPNGGC EYLCLPAPQI SSHSPKYTCA
CPDTMWLGPD MKRCYRAPQS TSTTTLASTM TRTVPATTRA PGTTVHRSTY QNHSTETPSL
TAAVPSSVSV PRAPSISPST LSPATSNHSQ HYANEDSKMG STVTAAVIGI IVPIVVIALL
CMSGYLIWRN WKRKNTKSMN FDNPVYRKTT EEEDEDELHI GRTAQIGHVY PAAISSFDRP
LWAEPCLGET REPEDPAPAL KELFVLPGEP RSQLHQLPKN PLSELPVVKS KRVALSLEDD
GLP
