LRP1_RAT
ID LRP1_RAT Reviewed; 4545 AA.
AC G3V928; Q5I0H1;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Prolow-density lipoprotein receptor-related protein 1 {ECO:0000305};
DE Short=LRP-1;
DE Contains:
DE RecName: Full=Low-density lipoprotein receptor-related protein 1 85 kDa subunit {ECO:0000250|UniProtKB:Q07954};
DE Short=LRP-85 {ECO:0000250|UniProtKB:Q07954};
DE Contains:
DE RecName: Full=Low-density lipoprotein receptor-related protein 1 515 kDa subunit {ECO:0000250|UniProtKB:Q07954};
DE Short=LRP-515 {ECO:0000250|UniProtKB:Q07954};
DE Contains:
DE RecName: Full=Low-density lipoprotein receptor-related protein 1 intracellular domain {ECO:0000250|UniProtKB:Q07954};
DE Short=LRPICD {ECO:0000250|UniProtKB:Q07954};
DE Flags: Precursor;
GN Name=Lrp1 {ECO:0000312|RGD:1307535};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|EMBL:EDM16460.1};
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4274-4545.
RC TISSUE=Spleen {ECO:0000312|EMBL:AAH88327.1};
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=31522887; DOI=10.1016/j.cell.2019.08.025;
RA Fu M.M., McAlear T.S., Nguyen H., Oses-Prieto J.A., Valenzuela A.,
RA Shi R.D., Perrino J.J., Huang T.T., Burlingame A.L., Bechstedt S.,
RA Barres B.A.;
RT "The Golgi outpost protein TPPP nucleates microtubules and is critical for
RT myelination.";
RL Cell 0:0-0(2019).
CC -!- FUNCTION: Endocytic receptor involved in endocytosis and in
CC phagocytosis of apoptotic cells (By similarity). Required for early
CC embryonic development (By similarity). Involved in cellular lipid
CC homeostasis. Involved in the plasma clearance of chylomicron remnants
CC and activated LRPAP1 (alpha 2-macroglobulin), as well as the local
CC metabolism of complexes between plasminogen activators and their
CC endogenous inhibitors. Acts as an LRPAP1 alpha-2-macroglobulin
CC receptor. Acts as TAU/MAPT receptor and controls the endocytosis of
CC TAU/MAPT as well as its subsequent spread. May modulate cellular
CC events, such as APP metabolism, kinase-dependent intracellular
CC signaling, neuronal calcium signaling as well as neurotransmission (By
CC similarity). {ECO:0000250|UniProtKB:Q07954,
CC ECO:0000250|UniProtKB:Q91ZX7}.
CC -!- SUBUNIT: Heterodimer of an 85-kDa membrane-bound carboxyl subunit and a
CC non-covalently attached 515-kDa N-terminal subunit. Intracellular
CC domain interacts with MAFB (By similarity). Found in a complex with
CC PID1/PCLI1, LRP1 and CUBNI. Interacts with SNX17, PID1/PCLI1, PDGF and
CC CUBN. The intracellular domain interacts with SHC1, GULP1 and DAB1. Can
CC weakly interact (via NPXY motif) with DAB2 (via PID domain); the
CC interaction is enhanced by tyrosine phosphorylation of the NPXY motif.
CC Interacts with MDK; promotes neuronal survival. Interacts with LRPAP1;
CC this interaction is followed by rapid internalization. Interacts with
CC uPA/PLAU and PAI1/SERPINE1, either individually or in complex with each
CC other, leading to rapid endocytosis; this interaction is abolished in
CC the presence of LRPAP1/RAP. Also interacts with tPA/PLAT alone or in
CC complex with SERPINE1. Interacts with the urokinase receptor PLAUR;
CC this interaction leads to PLAUR internalization and is impaired in the
CC presence of SORL1. Interacts with PDGFB. Interacts with TAU/MAPT,
CC leading to endocytosis; this interaction is reduced in the presence of
CC LRPAP1/RAP (By similarity). {ECO:0000250|UniProtKB:Q07954,
CC ECO:0000250|UniProtKB:Q91ZX7}.
CC -!- SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein
CC 1 85 kDa subunit]: Cell membrane {ECO:0000250|UniProtKB:Q07954};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q07954}.
CC Membrane, coated pit {ECO:0000250|UniProtKB:Q07954}.
CC -!- SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein
CC 1 515 kDa subunit]: Cell membrane {ECO:0000250|UniProtKB:Q07954};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q07954};
CC Extracellular side {ECO:0000250|UniProtKB:Q07954}. Membrane, coated pit
CC {ECO:0000250|UniProtKB:Q07954}.
CC -!- SUBCELLULAR LOCATION: Golgi outpost {ECO:0000269|PubMed:31522887}.
CC Cytoplasm, cytoskeleton, microtubule organizing center
CC {ECO:0000269|PubMed:31522887}. Note=Localizes to the postsynaptic Golgi
CC apparatus region, also named Golgi outpost, which shapes dendrite
CC morphology by functioning as sites of acentrosomal microtubule
CC nucleation. {ECO:0000269|PubMed:31522887}.
CC -!- SUBCELLULAR LOCATION: [Low-density lipoprotein receptor-related protein
CC 1 intracellular domain]: Cytoplasm {ECO:0000250|UniProtKB:Q07954}.
CC Nucleus {ECO:0000250|UniProtKB:Q07954}. Note=After cleavage, the
CC intracellular domain (LRPICD) is detected both in the cytoplasm and in
CC the nucleus. {ECO:0000250|UniProtKB:Q07954}.
CC -!- PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515
CC kDa large extracellular domain (LRP-515) that remains non-covalently
CC associated. Gamma-secretase-dependent cleavage of LRP-85 releases the
CC intracellular domain from the membrane. {ECO:0000250|UniProtKB:Q07954}.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000250|UniProtKB:Q07954}.
CC -!- PTM: Phosphorylated on tyrosine residues upon stimulation with PDGF.
CC Tyrosine phosphorylation promotes interaction with SHC1.
CC {ECO:0000250|UniProtKB:Q07954}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR EMBL; AABR07057430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07057431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473950; EDM16460.1; -; Genomic_DNA.
DR EMBL; BC088327; AAH88327.1; -; mRNA.
DR RefSeq; NP_001123962.1; NM_001130490.1.
DR SMR; G3V928; -.
DR ComplexPortal; CPX-4462; Prolow-density lipoprotein receptor-related protein 1 complex.
DR IntAct; G3V928; 3.
DR STRING; 10116.ENSRNOP00000034210; -.
DR GlyGen; G3V928; 49 sites, 14 N-linked glycans (11 sites).
DR iPTMnet; G3V928; -.
DR PhosphoSitePlus; G3V928; -.
DR jPOST; G3V928; -.
DR PaxDb; G3V928; -.
DR PRIDE; G3V928; -.
DR Ensembl; ENSRNOT00000031005; ENSRNOP00000034210; ENSRNOG00000025053.
DR GeneID; 299858; -.
DR KEGG; rno:299858; -.
DR CTD; 4035; -.
DR RGD; 1307535; Lrp1.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000157899; -.
DR HOGENOM; CLU_000085_1_0_1; -.
DR InParanoid; G3V928; -.
DR OMA; CEYDGTR; -.
DR OrthoDB; 1606at2759; -.
DR TreeFam; TF315253; -.
DR Reactome; R-RNO-2168880; Scavenging of heme from plasma.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:G3V928; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000025053; Expressed in liver and 19 other tissues.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0044295; C:axonal growth cone; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0032593; C:insulin-responsive compartment; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0062136; C:low-density lipoprotein receptor complex; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0016964; F:alpha-2 macroglobulin receptor activity; ISO:RGD.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0038024; F:cargo receptor activity; ISO:RGD.
DR GO; GO:0032050; F:clathrin heavy chain binding; ISO:RGD.
DR GO; GO:0015026; F:coreceptor activity; IDA:RGD.
DR GO; GO:0002020; F:protease binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0097242; P:amyloid-beta clearance; ISO:RGD.
DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; ISO:RGD.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; ISO:RGD.
DR GO; GO:0035909; P:aorta morphogenesis; ISO:RGD.
DR GO; GO:0043277; P:apoptotic cell clearance; ISO:RGD.
DR GO; GO:0002265; P:astrocyte activation involved in immune response; ISO:RGD.
DR GO; GO:0003279; P:cardiac septum development; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; IMP:RGD.
DR GO; GO:0044242; P:cellular lipid catabolic process; IMP:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0061642; P:chemoattraction of axon; IMP:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR GO; GO:0007167; P:enzyme-linked receptor protein signaling pathway; ISO:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEP:RGD.
DR GO; GO:0007041; P:lysosomal transport; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IMP:RGD.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IC:BHF-UCL.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; ISO:RGD.
DR GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; ISO:RGD.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; ISO:RGD.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:RGD.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:RGD.
DR GO; GO:0006909; P:phagocytosis; ISO:RGD.
DR GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISO:RGD.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
DR GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IDA:RGD.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IMP:RGD.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:RGD.
DR GO; GO:1904109; P:positive regulation of cholesterol import; IMP:RGD.
DR GO; GO:0032376; P:positive regulation of cholesterol transport; ISO:RGD.
DR GO; GO:0048694; P:positive regulation of collateral sprouting of injured axon; IDA:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
DR GO; GO:0032370; P:positive regulation of lipid transport; ISO:RGD.
DR GO; GO:1905167; P:positive regulation of lysosomal protein catabolic process; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0051222; P:positive regulation of protein transport; IMP:RGD.
DR GO; GO:1900149; P:positive regulation of Schwann cell migration; IMP:RGD.
DR GO; GO:1904300; P:positive regulation of transcytosis; ISO:RGD.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IMP:RGD.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0031623; P:receptor internalization; ISO:RGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:BHF-UCL.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0032374; P:regulation of cholesterol transport; ISO:RGD.
DR GO; GO:0032429; P:regulation of phospholipase A2 activity; ISO:RGD.
DR GO; GO:1905109; P:regulation of pulmonary blood vessel remodeling; ISO:RGD.
DR GO; GO:0150104; P:transport across blood-brain barrier; ISO:RGD.
DR CDD; cd00112; LDLa; 31.
DR Gene3D; 2.120.10.30; -; 8.
DR Gene3D; 4.10.400.10; -; 30.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR032485; DUF5050.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF16472; DUF5050; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 29.
DR Pfam; PF00058; Ldl_recept_b; 12.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 26.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM00192; LDLa; 31.
DR SMART; SM00135; LY; 35.
DR SUPFAM; SSF57184; SSF57184; 3.
DR SUPFAM; SSF57424; SSF57424; 30.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS01209; LDLRA_1; 15.
DR PROSITE; PS50068; LDLRA_2; 31.
DR PROSITE; PS51120; LDLRB; 34.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Cell membrane; Coated pit; Cytoplasm; Cytoskeleton;
KW Developmental protein; Disulfide bond; EGF-like domain; Endocytosis;
KW Glycoprotein; Golgi apparatus; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..4545
FT /note="Prolow-density lipoprotein receptor-related protein
FT 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5015091774"
FT CHAIN 20..?3944
FT /note="Low-density lipoprotein receptor-related protein 1
FT 515 kDa subunit"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT /id="PRO_0000448596"
FT CHAIN 3945..4545
FT /note="Low-density lipoprotein receptor-related protein 1
FT 85 kDa subunit"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT /id="PRO_0000448597"
FT CHAIN 4442..4545
FT /note="Low-density lipoprotein receptor-related protein 1
FT intracellular domain"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT /id="PRO_0000448598"
FT TOPO_DOM 20..4424
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 4425..4445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4446..4545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 27..66
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 72..110
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REPEAT 293..335
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 336..379
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 380..423
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 572..614
FT /note="LDL-receptor class B 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 615..660
FT /note="LDL-receptor class B 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 639..671
FT /note="HAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 661..711
FT /note="LDL-receptor class B 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 712..755
FT /note="LDL-receptor class B 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 854..892
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 895..933
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 936..973
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 976..1013
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1015..1053
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1062..1099
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1104..1142
FT /note="LDL-receptor class A 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1145..1184
FT /note="LDL-receptor class A 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REPEAT 1310..1356
FT /note="LDL-receptor class B 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1357..1399
FT /note="LDL-receptor class B 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1380..1413
FT /note="HAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 1400..1446
FT /note="LDL-receptor class B 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1447..1491
FT /note="LDL-receptor class B 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1470..1503
FT /note="HAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 1492..1532
FT /note="LDL-receptor class B 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1628..1670
FT /note="LDL-receptor class B 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1653..1684
FT /note="HAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 1671..1714
FT /note="LDL-receptor class B 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1715..1754
FT /note="LDL-receptor class B 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1755..1799
FT /note="LDL-receptor class B 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1935..1977
FT /note="LDL-receptor class B 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1978..2020
FT /note="LDL-receptor class B 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2021..2064
FT /note="LDL-receptor class B 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2065..2108
FT /note="LDL-receptor class B 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2254..2295
FT /note="LDL-receptor class B 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2277..2309
FT /note="HAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 2296..2344
FT /note="LDL-receptor class B 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2325..2358
FT /note="HAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 2345..2389
FT /note="LDL-receptor class B 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2390..2432
FT /note="LDL-receptor class B 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2411..2444
FT /note="HAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 2433..2474
FT /note="LDL-receptor class B 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 2524..2563
FT /note="LDL-receptor class A 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2566..2602
FT /note="LDL-receptor class A 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2605..2641
FT /note="LDL-receptor class A 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2639..2690
FT /note="LDL-receptor class A 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2696..2732
FT /note="LDL-receptor class A 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2734..2771
FT /note="LDL-receptor class A 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2774..2814
FT /note="LDL-receptor class A 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2818..2855
FT /note="LDL-receptor class A 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2858..2899
FT /note="LDL-receptor class A 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2904..2941
FT /note="LDL-receptor class A 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2983..3018
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 3070..3114
FT /note="LDL-receptor class B 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3115..3157
FT /note="LDL-receptor class B 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3128..3171
FT /note="HAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 3158..3201
FT /note="LDL-receptor class B 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3202..3244
FT /note="LDL-receptor class B 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3224..3256
FT /note="HAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 3245..3285
FT /note="LDL-receptor class B 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 3334..3371
FT /note="LDL-receptor class A 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3374..3410
FT /note="LDL-receptor class A 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3413..3450
FT /note="LDL-receptor class A 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3453..3491
FT /note="LDL-receptor class A 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3494..3533
FT /note="LDL-receptor class A 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3536..3572
FT /note="LDL-receptor class A 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3575..3611
FT /note="LDL-receptor class A 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3613..3649
FT /note="LDL-receptor class A 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3654..3692
FT /note="LDL-receptor class A 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3695..3733
FT /note="LDL-receptor class A 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3741..3778
FT /note="LDL-receptor class A 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REPEAT 3913..3925
FT /note="LDL-receptor class B 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3971..4013
FT /note="LDL-receptor class B 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3995..4027
FT /note="HAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 4014..4057
FT /note="LDL-receptor class B 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 4058..4102
FT /note="LDL-receptor class B 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 4197..4230
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4233..4269
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4270..4302
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4305..4341
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4376..4410
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 4446..4545
FT /note="Interaction with MAFB"
FT /evidence="ECO:0000250|UniProtKB:Q91ZX7"
FT BINDING 872
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 875
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 877
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 879
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 885
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 886
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1033
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1036
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1038
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1040
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1046
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1047
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1081
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1084
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1086
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1088
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1094
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT BINDING 1095
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT MOD_RES 2010
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZX7"
FT MOD_RES 4461
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT MOD_RES 4508
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT MOD_RES 4518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT MOD_RES 4521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07954"
FT MOD_RES 4524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91ZX7"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1051
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2906
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 4076
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 4126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 4180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 4280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 4365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 28..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 35..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 48..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 73..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 80..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 93..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 855..867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 862..880
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 874..891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 896..908
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 903..921
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 915..932
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 937..949
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 944..962
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 956..972
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 977..990
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 985..1003
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 997..1012
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1016..1028
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1023..1041
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1035..1052
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1063..1076
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1070..1089
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1083..1098
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1105..1119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1113..1132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1126..1141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1146..1160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1153..1173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1167..1183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2525..2538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2533..2551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2545..2562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2567..2579
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2574..2592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2586..2601
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2606..2618
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2613..2631
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2625..2640
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2640..2667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2645..2680
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2674..2689
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2697..2709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2704..2722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2716..2731
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2735..2747
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2742..2760
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2754..2770
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2775..2788
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2782..2801
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2795..2813
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2819..2831
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2826..2844
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2838..2854
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2859..2871
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2866..2885
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2879..2898
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2905..2918
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2913..2931
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2925..2940
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2987..2997
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2993..3006
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3335..3347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3342..3360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3354..3370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3375..3387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3382..3400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3394..3409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3414..3427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3421..3440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3434..3449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3454..3467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3461..3480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3474..3490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3495..3508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3502..3521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3515..3532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3537..3549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3544..3562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3556..3571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3576..3588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3583..3601
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3595..3610
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3614..3626
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3621..3639
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3633..3648
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3655..3667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3662..3680
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3674..3691
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3696..3710
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3704..3723
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3717..3732
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3742..3755
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3750..3768
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3762..3777
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 4201..4211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4205..4221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4237..4247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4241..4257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4259..4268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4273..4283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4277..4293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4309..4319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4313..4329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4331..4340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4378..4388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4382..4398
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4400..4409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 4545 AA; 504889 MW; E0C4668E30481D47 CRC64;
MLTPPLLLLL PLLSALVAGA TMDAPKTCSP KQFACRDQIT CISKGWRCDG ERDCPDGSDE
APEICPQSKA QRCPPNEHSC LGTELCVPMS RLCNGIQDCM DGSDEGAHCR ELRVNCSRMG
CQHHCVPTPS GPTCYCNNSF QLQADGKTCK DFDECSVYGT CSQLCTNTDG SFTCGCVEGY
LLQPDNRSCK AKNEPVDRPP VLLIANSQNI LATYLSGAQV STITPTSTRQ TTAMDFSYAN
ETVCWVHVGD SAAQTQLKCA RMPSLKGFVD EHTINISLSL HHVEQMAIDW LTGNFYFVDD
IDDRIFVCNR NGDTCVTLLD LELYNPKGIA LDPAMGKVFF TDYGQIPKVE RCDMDGQNRT
KLVDSKIVFP HGITLDLVSR LVYWADAYLD YIEVVDYEGK GRQTIIQGIL IEHLYGLTVF
ENYLYATNSD NANTQQKTSV IRVNRFNSTE YQVVTRVDKG GALHIYHQRR QPRVRSHACE
NDQYGKPGGC SDICLLANSH KARTCRCRSG FSLGSDGKSC KKPEHELFLV YGKGRPGIIR
GMDMGAKVPD EHMIPIENLM NPRALDFHAE TGFIYFADTT SYLIGRQKID GTERETILKD
GIHNVEGVAV DWMGDNLYWT DDGPKKTISV ARLEKAAQTR KTLIEGKMTH PRAIVVDPLN
GWMYWTDWEE DPKDSRRGRL ERAWMDGSHR DIFVTSKTVL WPNGLSLDIP AGRLYWVDAF
YDRIETILLN GTDRKIVYEG PELNHAFGLC HHGNYLFWTE YRSGSVYRLE RGVAGAQPTV
TLLRSERPPI FEIRMYDAQQ QQVGTNKCRV NNGGCSSLCL ATPGSRQCAC AEDQVLDADG
VTCLANPSYV PPPQCQPGEF ACANNRCIQE RWKCDGDNDC LDNSDEAPAL CHQHTCPSDR
FKCENNRCIP NRWLCDGDND CGNSEDESNA TCSARTCPPN QFSCASGRCI PISWTCDLDD
DCGDRSDESA SCAYPTCFPL TQFTCNNGRC ININWRCDND NDCGDNSDEA GCSHSCSSTQ
FKCNSGRCIP EHWTCDGDND CGDYSDETHA NCTNQATRPP GGCHSDEFQC RLDGLCIPLR
WRCDGDTDCM DSSDEKGCEG VTHVCDPNVK FGCKDSARCI SKAWVCDGDS DCEDNSDEEN
CEALACRPPS HPCANNTSVC LSPDKLCDGK DDCGDGSDEG ELCDQCSLNN GGCSHNCSVA
PGEGIVCSCP LGMELGPDNH TCQIQSYCAK HLKCSQKCDQ NKFSVKCSCY EGWVLEPDGE
SCRSLDPFKP FIIFSNRHEI RRIDLHKGDY SVLVPGLRNT IALDFHLSQS ALYWTDVVED
KIYRGKLLDN GALTSFEVVI QYGLATPEGL AVDWIAGNIY WVESNLDQIE VAKLDGTLRT
TLLAGDIEHP RAIALDPRDG ILFWTDWDAS LPRIEAASMS GAGRRTIHRE TGSGGWPNGL
TVDYLEKRIL WIDARSDAIY SARYDGSGHM EVLRGHEFLS HPFAVTLYGG EVYWTDWRTN
TLAKANKWTG HNVTVVQRTN TQPFDLQVYH PSRQPMAPNP CEANGGRGPC SHLCLINYNR
TVSCACPHLM KLHNDNTTCY EFKKFLLYAR QMEIRGVDLD APYYNYIISF TVPDIDNVTV
LDYDAREQRV YWSDVRTQAI KRAFINGTGV ETVVSADLPN AHGLAVDWVS RNLFWTSYDT
NKKQINVARL DGSFKNAVVQ GLEQPHGLVV HPLRGKLYWT DGDNISMVNM DGSNRTLLFS
GQKGPVGLAI DFPESKLYWI SSGNHTINRC NLDGSELEVI DTMRSQLGKA TALAIMGDKL
WWADQVSEKM GTCNKADGSG SVVLRNSTTL VMHMKVYDES IQLEHEGTNP CSVNNGDCSQ
LCLPTSETTR SCMCTAGYSL RSGQQACEGV GSFLLYSVHE GIRGIPLDPN DKSDALVPVS
GTSLAVGIDF HAENDTIYWV DMGLSTISRA KRDQTWREDV VTNGIGRVEG IAVDWIAGNI
YWTDQGFDVI EVARLNGSFR YVVISQGLDK PRAITVHPEK GYLFWTEWGH YPRIERSRLD
GTERVVLVNV SISWPNGISV DYQGGKLYWC DARMDKIERI DLETGENREV VLSSNNMDMF
SVSVFEDFIY WSDRTHANGS IKRGCKDNAT DSVPLRTGIG VQLKDIKVFN RDRQKGTNVC
AVANGGCQQL CLYRGGGQRA CACAHGMLAE DGASCREYAG YLLYSERTIL KSIHLSDERN
LNAPVQPFED PEHMKNVIAL AFDYRAGTSP GTPNRIFFSD IHFGNIQQIN DDGSGRTTIV
ENVGSVEGLA YHRGWDTLYW TSYTTSTITR HTVDQTRPGA FERETVITMS GDDHPRAFVL
DECQNLMFWT NWNELHPSIM RAALSGANVL TLIEKDIRTP NGLAIDHRAE KLYFSDATLD
KIERCEYDGS HRYVILKSEP VHPFGLAVYG EHIFWTDWVR RAVQRANKYV GSDMKLLRVD
IPQQPMGIIA VANDTNSCEL SPCRINNGGC QDLCLLTHQG HVNCSCRGGR ILQEDFTCRA
MNSSCRAQDE FECANGECIS FSLTCDGVSH CKDKSDEKPS YCNSRRCKKT FRQCNNGRCV
SNMLWCNGVD DCGDGSDEIP CNKTACGVGE FRCRDGSCIG NSSRCNQFVD CEDASDEMNC
SATDCSSYFR LGVKGVLFQP CERTSLCYAP SWVCDGANDC GDYSDERDCP GVKRPRCPLN
YFACPSGRCI PMSWTCDKED DCENGEDETH CNKFCSEAQF ECQNHRCISK QWLCDGSDDC
GDGSDEAAHC EGKTCGPSSF SCPGTHVCVP ERWLCDGDKD CADGADESIS AGCLYNSTCD
DREFMCQNRL CIPKHFVCDH DRDCADGSDE SPECEYPTCG PNEFRCANGR CLSSRQWECD
GENDCHDHSD EAPKNPHCTS PEHKCNASSQ FLCSSGRCVA EALLCNGQDD CGDGSDERGC
HVNECLSRKL SGCSQDCEDL KIGFKCRCRP GFRLKDDGRT CADVDECSTT FPCSQLCINT
HGSYKCLCVE GYAPRGGDPH SCKAVTDEEP FLIFANRYYL RKLNLDGSNY TLLKQGLNNA
VALDFDYRGQ MIYWTDVTTQ GSMIRRMHLN GSNVQVLHRT GLSNPDGLAV DWVGGNLYWC
DKGRDTIEVS KLNGAYRTVL VSSGLREPRA LVVDVQNGYL YWTDWGDHSL IGRIGMDGSG
RSIIVDTKIT WPNGLTVDYV TERIYWADAR EDYIEFASLD GSNRHVVLSQ DIPHIFALTL
FEDYVYWTDW ETKSINRAHK TTGANKTLLI STLHRPMDLH VFHALRQPDV PNHPCKVNNG
GCSNLCLLSP GGGHKCACPT NFYLGGDGRT CVSNCTASQF VCKNDKCIPF WWKCDTEDDC
GDHSDEPPDC PEFKCRPGQF QCSTGICTNP AFICDGDNDC QDNSDEANCD IHVCLPSQFK
CTNTNRCIPG IFRCNGQDNC GDGEDERDCP EVTCAPNQFQ CSITKRCIPR VWVCDRDNDC
VDGSDEPANC TQMTCGVDEF RCKDSGRCIP ARWKCDGEDD CGDGSDEPKE ECDERTCEPY
QFRCKNNRCV PGRWQCDYDN DCGDNSDEES CTPRPCSESE FSCANGRCIA GRWKCDGDHD
CADGSDEKDC TPRCDMDQFQ CKSGHCIPLR WRCDADADCM DGSDEEACGT GVRTCPLDEF
QCNNTLCKPL AWKCDGEDDC GDNSDENPEE CTRFQCPPNR PFRCKNDRVC LWIGRQCDGT
DNCGDGTDEE DCEPPTAQNP HCKDKKEFLC RNQRCLSSSL RCNMFDDCGD GSDEEDCSID
PKLTSCATNA SMCGDEARCV RTEKAAYCAC RPGFHTVPGQ PGCQDINECL RFGTCSQLCN
NTKGGHLCSC ARNFMKTHNT CKAEGSEYQV LYIADDNEIR SLFPGHPHSA YEQAFQGDES
VRIDAMDVHV KAGRVYWTNW HTGTISYRSL PPAAPPTTSN RHRRQIDRGV THLNISGLKM
PRGIAIDWVA GNVYWTDSGR DVIEVAQMKG ENRKTLISGM IDEPHAIVVD PLRGTMYWSD
WGNHPKIETA AMDGTLRETL VQDNIQWPTG LAVDYHNERL YWADAKLSVI GSIRLNGTDP
IVAVDSKRGL SHPFSIDVFE DYIYGVTYIN NRVFKIHKFG HSPLINLTGG LSHASDVVLY
HQHKQPEVTN PCDRKKCEWL CLLSPSGPVC TCPNGKRLDN GTCVPVPSPT PPPDAPRPGT
CTLQCFNGGS CFLNARRQPK CRCQPRYTGD KCELDQCWEY CHNGGTCAAS PSGMPTCRCP
TGFTGPRCTQ QVCAGYCANN STCTVNQGNQ PQCRCLPGFL GDRCQYRQCS GFCENFGTCQ
MAADGSRQCR CTVYFEGTRC EVNKCSRCLQ GACVVNKQTG DVTCNCTDGR VAPSCLTCID
HCSNGGSCTM NSKMMPECQC PPHMTGPRCE EQVVSQQQPG HMTSILIPLL LLLLLLLVAG
VVFWYKRRVR GAKGFQHQRM TNGAMNVEIG NPTYKMYEGG EPDDVGGLLD ADFALDPDKP
TNFTNPVYAT LYMGGHGSRH SLASTDEKRE LLGRGPEDEI GDPLA
