LRP2_RAT
ID LRP2_RAT Reviewed; 4660 AA.
AC P98158;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Low-density lipoprotein receptor-related protein 2;
DE Short=LRP-2;
DE AltName: Full=Glycoprotein 330 {ECO:0000303|PubMed:7937880};
DE Short=gp330 {ECO:0000303|PubMed:7937880};
DE AltName: Full=Megalin;
DE Flags: Precursor;
GN Name=Lrp2;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=7937880; DOI=10.1073/pnas.91.21.9725;
RA Saito A., Pietromonaco S., Loo A.K.C., Farquhar M.G.;
RT "Complete cloning and sequencing of rat gp330/'megalin,' a distinctive
RT member of the low density lipoprotein receptor gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9725-9729(1994).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=6752952; DOI=10.1073/pnas.79.18.5557;
RA Kerjaschki D., Farquhar M.G.;
RT "The pathogenic antigen of Heymann nephritis is a membrane glycoprotein of
RT the renal proximal tubule brush border.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:5557-5561(1982).
RN [3]
RP INTERACTION WITH LRPAP1.
RX PubMed=1400426; DOI=10.1016/s0021-9258(19)36811-5;
RA Kounnas M.Z., Argraves W.S., Strickland D.K.;
RT "The 39-kDa receptor-associated protein interacts with two members of the
RT low density lipoprotein receptor family, alpha 2-macroglobulin receptor and
RT glycoprotein 330.";
RL J. Biol. Chem. 267:21162-21166(1992).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=7510321; DOI=10.1177/42.4.7510321;
RA Zheng G., Bachinsky D.R., Stamenkovic I., Strickland D.K., Brown D.,
RA Andres G., McCluskey R.T.;
RT "Organ distribution in rats of two members of the low-density lipoprotein
RT receptor gene family, gp330 and LRP/alpa 2MR, and the receptor-associated
RT protein (RAP).";
RL J. Histochem. Cytochem. 42:531-542(1994).
RN [5]
RP FUNCTION IN UPTAKE OF POLYBASIC DRUGS.
RX PubMed=7544804; DOI=10.1172/jci118176;
RA Moestrup S.K., Cui S., Vorum H., Bregengaard C., Bjorn S.E., Norris K.,
RA Gliemann J., Christensen E.I.;
RT "Evidence that epithelial glycoprotein 330/megalin mediates uptake of
RT polybasic drugs.";
RL J. Clin. Invest. 96:1404-1413(1995).
RN [6]
RP FUNCTION.
RX PubMed=11964399; DOI=10.1074/jbc.m201933200;
RA McCarthy R.A., Barth J.L., Chintalapudi M.R., Knaak C., Argraves W.S.;
RT "Megalin functions as an endocytic sonic hedgehog receptor.";
RL J. Biol. Chem. 277:25660-25667(2002).
RN [7]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=12519751; DOI=10.1152/ajpcell.00514.2002;
RA Takeda T., Yamazaki H., Farquhar M.G.;
RT "Identification of an apical sorting determinant in the cytoplasmic tail of
RT megalin.";
RL Am. J. Physiol. 284:C1105-C1113(2003).
RN [8]
RP FUNCTION, INTERACTION WITH MB, AND SUBCELLULAR LOCATION.
RX PubMed=12724130; DOI=10.1152/ajprenal.00062.2003;
RA Gburek J., Birn H., Verroust P.J., Goj B., Jacobsen C., Moestrup S.K.,
RA Willnow T.E., Christensen E.I.;
RT "Renal uptake of myoglobin is mediated by the endocytic receptors megalin
RT and cubilin.";
RL Am. J. Physiol. 285:F451-F458(2003).
RN [9]
RP FUNCTION.
RX PubMed=15126248; DOI=10.1152/ajprenal.00233.2003;
RA Klassen R.B., Crenshaw K., Kozyraki R., Verroust P.J., Tio L., Atrian S.,
RA Allen P.L., Hammond T.G.;
RT "Megalin mediates renal uptake of heavy metal metallothionein complexes.";
RL Am. J. Physiol. 287:F393-F403(2004).
RN [10]
RP FUNCTION.
RX PubMed=15467006; DOI=10.1152/ajprenal.00243.2004;
RA Gonzalez-Villalobos R., Klassen R.B., Allen P.L., Navar L.G., Hammond T.G.;
RT "Megalin binds and internalizes angiotensin II.";
RL Am. J. Physiol. 288:F420-F427(2005).
RN [11]
RP FUNCTION, AND INTERACTION WITH SHBG.
RX PubMed=16143106; DOI=10.1016/j.cell.2005.06.032;
RA Hammes A., Andreassen T.K., Spoelgen R., Raila J., Hubner N., Schulz H.,
RA Metzger J., Schweigert F.J., Luppa P.B., Nykjaer A., Willnow T.E.;
RT "Role of endocytosis in cellular uptake of sex steroids.";
RL Cell 122:751-762(2005).
RN [12]
RP FUNCTION.
RX PubMed=16380466; DOI=10.1152/ajprenal.00164.2005;
RA Gonzalez-Villalobos R., Klassen R.B., Allen P.L., Johanson K., Baker C.B.,
RA Kobori H., Navar L.G., Hammond T.G.;
RT "Megalin binds and internalizes angiotensin-(1-7).";
RL Am. J. Physiol. 290:F1270-F1275(2006).
RN [13]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17063000; DOI=10.1247/csf.06013;
RA Ishida T., Hatae T., Nishi N., Araki N.;
RT "Soluble megalin is accumulated in the lumen of the rat endolymphatic
RT sac.";
RL Cell Struct. Funct. 31:77-85(2006).
RN [14]
RP FUNCTION.
RX PubMed=16801528; DOI=10.1369/jhc.5a6899.2006;
RA Morales C.R., Zeng J., El Alfy M., Barth J.L., Chintalapudi M.R.,
RA McCarthy R.A., Incardona J.P., Argraves W.S.;
RT "Epithelial trafficking of Sonic hedgehog by megalin.";
RL J. Histochem. Cytochem. 54:1115-1127(2006).
RN [15]
RP FUNCTION.
RX PubMed=16099815; DOI=10.1210/me.2005-0209;
RA Faber K., Hvidberg V., Moestrup S.K., Dahlbaeck B., Nielsen L.B.;
RT "Megalin is a receptor for apolipoprotein M, and kidney-specific megalin-
RT deficiency confers urinary excretion of apolipoprotein M.";
RL Mol. Endocrinol. 20:212-218(2006).
RN [16]
RP FUNCTION, AND INTERACTION WITH CST3.
RX PubMed=17462596; DOI=10.1016/j.bbrc.2007.04.072;
RA Kaseda R., Iino N., Hosojima M., Takeda T., Hosaka K., Kobayashi A.,
RA Yamamoto K., Suzuki A., Kasai A., Suzuki Y., Gejyo F., Saito A.;
RT "Megalin-mediated endocytosis of cystatin C in proximal tubule cells.";
RL Biochem. Biophys. Res. Commun. 357:1130-1134(2007).
RN [17]
RP FUNCTION.
RX PubMed=17846082; DOI=10.1096/fj.07-9171com;
RA Koenig O., Ruettiger L., Mueller M., Zimmermann U., Erdmann B.,
RA Kalbacher H., Gross M., Knipper M.;
RT "Estrogen and the inner ear: megalin knockout mice suffer progressive
RT hearing loss.";
RL FASEB J. 22:410-417(2008).
RN [18]
RP FUNCTION, INTERACTION WITH ALB, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=18466341; DOI=10.1111/j.1471-4159.2008.05462.x;
RA Bento-Abreu A., Velasco A., Polo-Hernandez E., Perez-Reyes P.L.,
RA Tabernero A., Medina J.M.;
RT "Megalin is a receptor for albumin in astrocytes and is required for the
RT synthesis of the neurotrophic factor oleic acid.";
RL J. Neurochem. 106:1149-1159(2008).
RN [19]
RP FUNCTION, INTERACTION WITH LEP, AND TISSUE SPECIFICITY.
RX PubMed=17324488; DOI=10.1016/j.neurobiolaging.2007.01.008;
RA Dietrich M.O., Spuch C., Antequera D., Rodal I., de Yebenes J.G.,
RA Molina J.A., Bermejo F., Carro E.;
RT "Megalin mediates the transport of leptin across the blood-CSF barrier.";
RL Neurobiol. Aging 29:902-912(2008).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19202329; DOI=10.1159/000199446;
RA Tauris J., Christensen E.I., Nykjaer A., Jacobsen C., Petersen C.M.,
RA Ovesen T.;
RT "Cubilin and megalin co-localize in the neonatal inner ear.";
RL Audiol. Neurootol. 14:267-278(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4464; SER-4577; SER-4624 AND
RP SER-4658, AND 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 [22]
RP INTERACTION WITH LDLRAP1, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
RP TYR-4527.
RX PubMed=23836931; DOI=10.1083/jcb.201211110;
RA Shah M., Baterina O.Y. Jr., Taupin V., Farquhar M.G.;
RT "ARH directs megalin to the endocytic recycling compartment to regulate its
RT proteolysis and gene expression.";
RL J. Cell Biol. 202:113-127(2013).
RN [23]
RP FUNCTION, AND INTERACTION WITH MMP2 AND TIMP1.
RX PubMed=28659595; DOI=10.1038/s41598-017-04648-y;
RA Johanns M., Lemoine P., Janssens V., Grieco G., Moestrup S.K., Nielsen R.,
RA Christensen E.I., Courtoy P.J., Emonard H., Marbaix E., Henriet P.;
RT "Cellular uptake of proMMP-2:TIMP-2 complexes by the endocytic receptor
RT megalin/LRP-2.";
RL Sci. Rep. 7:4328-4328(2017).
RN [24]
RP STRUCTURE BY NMR OF 1185-1229, CALCIUM-BINDING SITE, AND DISULFIDE BONDS.
RX PubMed=17245526; DOI=10.1007/s10858-006-9129-3;
RA Wolf C.A., Dancea F., Shi M., Bade-Noskova V., Ruterjans H., Kerjaschki D.,
RA Lucke C.;
RT "Solution structure of the twelfth cysteine-rich ligand-binding repeat in
RT rat megalin.";
RL J. Biomol. NMR 37:321-328(2007).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 4455-4465 IN COMPLEX WITH ANKRA2,
RP INTERACTION WITH ANKRA2, AND MOTIF.
RX PubMed=22649097; DOI=10.1126/scisignal.2002979;
RA Xu C., Jin J., Bian C., Lam R., Tian R., Weist R., You L., Nie J.,
RA Bochkarev A., Tempel W., Tan C.S., Wasney G.A., Vedadi M., Gish G.D.,
RA Arrowsmith C.H., Pawson T., Yang X.J., Min J.;
RT "Sequence-specific recognition of a PxLPxI/L motif by an ankyrin repeat
RT tumbler lock.";
RL Sci. Signal. 5:RA39-RA39(2012).
CC -!- FUNCTION: Multiligand endocytic receptor. Acts together with CUBN to
CC mediate endocytosis of high-density lipoproteins (By similarity).
CC Mediates receptor-mediated uptake of polybasic drugs such as aprotinin,
CC aminoglycosides and polymyxin B (PubMed:7544804, PubMed:19202329). In
CC the kidney, mediates the tubular uptake and clearance of leptin (By
CC similarity). Also mediates transport of leptin across the blood-brain
CC barrier through endocytosis at the choroid plexus epithelium
CC (PubMed:17324488). Endocytosis of leptin in neuronal cells is required
CC for hypothalamic leptin signaling and leptin-mediated regulation of
CC feeding and body weight (By similarity). Mediates endocytosis and
CC subsequent lysosomal degradation of CST3 in kidney proximal tubule
CC cells (PubMed:17462596). Mediates renal uptake of 25-hydroxyvitamin D3
CC in complex with the vitamin D3 transporter GC/DBP (By similarity).
CC Mediates renal uptake of metallothionein-bound heavy metals
CC (PubMed:15126248). Together with CUBN, mediates renal reabsorption of
CC myoglobin (PubMed:12724130). Mediates renal uptake and subsequent
CC lysosomal degradation of APOM (PubMed:16099815). Plays a role in kidney
CC selenium homeostasis by mediating renal endocytosis of selenoprotein
CC SEPP1 (By similarity). Mediates renal uptake of the antiapoptotic
CC protein BIRC5/survivin which may be important for functional integrity
CC of the kidney (By similarity). Mediates renal uptake of matrix
CC metalloproteinase MMP2 in complex with metalloproteinase inhibitor
CC TIMP1 (PubMed:28659595). Mediates endocytosis of Sonic hedgehog protein
CC N-product (ShhN), the active product of SHH (PubMed:11964399,
CC PubMed:16801528). Also mediates ShhN transcytosis (PubMed:16801528). In
CC the embryonic neuroepithelium, mediates endocytic uptake and
CC degradation of BMP4, is required for correct SHH localization in the
CC ventral neural tube and plays a role in patterning of the ventral
CC telencephalon (By similarity). Required at the onset of neurulation to
CC sequester SHH on the apical surface of neuroepithelial cells of the
CC rostral diencephalon ventral midline and to control PTCH1-dependent
CC uptake and intracellular trafficking of SHH (By similarity). During
CC neurulation, required in neuroepithelial cells for uptake of folate
CC bound to the folate receptor FOLR1 which is necessary for neural tube
CC closure (By similarity). In the adult brain, negatively regulates BMP
CC signaling in the subependymal zone which enables neurogenesis to
CC proceed (By similarity). In astrocytes, mediates endocytosis of ALB
CC which is required for the synthesis of the neurotrophic factor oleic
CC acid (PubMed:18466341). Involved in neurite branching (By similarity).
CC During optic nerve development, required for SHH-mediated migration and
CC proliferation of oligodendrocyte precursor cells (By similarity).
CC Mediates endocytic uptake and clearance of SHH in the retinal margin
CC which protects retinal progenitor cells from mitogenic stimuli and
CC keeps them quiescent (By similarity). Plays a role in reproductive
CC organ development by mediating uptake in reproductive tissues of
CC androgen and estrogen bound to the sex hormone binding protein SHBG
CC (PubMed:16143106). Mediates endocytosis of angiotensin-2
CC (PubMed:15467006). Also mediates endocytosis of angiotensin 1-7
CC (PubMed:16380466). Binds to the complex composed of beta-amyloid
CC protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal
CC degradation (By similarity). Required for embryonic heart development
CC (By similarity). Required for normal hearing, possibly through
CC interaction with estrogen in the inner ear (PubMed:17846082).
CC {ECO:0000250|UniProtKB:A2ARV4, ECO:0000250|UniProtKB:C0HL13,
CC ECO:0000250|UniProtKB:P98164, ECO:0000269|PubMed:11964399,
CC ECO:0000269|PubMed:12724130, ECO:0000269|PubMed:15126248,
CC ECO:0000269|PubMed:15467006, ECO:0000269|PubMed:16099815,
CC ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:16380466,
CC ECO:0000269|PubMed:16801528, ECO:0000269|PubMed:17324488,
CC ECO:0000269|PubMed:17462596, ECO:0000269|PubMed:17846082,
CC ECO:0000269|PubMed:18466341, ECO:0000269|PubMed:19202329,
CC ECO:0000269|PubMed:28659595, ECO:0000269|PubMed:7544804}.
CC -!- SUBUNIT: Binds plasminogen, extracellular matrix components,
CC plasminogen activator-plasminogen activator inhibitor type I complex,
CC apolipoprotein E-enriched beta-VLDL, lipoprotein lipase, lactoferrin,
CC CLU/clusterin and calcium. Forms a multimeric complex together with
CC LRPAP1 (PubMed:1400426). Interacts (via PxLPxI/L motif) with ANKRA2
CC (via ankyrin repeats) (PubMed:22649097). Interacts with LRP2BP.
CC Interacts (via NPXY motif) with DAB2; the interaction is not affected
CC by tyrosine phosphorylation of the NPXY motif (By similarity).
CC Interacts with MB (PubMed:12724130). Interacts with BMP4 (By
CC similarity). Interacts with the Sonic hedgehog protein N-product which
CC is the active product of SHH (By similarity). Interacts with CST3 in a
CC calcium-dependent manner (PubMed:17462596). Interacts with the vitamin-
CC D binding protein GC/DBP (By similarity). Interacts with sex hormone-
CC binding protein SHBG (PubMed:16143106). Interacts with angiotensin-2
CC (By similarity). Also interacts with angiotensin 1-7 (By similarity).
CC Interacts with APOM (By similarity). Interacts with selenoprotein SEPP1
CC (By similarity). Interacts with LEP (PubMed:17324488). Interacts with
CC ALB (PubMed:18466341). Interacts with the antiapoptotic protein
CC BIRC5/survivin (By similarity). Interacts with matrix metalloproteinase
CC MMP2 in complex with metalloproteinase inhibitor TIMP1
CC (PubMed:28659595). In neurons, forms a trimeric complex with APP and
CC APPB1/FE65 (By similarity). Interacts with LDLRAP1/ARH; mediates
CC trafficking of LRP2 to the endocytic recycling compartment
CC (PubMed:23836931). Does not interact with beta-amyloid protein 40 alone
CC but interacts with the complex composed of beta-amyloid protein 40 and
CC CLU/APOJ (By similarity). Interacts with MDK (By similarity).
CC {ECO:0000250|UniProtKB:A2ARV4, ECO:0000250|UniProtKB:C0HL13,
CC ECO:0000250|UniProtKB:P98164, ECO:0000269|PubMed:12724130,
CC ECO:0000269|PubMed:1400426, ECO:0000269|PubMed:15467006,
CC ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:17462596,
CC ECO:0000269|PubMed:18466341, ECO:0000269|PubMed:22649097,
CC ECO:0000269|PubMed:23836931, ECO:0000269|PubMed:28659595}.
CC -!- INTERACTION:
CC P98158; O88797: Dab2; NbExp=2; IntAct=EBI-6306650, EBI-6109302;
CC PRO_0000017322; D3ZAR1: Ldlrap1; NbExp=3; IntAct=EBI-9251342, EBI-9250714;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:12519751, ECO:0000269|PubMed:18466341,
CC ECO:0000269|PubMed:19202329, ECO:0000269|PubMed:6752952}; Single-pass
CC type I membrane protein {ECO:0000255}. Endosome lumen
CC {ECO:0000269|PubMed:17063000}. Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:A2ARV4}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:A2ARV4}. Cell projection, axon
CC {ECO:0000250|UniProtKB:A2ARV4}. Note=Localizes to brush border
CC membranes in the kidney (PubMed:6752952, PubMed:12724130). In the
CC endolymphatic sac of the inner ear, located in the lumen of endosomes
CC as a soluble form (PubMed:17063000). {ECO:0000269|PubMed:12724130,
CC ECO:0000269|PubMed:6752952}.
CC -!- TISSUE SPECIFICITY: In the inner ear, expressed in the lumen of the
CC endolymphatic sac where it localizes to macrophage-like cells as well
CC as to mitochondria-rich and ribosome-rich epithelial cells (at protein
CC level) (PubMed:17063000). In the inner ear, expressed in marginal cells
CC of the stria vascularis, epithelial cells at the spiral prominence,
CC epithelial cells of Reissner's membrane facing the cochlear duct, and
CC Kolliker's organ (at protein level) (PubMed:19202329). Expressed in the
CC choroid plexus epithelium in the brain (at protein level)
CC (PubMed:17324488). In the brain, also expressed in astrocytes (at
CC protein level) (PubMed:18466341). Expression also detected in
CC epithelial cells of the kidney glomerulus and proximal tubule, lung,
CC epididymis and yolk sac (PubMed:7510321). {ECO:0000269|PubMed:17063000,
CC ECO:0000269|PubMed:17324488, ECO:0000269|PubMed:18466341,
CC ECO:0000269|PubMed:19202329, ECO:0000269|PubMed:7510321}.
CC -!- DEVELOPMENTAL STAGE: In the brain, expression is high after birth and
CC gradually decreases from postnatal day 4 until the end of the first
CC postnatal week. {ECO:0000269|PubMed:18466341}.
CC -!- DOMAIN: Two overlapping PxLPxI/L motifs mediate interaction with
CC ankyrin repeats of ANKRA2. {ECO:0000269|PubMed:22649097}.
CC -!- DOMAIN: The cytoplasmic domain is required for sorting to the apical
CC cell membrane. {ECO:0000269|PubMed:12519751}.
CC -!- PTM: A fraction undergoes proteolytic cleavage of the extracellular
CC domain at the cell membrane to generate a cytoplasmic tail fragment.
CC This is internalized into the early endosome from where it trafficks in
CC an LDLRAP1/ARH-dependent manner to the endocytic recycling compartment
CC (ERC). In the ERC, it is further cleaved by gamma-secretase to release
CC a fragment which translocates to the nucleus and mediates
CC transcriptional repression. {ECO:0000269|PubMed:23836931}.
CC -!- PTM: N-glycosylation is required for ligand binding.
CC {ECO:0000250|UniProtKB:A2ARV4}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR EMBL; L34049; AAA51369.1; -; mRNA.
DR PIR; T42737; T42737.
DR RefSeq; NP_110454.1; NM_030827.1.
DR PDB; 2I1P; NMR; -; A=1185-1229.
DR PDB; 3V2O; X-ray; 1.89 A; B=4448-4466.
DR PDB; 3V2X; X-ray; 1.85 A; B=4455-4465.
DR PDBsum; 2I1P; -.
DR PDBsum; 3V2O; -.
DR PDBsum; 3V2X; -.
DR SMR; P98158; -.
DR BioGRID; 247894; 2.
DR CORUM; P98158; -.
DR DIP; DIP-44866N; -.
DR IntAct; P98158; 6.
DR STRING; 10116.ENSRNOP00000066394; -.
DR GlyConnect; 344; 25 N-Linked glycans.
DR GlyGen; P98158; 43 sites, 48 N-linked glycans (1 site).
DR iPTMnet; P98158; -.
DR PhosphoSitePlus; P98158; -.
DR PaxDb; P98158; -.
DR PRIDE; P98158; -.
DR GeneID; 29216; -.
DR KEGG; rno:29216; -.
DR UCSC; RGD:68407; rat.
DR CTD; 4036; -.
DR RGD; 68407; Lrp2.
DR eggNOG; KOG1215; Eukaryota.
DR InParanoid; P98158; -.
DR OrthoDB; 1606at2759; -.
DR PhylomeDB; P98158; -.
DR EvolutionaryTrace; P98158; -.
DR PRO; PR:P98158; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; IDA:RGD.
DR GO; GO:0005903; C:brush border; IDA:RGD.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0030492; F:hemoglobin binding; IDA:RGD.
DR GO; GO:0042562; F:hormone binding; IPI:RGD.
DR GO; GO:0031994; F:insulin-like growth factor I binding; IDA:ARUK-UCL.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:RGD.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0140318; F:protein transporter activity; IDA:ARUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; TAS:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0097242; P:amyloid-beta clearance; IMP:ARUK-UCL.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0035904; P:aorta development; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:ARUK-UCL.
DR GO; GO:0061642; P:chemoattraction of axon; IMP:RGD.
DR GO; GO:0060982; P:coronary artery morphogenesis; ISS:UniProtKB.
DR GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR GO; GO:0020028; P:endocytic hemoglobin import into cell; IMP:RGD.
DR GO; GO:0006897; P:endocytosis; IMP:RGD.
DR GO; GO:0016197; P:endosomal transport; IMP:RGD.
DR GO; GO:1904447; P:folate import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0046879; P:hormone secretion; IMP:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR GO; GO:0030001; P:metal ion transport; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IC:BHF-UCL.
DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR GO; GO:0140058; P:neuron projection arborization; ISS:UniProtKB.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:UniProtKB.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
DR GO; GO:0140077; P:positive regulation of lipoprotein transport; IMP:RGD.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
DR GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0015031; P:protein transport; ISO:RGD.
DR GO; GO:0061156; P:pulmonary artery morphogenesis; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR GO; GO:0044321; P:response to leptin; IMP:ARUK-UCL.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0033280; P:response to vitamin D; IEP:RGD.
DR GO; GO:0010165; P:response to X-ray; IDA:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0003139; P:secondary heart field specification; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0045056; P:transcytosis; IMP:UniProtKB.
DR GO; GO:0060068; P:vagina development; ISS:UniProtKB.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISS:UniProtKB.
DR GO; GO:0003281; P:ventricular septum development; ISO:RGD.
DR GO; GO:0006766; P:vitamin metabolic process; ISO:RGD.
DR CDD; cd00112; LDLa; 36.
DR Gene3D; 2.120.10.30; -; 8.
DR Gene3D; 4.10.400.10; -; 36.
DR IDEAL; IID50221; -.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
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; 2.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 35.
DR Pfam; PF00058; Ldl_recept_b; 14.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 22.
DR SMART; SM00179; EGF_CA; 9.
DR SMART; SM00192; LDLa; 36.
DR SMART; SM00135; LY; 36.
DR SUPFAM; SSF57184; SSF57184; 2.
DR SUPFAM; SSF57424; SSF57424; 35.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 8.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS01209; LDLRA_1; 31.
DR PROSITE; PS50068; LDLRA_2; 36.
DR PROSITE; PS51120; LDLRB; 35.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Cell projection; Coated pit;
KW Disulfide bond; EGF-like domain; Endocytosis; Endosome; Glycoprotein;
KW Hearing; Membrane; Metal-binding; Neurogenesis; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; SH3-binding; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..4660
FT /note="Low-density lipoprotein receptor-related protein 2"
FT /id="PRO_0000017322"
FT TOPO_DOM 26..4425
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4426..4446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4447..4660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..63
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 66..104
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 107..143
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 141..180
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 182..218
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 221..257
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 264..307
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 347..382
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 435..477
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 478..520
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 521..567
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 568..612
FT /note="LDL-receptor class B 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 752..794
FT /note="LDL-receptor class B 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 795..836
FT /note="LDL-receptor class B 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 837..880
FT /note="LDL-receptor class B 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 881..924
FT /note="LDL-receptor class B 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 1024..1060
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1065..1102
FT /note="LDL-receptor class A 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1109..1145
FT /note="LDL-receptor class A 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1149..1185
FT /note="LDL-receptor class A 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1187..1224
FT /note="LDL-receptor class A 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1230..1268
FT /note="LDL-receptor class A 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1271..1307
FT /note="LDL-receptor class A 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1312..1350
FT /note="LDL-receptor class A 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1350..1390
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1391..1430
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1479..1521
FT /note="LDL-receptor class B 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1522..1564
FT /note="LDL-receptor class B 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1567..1610
FT /note="LDL-receptor class B 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1611..1655
FT /note="LDL-receptor class B 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1656..1696
FT /note="LDL-receptor class B 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1791..1833
FT /note="LDL-receptor class B 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1834..1883
FT /note="LDL-receptor class B 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1884..1931
FT /note="LDL-receptor class B 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1932..1973
FT /note="LDL-receptor class B 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 1974..2014
FT /note="LDL-receptor class B 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2108..2157
FT /note="LDL-receptor class B 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2158..2202
FT /note="LDL-receptor class B 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2203..2246
FT /note="LDL-receptor class B 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2247..2290
FT /note="LDL-receptor class B 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2432..2478
FT /note="LDL-receptor class B 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2479..2519
FT /note="LDL-receptor class B 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2520..2563
FT /note="LDL-receptor class B 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2564..2605
FT /note="LDL-receptor class B 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 2606..2647
FT /note="LDL-receptor class B 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 2700..2738
FT /note="LDL-receptor class A 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2741..2777
FT /note="LDL-receptor class A 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2780..2819
FT /note="LDL-receptor class A 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2822..2861
FT /note="LDL-receptor class A 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2864..2902
FT /note="LDL-receptor class A 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2907..2946
FT /note="LDL-receptor class A 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2949..2991
FT /note="LDL-receptor class A 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 2994..3030
FT /note="LDL-receptor class A 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3033..3071
FT /note="LDL-receptor class A 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3076..3112
FT /note="LDL-receptor class A 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3112..3153
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3154..3194
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 3241..3283
FT /note="LDL-receptor class B 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3284..3326
FT /note="LDL-receptor class B 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3335..3378
FT /note="LDL-receptor class B 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3379..3421
FT /note="LDL-receptor class B 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 3422..3462
FT /note="LDL-receptor class B 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 3513..3551
FT /note="LDL-receptor class A 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3554..3592
FT /note="LDL-receptor class A 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3595..3633
FT /note="LDL-receptor class A 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3636..3674
FT /note="LDL-receptor class A 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3679..3717
FT /note="LDL-receptor class A 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3720..3757
FT /note="LDL-receptor class A 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3760..3796
FT /note="LDL-receptor class A 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3799..3835
FT /note="LDL-receptor class A 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3843..3881
FT /note="LDL-receptor class A 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3884..3923
FT /note="LDL-receptor class A 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3929..3965
FT /note="LDL-receptor class A 36"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 3968..4003
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4009..4050
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 4156..4198
FT /note="LDL-receptor class B 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 4199..4242
FT /note="LDL-receptor class B 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT REPEAT 4244..4285
FT /note="LDL-receptor class B 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00461"
FT DOMAIN 4379..4413
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 4559..4582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4597..4610
FT /note="Interaction with DAB2"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT REGION 4617..4660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4454..4463
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 4457..4462
FT /note="PxLPxI/L motif 1; mediates interaction with ANKRA2"
FT /evidence="ECO:0000269|PubMed:22649097"
FT MOTIF 4460..4465
FT /note="PxLPxI/L motif 2; mediates interaction with ANKRA2"
FT /evidence="ECO:0000269|PubMed:22649097"
FT MOTIF 4522..4527
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT MOTIF 4603..4606
FT /note="NPXY motif"
FT MOTIF 4606..4609
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 4619..4630
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT BINDING 1127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P98164"
FT BINDING 1206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17245526"
FT BINDING 1209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17245526"
FT BINDING 1211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17245526"
FT BINDING 1213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17245526"
FT BINDING 1219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17245526"
FT BINDING 1220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17245526"
FT MOD_RES 4464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2ARV4"
FT MOD_RES 4577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4637
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A2ARV4"
FT MOD_RES 4658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1063
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3682
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3969
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3980
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 35..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 47..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 67..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 74..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 87..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 108..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 115..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 127..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 142..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 152..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 164..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 183..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 190..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 202..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 222..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 229..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 241..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 265..278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 272..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 285..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 351..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 357..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1025..1037
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1032..1050
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1044..1059
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1066..1079
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1073..1092
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1086..1101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1110..1122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1117..1135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1129..1144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1150..1162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1157..1175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1169..1184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1188..1201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124,
FT ECO:0000269|PubMed:17245526"
FT DISULFID 1195..1214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124,
FT ECO:0000269|PubMed:17245526"
FT DISULFID 1208..1223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124,
FT ECO:0000269|PubMed:17245526"
FT DISULFID 1231..1244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1238..1257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1251..1267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1272..1284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1279..1297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1291..1306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1313..1326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1320..1339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1333..1349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1354..1365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1361..1374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1376..1389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1395..1405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1401..1414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1416..1429
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2701..2713
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2708..2726
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2720..2737
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2742..2754
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2749..2767
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2761..2776
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2781..2794
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2789..2807
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2801..2818
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2823..2836
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2830..2849
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2843..2860
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2865..2878
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2872..2891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2885..2901
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2908..2920
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2915..2933
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2927..2945
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2950..2967
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2957..2980
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2974..2990
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 2995..3007
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3002..3020
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3014..3029
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3034..3046
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3041..3059
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3053..3070
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3077..3089
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3084..3102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3096..3111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3116..3128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3124..3137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3139..3152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3158..3169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3165..3178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3180..3193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3514..3527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3521..3540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3534..3550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3555..3567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3562..3580
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3574..3591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3596..3608
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3603..3621
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3615..3632
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3637..3649
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3644..3662
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3656..3673
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3680..3694
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3688..3707
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3701..3716
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3721..3734
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3729..3747
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3741..3756
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3761..3773
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3768..3786
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3780..3795
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3800..3812
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3807..3825
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3819..3834
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3844..3856
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3851..3869
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3863..3880
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3885..3898
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3893..3911
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3905..3922
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3930..3942
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3937..3955
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3949..3964
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 3972..3981
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3977..3991
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4013..4023
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4019..4032
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4034..4049
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4383..4391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4385..4401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 4403..4412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 4527
FT /note="Y->C: Reduced interaction with ARH and dynein."
FT /evidence="ECO:0000269|PubMed:23836931"
FT STRAND 1190..1194
FT /evidence="ECO:0007829|PDB:2I1P"
FT STRAND 1196..1199
FT /evidence="ECO:0007829|PDB:2I1P"
FT HELIX 1204..1206
FT /evidence="ECO:0007829|PDB:2I1P"
FT STRAND 1207..1211
FT /evidence="ECO:0007829|PDB:2I1P"
FT STRAND 1214..1217
FT /evidence="ECO:0007829|PDB:2I1P"
FT HELIX 1218..1221
FT /evidence="ECO:0007829|PDB:2I1P"
SQ SEQUENCE 4660 AA; 519276 MW; E2A0CFD23D0923C3 CRC64;
MERGAAAAAW MLLLAIAACL EPVSSQECGS GNFRCDNGYC IPASWRCDGT RDCLDDTDEI
GCPPRSCESG LFLCPAEGTC IPSSWVCDED KDCSDGADEQ QNCAGTTCSA QQMTCSNGQC
IPSEYRCDHV SDCPDGSDER NCHYPTCDQL TCANGACYNT SQRCDQKVDC RDSSDEANCT
TLCSQKEFEC GSGECILRAY VCDHDNDCED NSDERNCNYD TCGGHQFTCS NGQCINQNWV
CDGDDDCQDS GDEDGCESNQ SHHRCYPREW ACPGSGRCIS IDKVCDGVPD CPEGDDENNV
TSGRTCGMGV CSVLNCEYQC HQTPFGGECF CPPGHIINSN DSRTCIDFDD CQIWGICDQK
CENRQGRHQC LCEEGYILER GQHCKSSDSF SAASVIFSNG RDLLVGDLHG RNFRILAESK
NRGMVMGVDF HYQKHRVFWT DPMQEKVFST DINGLNTQEI LNVSVDTPEN LAVDWINNKL
YLVETKVNRI DVVNLEGNQR VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA
FMDGSNRKDL VTTKVGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV
PHPFGISLFE EHVFFTDWTK MAVMKASKFT ETNPQVYHQS SLRPHGVTVY HALRQPNATN
PCGSNNGGCA QVCVLSHRTD NGGLGYRCKC EFGFELDDDE HRCVAVKNFL LFSSKTAVRG
IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ HSTVFYSDLS KDIIYKQKID GTGKEVITAN
RLESVECLTF DWISRNLYWT DGGLKSVTVL RLADKSRRQI ISNLNNPRSI VVHPTAGYMF
LSDWFRPAKI MRAWSDGSHL MPIVNTSLGW PNGLAIDWSA SRLYWVDAFF DKIEHSTLDG
LDRKRLGHVD QMTHPFGLTV FKDNVFITDW RLGAIIRVRK SDGGDMTVIR RGISSVMHVK
AYDADLQTGS NYCSQTTHAN GDCSHFCFPV PNFQRVCGCP YGMKLQRDQM TCEGDPAREP
PTQQCGSLSF PCNNGKCVPS FFRCDGVDDC HDNSDEHQCG VFNNTCSPSA FACVRGGQCI
PGQWHCDRQN DCLDGSDEQN CPTHATSSTC PSTSFTCDNH VCIPKDWVCD TDNDCSDGSD
EKNCQASGTC QPTQFRCPDH RCISPLYVCD GDKDCADGSD EAGCVLNCTS AQFKCADGSS
CINSRYRCDG VYDCRDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE CDGHPDCIHG
SDEHTGCVPK TCSPTHFLCD NGNCIYKAWI CDGDNDCRDM SDEKDCPTQP FHCPSTQWQC
PGYSTCINLS ALCDGVFDCP NGTDESPLCN QDSCSHFNGG CTHQCMQGPF GATCLCPLGY
QLANDTKTCE DINECDIPGF CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTGSENPLLV
VASRDKIIVD NITAHTHNLY SLVQDVSFVV ALDFDSVTGR VFWSDLLQGK TWSVFQNGTD
KRVVHDSGLS VTEMIAVDWI GRNLYWTDYA LETIEVSKID GSHRTVLISK NVTKPRGLAL
DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW PCGLSIDYPN RLIYFMDAYL
DYIEFCDYDG HNRRQVIASD LVLHHPHALT LFEDFVYWTD RGTRQVMQAN KWHGGNQSVV
MYSVHQPLGI TAIHPSRQPP SRNPCASASC SHLCLLSAQA PRHYSCACPS GWNLSDDSVN
CVRGDQPFLM SVRDNIIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG
EIHRVKTDGS NRTVFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT LKGDTRYGKT
LIANDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK IASANMDGTS LKILFTGNLQ
HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD GTERMILVHH LAHPWGLVVY GSFLYYSDEQ
YEVIERVDKS SGNNKVVLRD NVPYLRGLRV YHRRNAADSS NGCSNNPNAC QQICLPVPGG
MFSCACASGF KLSPDGRSCS PYNSFMVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH
ADVDVANGFI YWCDFSSSVR SSNGIRRIKP DGSNFTNVVT YGIGANGIRG VALDWAAGNL
YFTNAFVYET LIEVLRINTT YRRVLLKVSV DMPRHIIVDP KHRYLFWADY GQKPKIERSF
LDCTNRTVLV SEGIVTPRGL AMDHDTGYIY WVDDSLDLIA RIHLDGGESQ VVRYGSRYPT
PYGITVFGES IIWVDRNLKK VFQASKQPGN TDPPVVIRDK INLLRDVTIF DEHAQPLSPA
ELNNNPCLQS NGGCSHFCFA LPELPTPRCG CAFGTLGNDG KSCATSQEDF LIYSLNNSLR
SLHFDPRDHS LPFQVISVAG TAIALDYDRR NNRIFFTQKL NSLRGQISYV SLYSGSSSPT
VLLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN RAVIARVSKP RAIVLDPCRG
YMYWTDWGTN AKIERATLGG NFRVPIVNTS LVWPNGLALD LETDLLYWAD ASLQKIERST
LTGTNREVVV STAFHSFGLT VYGQYIYWTD LYTRKIYRAN KYDGSDLVAM TTRLPTQPSG
ISTVVKTQRQ QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGNWYLANDN KYCVVDTGTR
CNQLQFTCLN GHCINQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCG NGRCVPYHYR
CDYYNDCGDN SDEAGCLFRN CNSTTEFTCS NGRCIPLSYV CNGINNCHDN DTSDEKNCPP
HTCPPDFTKC QTTNICVPRA FLCDGDNDCG DGSDENPIYC ASHTCRSNEF QCLSPQRCIP
SYWFCDGEAD CADGSDEPDT CGHSVNTCRA SQFQCDNGRC ISGNWVCDGD NDCGDMSDED
QRHHCELQNC SSTQFTCVNS RPPNRRCIPQ YWVCDGDADC SDALDELQNC TMRTCSAGEF
SCANGRCVRQ SFRCDRRNDC GDYSDERGCS YPPCHANQFT CQNGRCIPRF FVCDEDNDCG
DGSDEQEHLC HTPEPTCPLH QFRCDNGHCI EMGRVCNHVD DCSDNSDEKG CGINECLDSS
ISRCDHNCTD TITSFYCSCL PGYKLMSDKR SCVDIDECKE SPQLCSQKCE NVVGSYICKC
APGYIREPDG KSCRQNSNIE PYLIFSNRYY IRNLTTDGSS YSLILQGLGN VVALDFDRVE
KRLYWIDAEK QIIERMFLNK TNRETIINHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD
LEGRHRKMIA QHCVDANNTF CFEHPRGIVL HPQRGHVYWA DWGVHAYIGR IGMDGTNKSV
IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH RHTVYDGSLP HPFALTIFED
TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT HKPFDIHVYH PYRQPIMSNP CGTNNGGCSH
LCLIKAGGRG FTCACPDDFQ TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC
SDGSDEPDLC PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCESNE
WQCANKRCIP QSWQCDSVND CLDNSDEDTS HCASRTCRPG QFKCNNGRCI PQSWKCDVDN
DCGDYSDEPI DECTTAAYNC DNHTEFSCKT NYRCIPQWAV CNGFDDCRDN SDEQGCESVP
CHPSGDFRCA NHHCIPLRWK CDGTDDCGDN SDEENCVPRE CSESEFRCAD QQCIPSRWVC
DQENDCGDNS DERDCEMKTC HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN
GTYCPAAMFE CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNIPCESPQR FRCDNSRCVY
GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCISQHYVCD NVNDCGDLSD
ETGCNLGDNR TCAENICEQN CTQLSSGGFI CSCRPGFKPS TSDKNSCQDI NECEEFGICP
QSCRNSKGSY ECFCVDGFKS MSTHYGERCA ADGSPPLLLL PENVRIRKYN TSSEKFSEYL
EEEEHIQTID YDWDPEHIGL SVVYYTVLAQ GSQFGAIKRA YIPNFESGSN NPIREVDLGL
KYLMQPDGLA VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL
MFWTDQGKQP KIESAWMNGE HRSVLVSENL GWPNGLSIDY LNDDRVYWSD SKEDVIEAIK
YDGTDRRLII NEAMKPFSLD IFEDKLYWVA KEKGEVWRQN KFGKENKEKV LVVNPWLTQV
RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG YSCACPQGSD FVTGSTVQCD AASELPVTMP
PPCRCMHGGN CYFDENELPK CKCSSGYSGE YCEVGLSRGI PPGTTMAVLL TFVIVIIVGA
LVLVGLFHYR KTGSLLPTLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI
IDRSMAMNEH FVMEVGKQPV IFENPMYAAK DNTSKVALAV QGPSTGAQVT VPENVENQNY
GRPIDPSEIV PEPKPASPGA DEIQGKKWNI FKRKPKQTTN FENPIYAEMD SEVKDAVAVA
PPPSPSLPAK ASKRNLTPGY TATEDTFKDT ANLVKEDSDV
