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Database: UniProt
Entry: P98158
LinkDB: P98158
Original site: P98158 
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   13-FEB-2019, entry version 161.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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;
RA   Kerjaschki D., Farquhar M.G.;
RT   "The pathogenic antigen of Heymann nephritis is a membrane
RT   glycoprotein of 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;
RA   Kounnas M.Z., Argraves W.S., Strickland D.K.;
RT   "The 39-kDa receptor-associated protein interacts with two members of
RT   the low density lipoprotein receptor family, alpha 2-macroglobulin
RT   receptor and 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
RT   lipoprotein receptor gene family, gp330 and LRP/alpa 2MR, and the
RT   receptor-associated 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.,
RA   Norris K., 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
RT   tail of 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
RT   megalin 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.,
RA   Atrian S., Allen P.L., Hammond T.G.;
RT   "Megalin mediates renal uptake of heavy metal metallothionein
RT   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.,
RA   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.,
RA   Schulz H., Metzger J., Schweigert F.J., Luppa P.B., Nykjaer A.,
RA   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.,
RA   Baker C.B., 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;
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
RT   megalin-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
RT   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
RP   SPECIFICITY, 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
RT   the 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
RT   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
RP   AND SER-4658, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat 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
RT   regulate its 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.,
RA   Nielsen R., Christensen E.I., Courtoy P.J., Emonard H., Marbaix E.,
RA   Henriet P.;
RT   "Cellular uptake of proMMP-2:TIMP-2 complexes by the endocytic
RT   receptor megalin/LRP-2.";
RL   Sci. Rep. 7:4328-4328(2017).
RN   [24]
RP   STRUCTURE BY NMR OF 1185-1229, CALCIUM-BINDING SITE, AND DISULFIDE
RP   BONDS.
RX   PubMed=17245526; DOI=10.1007/s10858-006-9129-3;
RA   Wolf C.A., Dancea F., Shi M., Bade-Noskova V., Ruterjans H.,
RA   Kerjaschki D., Lucke C.;
RT   "Solution structure of the twelfth cysteine-rich ligand-binding repeat
RT   in 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
RP   ANKRA2, 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
RT   repeat tumbler lock.";
RL   Sci. Signal. 5:RA39-RA39(2012).
CC   -!- FUNCTION: Multiligand endocytic receptor. Acts together with CUBN
CC       to mediate endocytosis of high-density lipoproteins (By
CC       similarity). Mediates receptor-mediated uptake of polybasic drugs
CC       such as aprotinin, aminoglycosides and polymyxin B
CC       (PubMed:7544804, PubMed:19202329). In the kidney, mediates the
CC       tubular uptake and clearance of leptin (By similarity). Also
CC       mediates transport of leptin across the blood-brain barrier
CC       through endocytosis at the choroid plexus epithelium
CC       (PubMed:17324488). Endocytosis of leptin in neuronal cells is
CC       required for hypothalamic leptin signaling and leptin-mediated
CC       regulation of feeding and body weight (By similarity). Mediates
CC       endocytosis and subsequent lysosomal degradation of CST3 in kidney
CC       proximal tubule cells (PubMed:17462596). Mediates renal uptake of
CC       25-hydroxyvitamin D3 in complex with the vitamin D3 transporter
CC       GC/DBP (By similarity). Mediates renal uptake of metallothionein-
CC       bound heavy metals (PubMed:15126248). Together with CUBN, mediates
CC       renal reabsorption of myoglobin (PubMed:12724130). Mediates renal
CC       uptake and subsequent lysosomal degradation of APOM
CC       (PubMed:16099815). Plays a role in kidney selenium homeostasis by
CC       mediating renal endocytosis of selenoprotein SEPP1 (By
CC       similarity). Mediates renal uptake of the antiapoptotic protein
CC       BIRC5/survivin which may be important for functional integrity of
CC       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
CC       protein N-product (ShhN), the active product of SHH
CC       (PubMed:11964399, PubMed:16801528). Also mediates ShhN
CC       transcytosis (PubMed:16801528). In the embryonic neuroepithelium,
CC       mediates endocytic uptake and degradation of BMP4, is required for
CC       correct SHH localization in the ventral neural tube and plays a
CC       role in patterning of the ventral telencephalon (By similarity).
CC       Required at the onset of neurulation to sequester SHH on the
CC       apical surface of neuroepithelial cells of the rostral
CC       diencephalon ventral midline and to control PTCH1-dependent uptake
CC       and intracellular trafficking of SHH (By similarity). During
CC       neurulation, required in neuroepithelial cells for uptake of
CC       folate bound to the folate receptor FOLR1 which is necessary for
CC       neural tube closure (By similarity). In the adult brain,
CC       negatively regulates BMP signaling in the subependymal zone which
CC       enables neurogenesis to proceed (By similarity). In astrocytes,
CC       mediates endocytosis of ALB which is required for the synthesis of
CC       the neurotrophic factor oleic acid (PubMed:18466341). Involved in
CC       neurite branching (By similarity). During optic nerve development,
CC       required for SHH-mediated migration and proliferation of
CC       oligodendrocyte precursor cells (By similarity). Mediates
CC       endocytic uptake and clearance of SHH in the retinal margin which
CC       protects retinal progenitor cells from mitogenic stimuli and keeps
CC       them quiescent (By similarity). Plays a role in reproductive organ
CC       development by mediating uptake in reproductive tissues of
CC       androgen and estrogen bound to the sex hormone binding protein
CC       SHBG (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
CC       development (By similarity). Required for normal hearing, possibly
CC       through interaction with estrogen in the inner ear
CC       (PubMed:17846082). {ECO:0000250|UniProtKB:A2ARV4,
CC       ECO:0000250|UniProtKB:C0HL13, ECO:0000250|UniProtKB:P98164,
CC       ECO:0000269|PubMed:11964399, ECO:0000269|PubMed:12724130,
CC       ECO:0000269|PubMed:15126248, ECO:0000269|PubMed:15467006,
CC       ECO:0000269|PubMed:16099815, ECO:0000269|PubMed:16143106,
CC       ECO:0000269|PubMed:16380466, ECO:0000269|PubMed:16801528,
CC       ECO:0000269|PubMed:17324488, ECO:0000269|PubMed:17462596,
CC       ECO:0000269|PubMed:17846082, ECO:0000269|PubMed:18466341,
CC       ECO:0000269|PubMed:19202329, ECO:0000269|PubMed:28659595,
CC       ECO:0000269|PubMed:7544804}.
CC   -!- SUBUNIT: Binds plasminogen, extracellular matrix components,
CC       plasminogen activator-plasminogen activator inhibitor type I
CC       complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase,
CC       lactoferrin, CLU/clusterin and calcium. Forms a multimeric complex
CC       together with LRPAP1 (PubMed:1400426). Interacts (via PxLPxI/L
CC       motif) with ANKRA2 (via ankyrin repeats) (PubMed:22649097).
CC       Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the
CC       interaction is not affected by tyrosine phosphorylation of the
CC       NPXY motif (By similarity). Interacts with MB (PubMed:12724130).
CC       Interacts with BMP4 (By similarity). Interacts with the Sonic
CC       hedgehog protein N-product which is the active product of SHH (By
CC       similarity). Interacts with CST3 in a calcium-dependent manner
CC       (PubMed:17462596). Interacts with the vitamin-D binding protein
CC       GC/DBP (By similarity). Interacts with sex hormone-binding protein
CC       SHBG (PubMed:16143106). Interacts with angiotensin-2 (By
CC       similarity). Also interacts with angiotensin 1-7 (By similarity).
CC       Interacts with APOM (By similarity). Interacts with selenoprotein
CC       SEPP1 (By similarity). Interacts with LEP (PubMed:17324488).
CC       Interacts with ALB (PubMed:18466341). Interacts with the
CC       antiapoptotic protein BIRC5/survivin (By similarity). Interacts
CC       with matrix metalloproteinase MMP2 in complex with
CC       metalloproteinase inhibitor TIMP1 (PubMed:28659595). In neurons,
CC       forms a trimeric complex with APP and APPB1/FE65 (By similarity).
CC       Interacts with LDLRAP1/ARH; mediates trafficking of LRP2 to the
CC       endocytic recycling compartment (PubMed:23836931). Does not
CC       interact with beta-amyloid protein 40 alone but interacts with the
CC       complex composed of beta-amyloid protein 40 and CLU/APOJ (By
CC       similarity). {ECO:0000250|UniProtKB:A2ARV4,
CC       ECO:0000250|UniProtKB:C0HL13, ECO:0000250|UniProtKB:P98164,
CC       ECO:0000269|PubMed:12724130, ECO:0000269|PubMed:1400426,
CC       ECO:0000269|PubMed:15467006, ECO:0000269|PubMed:16143106,
CC       ECO:0000269|PubMed:17462596, ECO:0000269|PubMed:18466341,
CC       ECO:0000269|PubMed:22649097, ECO:0000269|PubMed:23836931,
CC       ECO:0000269|PubMed:28659595}.
CC   -!- INTERACTION:
CC       O88797:Dab2; NbExp=2; IntAct=EBI-6306650, EBI-6109302;
CC       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-
CC       pass 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
CC       endosomes as a soluble form (PubMed:17063000).
CC       {ECO:0000269|PubMed:12724130, ECO:0000269|PubMed:6752952}.
CC   -!- TISSUE SPECIFICITY: In the inner ear, expressed in the lumen of
CC       the endolymphatic sac where it localizes to macrophage-like cells
CC       as well as to mitochondria-rich and ribosome-rich epithelial cells
CC       (at protein level) (PubMed:17063000). In the inner ear, expressed
CC       in marginal cells of the stria vascularis, epithelial cells at the
CC       spiral prominence, epithelial cells of Reissner's membrane facing
CC       the cochlear duct, and Kolliker's organ (at protein level)
CC       (PubMed:19202329). Expressed in the choroid plexus epithelium in
CC       the brain (at protein level) (PubMed:17324488). In the brain, also
CC       expressed in astrocytes (at protein level) (PubMed:18466341).
CC       Expression also detected in epithelial cells of the kidney
CC       glomerulus and proximal tubule, lung, epididymis and yolk sac
CC       (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
CC       and gradually decreases from postnatal day 4 until the end of the
CC       first 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
CC       apical cell membrane. {ECO:0000269|PubMed:12519751}.
CC   -!- PTM: A fraction undergoes proteolytic cleavage of the
CC       extracellular domain at the cell membrane to generate a
CC       cytoplasmic tail fragment. This is internalized into the early
CC       endosome from where it trafficks in an LDLRAP1/ARH-dependent
CC       manner to the endocytic recycling compartment (ERC). In the ERC,
CC       it is further cleaved by gamma-secretase to release a fragment
CC       which translocates to the nucleus and mediates transcriptional
CC       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}.
DR   EMBL; L34049; AAA51369.1; -; mRNA.
DR   PIR; T42737; T42737.
DR   RefSeq; NP_110454.1; NM_030827.1.
DR   UniGene; Rn.26430; -.
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   ProteinModelPortal; P98158; -.
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; -.
DR   iPTMnet; P98158; -.
DR   PhosphoSitePlus; P98158; -.
DR   UniCarbKB; 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   eggNOG; ENOG410XP34; LUCA.
DR   HOGENOM; HOG000231853; -.
DR   HOVERGEN; HBG097941; -.
DR   InParanoid; P98158; -.
DR   KO; K06233; -.
DR   OrthoDB; 1606at2759; -.
DR   PhylomeDB; P98158; -.
DR   EvolutionaryTrace; P98158; -.
DR   PRO; PR:P98158; -.
DR   Proteomes; UP000002494; Unplaced.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
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: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:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0008144; F:drug binding; IDA:UniProtKB.
DR   GO; GO:0030492; F:hemoglobin binding; IDA:RGD.
DR   GO; GO:0042562; F:hormone binding; IPI:RGD.
DR   GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:RGD.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
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:0035258; F:steroid hormone receptor binding; IPI:UniProtKB.
DR   GO; GO:0007568; P:aging; IEP:RGD.
DR   GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR   GO; GO:0061642; P:chemoattraction of axon; IMP:RGD.
DR   GO; GO:0060982; P:coronary artery morphogenesis; ISS:UniProtKB.
DR   GO; GO:0020028; P:endocytic hemoglobin import; 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:0046879; P:hormone secretion; IMP:RGD.
DR   GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR   GO; GO:0030001; P:metal ion transport; IDA:UniProtKB.
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:0061156; P:pulmonary artery morphogenesis; ISS:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
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: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:0006766; P:vitamin metabolic process; TAS:RGD.
DR   CDD; cd00112; LDLa; 36.
DR   Gene3D; 2.120.10.30; -; 8.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; 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   Complete proteome; Disulfide bond; EGF-like domain; Endocytosis;
KW   Endosome; Glycoprotein; Hearing; Membrane; Metal-binding;
KW   Neurogenesis; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   SH3-binding; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26   4660       Low-density lipoprotein receptor-related
FT                                protein 2.
FT                                /FTId=PRO_0000017322.
FT   TOPO_DOM     26   4425       Extracellular. {ECO:0000255}.
FT   TRANSMEM   4426   4446       Helical. {ECO:0000255}.
FT   TOPO_DOM   4447   4660       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       27     63       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN       66    104       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      107    143       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      141    180       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      182    218       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      221    257       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      264    307       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      347    382       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT      435    477       LDL-receptor class B 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      478    520       LDL-receptor class B 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      521    567       LDL-receptor class B 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      568    612       LDL-receptor class B 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      752    794       LDL-receptor class B 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      795    836       LDL-receptor class B 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      837    880       LDL-receptor class B 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT      881    924       LDL-receptor class B 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   DOMAIN     1024   1060       LDL-receptor class A 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1065   1102       LDL-receptor class A 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1109   1145       LDL-receptor class A 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1149   1185       LDL-receptor class A 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1187   1224       LDL-receptor class A 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1230   1268       LDL-receptor class A 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1271   1307       LDL-receptor class A 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1312   1350       LDL-receptor class A 15.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1350   1390       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1391   1430       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT     1479   1521       LDL-receptor class B 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1522   1564       LDL-receptor class B 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1567   1610       LDL-receptor class B 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1611   1655       LDL-receptor class B 12.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1656   1696       LDL-receptor class B 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1791   1833       LDL-receptor class B 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1834   1883       LDL-receptor class B 15.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1884   1931       LDL-receptor class B 16.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1932   1973       LDL-receptor class B 17.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     1974   2014       LDL-receptor class B 18.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2108   2157       LDL-receptor class B 19.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2158   2202       LDL-receptor class B 20.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2203   2246       LDL-receptor class B 21.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2247   2290       LDL-receptor class B 22.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2432   2478       LDL-receptor class B 23.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2479   2519       LDL-receptor class B 24.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2520   2563       LDL-receptor class B 25.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2564   2605       LDL-receptor class B 26.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     2606   2647       LDL-receptor class B 27.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   DOMAIN     2700   2738       LDL-receptor class A 16.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2741   2777       LDL-receptor class A 17.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2780   2819       LDL-receptor class A 18.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2822   2861       LDL-receptor class A 19.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2864   2902       LDL-receptor class A 20.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2907   2946       LDL-receptor class A 21.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2949   2991       LDL-receptor class A 22.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     2994   3030       LDL-receptor class A 23.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3033   3071       LDL-receptor class A 24.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3076   3112       LDL-receptor class A 25.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3112   3153       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     3154   3194       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT     3241   3283       LDL-receptor class B 28.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     3284   3326       LDL-receptor class B 29.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     3335   3378       LDL-receptor class B 30.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     3379   3421       LDL-receptor class B 31.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     3422   3462       LDL-receptor class B 32.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   DOMAIN     3513   3551       LDL-receptor class A 26.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3554   3592       LDL-receptor class A 27.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3595   3633       LDL-receptor class A 28.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3636   3674       LDL-receptor class A 29.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3679   3717       LDL-receptor class A 30.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3720   3757       LDL-receptor class A 31.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3760   3796       LDL-receptor class A 32.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3799   3835       LDL-receptor class A 33.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3843   3881       LDL-receptor class A 34.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3884   3923       LDL-receptor class A 35.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3929   3965       LDL-receptor class A 36.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     3968   4003       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     4009   4050       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REPEAT     4156   4198       LDL-receptor class B 33.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     4199   4242       LDL-receptor class B 34.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   REPEAT     4244   4285       LDL-receptor class B 35.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00461}.
FT   DOMAIN     4379   4413       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REGION     4597   4610       Interaction with DAB2.
FT                                {ECO:0000250|UniProtKB:P98164}.
FT   MOTIF      4454   4463       SH3-binding. {ECO:0000255}.
FT   MOTIF      4457   4462       PxLPxI/L motif 1; mediates interaction
FT                                with ANKRA2.
FT                                {ECO:0000269|PubMed:22649097}.
FT   MOTIF      4460   4465       PxLPxI/L motif 2; mediates interaction
FT                                with ANKRA2.
FT                                {ECO:0000269|PubMed:22649097}.
FT   MOTIF      4522   4527       Endocytosis signal. {ECO:0000255}.
FT   MOTIF      4603   4606       NPXY motif.
FT   MOTIF      4606   4609       SH2-binding. {ECO:0000255}.
FT   MOTIF      4619   4630       SH3-binding. {ECO:0000255}.
FT   METAL      1127   1127       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1130   1130       Calcium. {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1132   1132       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1134   1134       Calcium. {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1140   1140       Calcium. {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1141   1141       Calcium. {ECO:0000250|UniProtKB:P98164}.
FT   METAL      1206   1206       Calcium; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:17245526}.
FT   METAL      1209   1209       Calcium. {ECO:0000269|PubMed:17245526}.
FT   METAL      1211   1211       Calcium; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:17245526}.
FT   METAL      1213   1213       Calcium. {ECO:0000269|PubMed:17245526}.
FT   METAL      1219   1219       Calcium. {ECO:0000269|PubMed:17245526}.
FT   METAL      1220   1220       Calcium. {ECO:0000269|PubMed:17245526}.
FT   MOD_RES    4464   4464       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    4467   4467       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:A2ARV4}.
FT   MOD_RES    4577   4577       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    4624   4624       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES    4637   4637       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:A2ARV4}.
FT   MOD_RES    4658   4658       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   CARBOHYD    159    159       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    178    178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    259    259       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    299    299       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    340    340       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    462    462       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    657    657       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    865    865       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1063   1063       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1187   1187       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1328   1328       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1341   1341       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1384   1384       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1451   1451       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1497   1497       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1551   1551       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1676   1676       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1733   1733       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1811   1811       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2134   2134       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2178   2178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2225   2225       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2396   2396       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2488   2488       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2548   2548       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2782   2782       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2810   2810       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2949   2949       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2989   2989       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3127   3127       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3213   3213       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3259   3259       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3317   3317       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3357   3357       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3448   3448       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3566   3566       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3682   3682       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3840   3840       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3969   3969       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3980   3980       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4070   4070       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4329   4329       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     28     40       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     35     53       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     47     62       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     67     80       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     74     93       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     87    103       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    108    120       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    115    133       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    127    142       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    142    157       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    152    170       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    164    179       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    183    195       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    190    208       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    202    217       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    222    234       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    229    247       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    241    256       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    265    278       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    272    291       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    285    306       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    351    361       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    357    370       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1025   1037       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1032   1050       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1044   1059       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1066   1079       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1073   1092       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1086   1101       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1110   1122       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1117   1135       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1129   1144       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1150   1162       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1157   1175       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1169   1184       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1188   1201       {ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:17245526}.
FT   DISULFID   1195   1214       {ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:17245526}.
FT   DISULFID   1208   1223       {ECO:0000255|PROSITE-ProRule:PRU00124,
FT                                ECO:0000269|PubMed:17245526}.
FT   DISULFID   1231   1244       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1238   1257       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1251   1267       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1272   1284       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1279   1297       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1291   1306       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1313   1326       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1320   1339       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1333   1349       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1354   1365       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1361   1374       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1376   1389       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1395   1405       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1401   1414       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1416   1429       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2701   2713       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2708   2726       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2720   2737       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2742   2754       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2749   2767       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2761   2776       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2781   2794       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2789   2807       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2801   2818       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2823   2836       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2830   2849       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2843   2860       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2865   2878       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2872   2891       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2885   2901       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2908   2920       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2915   2933       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2927   2945       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2950   2967       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2957   2980       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2974   2990       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   2995   3007       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3002   3020       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3014   3029       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3034   3046       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3041   3059       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3053   3070       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3077   3089       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3084   3102       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3096   3111       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3116   3128       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3124   3137       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3139   3152       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3158   3169       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3165   3178       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3180   3193       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3514   3527       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3521   3540       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3534   3550       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3555   3567       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3562   3580       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3574   3591       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3596   3608       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3603   3621       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3615   3632       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3637   3649       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3644   3662       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3656   3673       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3680   3694       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3688   3707       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3701   3716       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3721   3734       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3729   3747       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3741   3756       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3761   3773       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3768   3786       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3780   3795       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3800   3812       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3807   3825       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3819   3834       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3844   3856       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3851   3869       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3863   3880       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3885   3898       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3893   3911       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3905   3922       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3930   3942       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3937   3955       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3949   3964       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   3972   3981       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3977   3991       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4013   4023       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4019   4032       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4034   4049       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4383   4391       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4385   4401       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   4403   4412       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   MUTAGEN    4527   4527       Y->C: Reduced interaction with ARH and
FT                                dynein. {ECO:0000269|PubMed:23836931}.
FT   STRAND     1190   1194       {ECO:0000244|PDB:2I1P}.
FT   STRAND     1196   1199       {ECO:0000244|PDB:2I1P}.
FT   HELIX      1204   1206       {ECO:0000244|PDB:2I1P}.
FT   STRAND     1207   1211       {ECO:0000244|PDB:2I1P}.
FT   STRAND     1214   1217       {ECO:0000244|PDB:2I1P}.
FT   HELIX      1218   1221       {ECO:0000244|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
//
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