ID CTNB1_MOUSE Reviewed; 781 AA.
AC Q02248; Q922W1; Q9D335;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 01-MAY-2013, entry version 156.
DE RecName: Full=Catenin beta-1;
DE AltName: Full=Beta-catenin;
GN Name=Ctnnb1; Synonyms=Catnb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1509266; DOI=10.1126/science.257.5073.1142-a;
RA Butz S., Stappert J., Weissig H., Kemler R.;
RT "Plakoglobin and beta-catenin: distinct but closely related.";
RL Science 257:1142-1144(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6; TISSUE=Brain, and Mammary cancer;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
RA Butz S., Kemler R.;
RT "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
RT adhesion.";
RL FEBS Lett. 355:195-200(1994).
RN [5]
RP INTERACTION WITH TCF7; TCF7L1; TCF7L2 AND LEF1.
RX PubMed=9783587; DOI=10.1038/26989;
RA Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H.,
RA Moerer P., van de Wetering M., Destree O., Clevers H.;
RT "The Xenopus Wnt effector XTcf-3 interacts with Groucho-related
RT transcriptional repressors.";
RL Nature 395:608-612(1998).
RN [6]
RP INTERACTION WITH AXIN1.
RX PubMed=10581160; DOI=10.1006/bbrc.1999.1760;
RA Jho E., Lomvardas S., Costantini F.;
RT "A GSK3beta phosphorylation site in axin modulates interaction with
RT beta-catenin and Tcf-mediated gene expression.";
RL Biochem. Biophys. Res. Commun. 266:28-35(1999).
RN [7]
RP INTERACTION WITH BAIAP1.
RX PubMed=10772923; DOI=10.1006/bbrc.2000.2471;
RA Dobrosotskaya I.Y., James G.L.;
RT "MAGI-1 interacts with beta-catenin and is associated with cell-cell
RT adhesion structures.";
RL Biochem. Biophys. Res. Commun. 270:903-909(2000).
RN [8]
RP INTERACTION WITH CTNNA3.
RX PubMed=11590244;
RA Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J.,
RA Colpaert C., Bruyneel E., Mareel M., van Roy F.;
RT "AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein
RT mediating strong cell-cell adhesion.";
RL J. Cell Sci. 114:3177-3188(2001).
RN [9]
RP INTERACTION WITH TAX1BP3.
RX PubMed=12874278; DOI=10.1074/jbc.M306324200;
RA Kanamori M., Sandy P., Marzinotto S., Benetti R., Kai C.,
RA Hayashizaki Y., Schneider C., Suzuki H.;
RT "The PDZ protein tax-interacting protein-1 inhibits beta-catenin
RT transcriptional activity and growth of colorectal cancer cells.";
RL J. Biol. Chem. 278:38758-38764(2003).
RN [10]
RP PHOSPHORYLATION AT TYR-142 BY FYN.
RX PubMed=12640114; DOI=10.1128/MCB.23.7.2287-2297.2003;
RA Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N.,
RA Garcia de Herreros A., Dunach M.;
RT "p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-
RT catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin
RT Interaction.";
RL Mol. Cell. Biol. 23:2287-2297(2003).
RN [11]
RP INTERACTION WITH AXIN1.
RX PubMed=15063782; DOI=10.1016/j.bbrc.2004.03.065;
RA Kim S.I., Park C.S., Lee M.S., Kwon M.S., Jho E.H., Song W.K.;
RT "Cyclin-dependent kinase 2 regulates the interaction of Axin with
RT beta-catenin.";
RL Biochem. Biophys. Res. Commun. 317:478-483(2004).
RN [12]
RP RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND LACK OF
RP ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=16325582; DOI=10.1016/j.cell.2005.09.020;
RA Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.;
RT "Deconstructing the cadherin-catenin-actin complex.";
RL Cell 123:889-901(2005).
RN [13]
RP INTERACTION WITH GLIS2, AND SUBCELLULAR LOCATION.
RX PubMed=17289029; DOI=10.1016/j.febslet.2007.01.058;
RA Kim Y.-S., Kang H.S., Jetten A.M.;
RT "The Kruppel-like zinc finger protein Glis2 functions as a negative
RT modulator of the Wnt/beta-catenin signaling pathway.";
RL FEBS Lett. 581:858-864(2007).
RN [14]
RP INTERACTION WITH XIRP1.
RX PubMed=17925400; DOI=10.1074/jbc.M707639200;
RA Choi S., Gustafson-Wagner E.A., Wang Q., Harlan S.M., Sinn H.W.,
RA Lin J.L.-C., Lin J.J.-C.;
RT "The intercalated disc protein, mXin{alpha}, is capable of interacting
RT with beta-catenin and bundling actin filaments.";
RL J. Biol. Chem. 282:36024-36036(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551 AND THR-556, AND
RP MASS SPECTROMETRY.
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in
RT naive and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [16]
RP INTERACTION WITH SLC30A9.
RX PubMed=17344318; DOI=10.1093/nar/gkm095;
RA Chen Y.H., Yang C.K., Xia M., Ou C.Y., Stallcup M.R.;
RT "Role of GAC63 in transcriptional activation mediated by beta-
RT catenin.";
RL Nucleic Acids Res. 35:2084-2092(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551; SER-552 AND
RP THR-556, AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-654, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND SER-675, AND
RP MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=19367708; DOI=10.1021/pr800599n;
RA Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA Faessler R., Mann M.;
RT "Solid tumor proteome and phosphoproteome analysis by high resolution
RT mass spectrometry.";
RL J. Proteome Res. 7:5314-5326(2008).
RN [20]
RP LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=18093941; DOI=10.1073/pnas.0710504105;
RA Abe K., Takeichi M.;
RT "EPLIN mediates linkage of the cadherin catenin complex to F-actin and
RT stabilizes the circumferential actin belt.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008).
RN [21]
RP INTERACTION WITH TCF7L2 AND TNIK.
RX PubMed=19816403; DOI=10.1038/emboj.2009.285;
RA Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J.,
RA Mohammed S., Heck A.J., Clevers H.;
RT "The kinase TNIK is an essential activator of Wnt target genes.";
RL EMBO J. 28:3329-3340(2009).
RN [22]
RP INTERACTION WITH SCRIB.
RX PubMed=19458197; DOI=10.1091/mbc.E08-12-1172;
RA Sun Y., Aiga M., Yoshida E., Humbert P.O., Bamji S.X.;
RT "Scribble interacts with beta-catenin to localize synaptic vesicles to
RT synapses.";
RL Mol. Biol. Cell 20:3390-3400(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of
RT electron capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [24]
RP PHOSPHORYLATION AT SER-33 AND SER-37 BY HIPK2, AND MUTAGENESIS OF
RP SER-33 AND SER-37.
RX PubMed=20307497; DOI=10.1016/j.bbrc.2010.03.099;
RA Kim E.-A., Kim J.E., Sung K.S., Choi D.W., Lee B.J., Choi C.Y.;
RT "Homeodomain-interacting protein kinase 2 (HIPK2) targets beta-catenin
RT for phosphorylation and proteasomal degradation.";
RL Biochem. Biophys. Res. Commun. 394:966-971(2010).
RN [25]
RP PHOSPHORYLATION AT SER-552, AND MUTAGENESIS OF SER-552.
RX PubMed=20361929; DOI=10.1016/j.bbrc.2010.03.161;
RA Zhao J., Yue W., Zhu M.J., Sreejayan N., Du M.;
RT "AMP-activated protein kinase (AMPK) cross-talks with canonical Wnt
RT signaling via phosphorylation of beta-catenin at Ser 552.";
RL Biochem. Biophys. Res. Commun. 395:146-151(2010).
RN [26]
RP INTERACTION WITH TRPV4 AND CDH1.
RX PubMed=20413591; DOI=10.1074/jbc.M110.103606;
RA Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.;
RT "The TRPV4 channel contributes to intercellular junction formation in
RT keratinocytes.";
RL J. Biol. Chem. 285:18749-18758(2010).
RN [27]
RP INTERACTION WITH VCL, AND MUTAGENESIS OF MET-8.
RX PubMed=20086044; DOI=10.1242/jcs.056432;
RA Peng X., Cuff L.E., Lawton C.D., DeMali K.A.;
RT "Vinculin regulates cell-surface E-cadherin expression by binding to
RT beta-catenin.";
RL J. Cell Sci. 123:567-577(2010).
RN [28]
RP REVIEW.
RX PubMed=10679188; DOI=10.1006/bbrc.1999.1860;
RA Kikuchi A.;
RT "Regulation of beta-catenin signaling in the Wnt pathway.";
RL Biochem. Biophys. Res. Commun. 268:243-248(2000).
RN [29]
RP S-NITROSYLATION AT CYS-619, AND SUBCELLULAR LOCATION.
RX PubMed=20705246; DOI=10.1016/j.molcel.2010.07.013;
RA Thibeault S., Rautureau Y., Oubaha M., Faubert D., Wilkes B.C.,
RA Delisle C., Gratton J.P.;
RT "S-nitrosylation of beta-catenin by eNOS-derived NO promotes VEGF-
RT induced endothelial cell permeability.";
RL Mol. Cell 39:468-476(2010).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 150-665.
RX PubMed=9298899; DOI=10.1016/S0092-8674(00)80352-9;
RA Huber A.H., Nelson W.J., Weis W.I.;
RT "Three-dimensional structure of the armadillo repeat region of beta-
RT catenin.";
RL Cell 90:871-882(1997).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 118-149 IN COMPLEX WITH
RP CTNNA1.
RX PubMed=10882138; DOI=10.1016/S1097-2765(00)80447-5;
RA Pokutta S., Weis W.I.;
RT "Structure of the dimerization and beta-catenin-binding region of
RT alpha-catenin.";
RL Mol. Cell 5:533-543(2000).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.0 AND 3.0 ANGSTROMS) OF 134-671 IN COMPLEX
RP WITH PHOSPHORYLATED AND UNPHOSPHORYLATED CDH1.
RX PubMed=11348595; DOI=10.1016/S0092-8674(01)00330-0;
RA Huber A.H., Weis W.I.;
RT "The structure of the beta-catenin/E-cadherin complex and the
RT molecular basis of diverse ligand recognition by beta-catenin.";
RL Cell 105:391-402(2001).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH APC.
RX PubMed=11707392; DOI=10.1093/emboj/20.22.6203;
RA Eklof Spink K., Fridman S.G., Weis W.I.;
RT "Molecular mechanisms of beta-catenin recognition by adenomatous
RT polyposis coli revealed by the structure of an APC-beta-catenin
RT complex.";
RL EMBO J. 20:6203-6212(2001).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH
RP CTNNBIP1, AND INTERACTION WITH EP300.
RX PubMed=12408825; DOI=10.1016/S1097-2765(02)00631-7;
RA Daniels D.L., Weis W.I.;
RT "ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription
RT factors and the general coactivator p300 using independent structural
RT modules.";
RL Mol. Cell 10:573-584(2002).
CC -!- FUNCTION: Key downstream component of the canonical Wnt signaling
CC pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2,
CC APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal
CC Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its
CC subsequent degradation by the proteasome. In the presence of Wnt
CC ligand, CTNNB1 is not ubiquitinated and accumulates in the
CC nucleus, where it acts as a coactivator for transcription factors
CC of the TCF/LEF family, leading to activate Wnt responsive genes.
CC Involved in the regulation of cell adhesion. Acts as a negative
CC regulator of centrosome cohesion. Involved in the
CC CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization.
CC Blocks anoikis of malignant kidney and intestinal epithelial cells
CC and promotes their anchorage-independent growth by down-regulating
CC DAPK2 (By similarity). Disrupts PML function and PML-NB formation
CC by inhibiting RANBP2-mediated sumoylation of PML (By similarity).
CC -!- SUBUNIT: Two separate complex-associated pools are found in the
CC cytoplasm. The majority is present as component of an E-cadherin/
CC catenin adhesion complex composed of at least E-cadherin/CDH1 and
CC beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the
CC complex is located to adherens junctions. The stable association
CC of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-
CC actin when assembled in the complex. Alternatively, the CTNNA1-
CC containing complex may be linked to F-actin by other proteins such
CC as LIMA1. Binds SLC9A3R1 (By similarity). Interacts with PTPRU
CC (via the cytoplasmic juxtamembrane domain) and with EMD (By
CC similarity). Interacts with SESTD1 and TRPC4 (By similarity).
CC Interacts with CAV1. Interacts with PTPRJ (By similarity).
CC Interacts with PKT7 (By similarity). Interacts with FAT1 (via the
CC cytoplasmic domain) (By similarity). Interacts with CDK2, NDRG2
CC and NANOS1 (By similarity). Interacts with NEK2 and CDK5 (By
CC similarity). Interacts with CARM1, CXADR, PCDH11Y and PTK6 (By
CC similarity). Interacts with SOX7; this interaction may lead to
CC proteasomal degradation of active CTNNB1 and thus inhibition of
CC Wnt/beta-catenin-stimulated transcription. Identified in a complex
CC with HINT1 and MITF. Interacts with FHIT (By similarity). Another
CC cytoplasmic pool is part of a large complex containing AXIN1,
CC AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-
CC terminal Ser and Thr residues and ubiquitination of CTNNB1 via
CC BTRC and its subsequent degradation by the proteasome. Wnt-
CC dependent activation of DVL antagonizes the action of GSK3B. When
CC GSK3B activity is inhibited the complex dissociates, CTNNB1 is
CC dephosphorylated and is no longer targeted for destruction. The
CC stabilized protein translocates to the nucleus, where it binds
CC TCF/LEF-1 family members, TBP, BCL9 and possibly also RUVBL1 and
CC CHD8. Binds CTNNBIP and EP300. CTNNB1 forms a ternary complex with
CC LEF1 and EP300 that is disrupted by CTNNBIP1 binding. Interacts
CC with TAX1BP3 (via the PDZ domain); this interaction inhibits the
CC transcriptional activity of CTNNB1. Interacts with AJAP1, BAIAP1
CC and CTNNA3. Interacts with GLIS2. Interacts with XIRP1. Interacts
CC with SCRIB. Interacts with TNIK and TCF7L2. Interacts with
CC SLC30A9. Interacts directly with AXIN1; the interaction is
CC regulated by CDK2 phosphorylation of AXIN1. Interacts with TRPV4;
CC the TRPV4 and CTNNB1 complex can interact with CDH1. Interacts
CC with VCL. The CTNNB1 and TCF4 complex interacts with PML (By
CC similarity).
CC -!- INTERACTION:
CC P25054:APC (xeno); NbExp=8; IntAct=EBI-397872, EBI-727707;
CC O15169:AXIN1 (xeno); NbExp=5; IntAct=EBI-397872, EBI-710484;
CC P09803:Cdh1; NbExp=13; IntAct=EBI-397872, EBI-984420;
CC P45481:Crebbp; NbExp=2; IntAct=EBI-397872, EBI-296306;
CC P26231:Ctnna1; NbExp=2; IntAct=EBI-397872, EBI-647895;
CC Q9NSA3:CTNNBIP1 (xeno); NbExp=7; IntAct=EBI-397872, EBI-747082;
CC P27782:Lef1; NbExp=6; IntAct=EBI-397872, EBI-984464;
CC P97458:Prop1; NbExp=2; IntAct=EBI-397872, EBI-937831;
CC Q9DBG9:Tax1bp3; NbExp=6; IntAct=EBI-397872, EBI-1161647;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus.
CC Cell junction, adherens junction. Cell membrane (By similarity).
CC Cytoplasm, cytoskeleton, centrosome (By similarity). Cytoplasm,
CC cytoskeleton, spindle pole (By similarity). Note=Cytoplasmic when
CC it is unstabilized (high level of phosphorylation) or bound to
CC CDH1. Translocates to the nucleus when it is stabilized (low level
CC of phosphorylation). Interaction with GLIS2 promotes nuclear
CC translocation. Interaction with EMD inhibits nuclear localization.
CC The majority of beta-catenin is localized to the cell membrane. In
CC interphase, colocalizes with CROCC between CEP250 puncta at the
CC proximal end of centrioles, and this localization is dependent on
CC CROCC and CEP250. In mitosis, when NEK2 activity increases, it
CC localizes to centrosomes at spindle poles independent of CROCC.
CC Co-localizes with CDK5 in the cell-cell contacts and plasma
CC membrane of undifferentiated and differentiated neuroblastoma
CC cells (By similarity).
CC -!- PTM: Phosphorylation by GSK3B requires prior phosphorylation of
CC Ser-45 by another kinase. Phosphorylation proceeds then from Thr-
CC 41 to Ser-33. Phosphorylated by NEK2. EGF stimulates tyrosine
CC phosphorylation. Phosphorylation on Tyr-654 decreases CDH1 binding
CC and enhances TBP binding (By similarity). Phosphorylated on Ser-33
CC and Ser-37 by HIPK2. This phosphorylation triggers proteasomal
CC degradation. Phosphorylation at Ser-552 by AMPK promotes
CC stabilizion of the protein, enhancing TCF/LEF-mediated
CC transcription. Phosphorylation on Ser-191 and Ser-246 by CDK5.
CC Phosphorylation by CDK2 regulates insulin internalization (By
CC similarity). Phosphorylation by PTK6 at Tyr-64, Tyr-142, Tyr-331
CC and/or Tyr-333 with the predominant site at Tyr-64 is not
CC essential for inhibition of transcriptional activity (By
CC similarity).
CC -!- PTM: Ubiquitinated by the SCF(BTRC) E3 ligase complex when
CC phosphorylated by GSK3B, leading to its degradation. Ubiquitinated
CC by a E3 ubiquitin ligase complex containing UBE2D1, SIAH1,
CC CACYBP/SIP, SKP1, APC and TBL1X, leading to its subsequent
CC proteasomal degradation (By similarity).
CC -!- PTM: S-nitrosylation at Cys-619 within adherens junctions promotes
CC VEGF-induced, NO-dependent endothelial cell permeability by
CC disrupting interaction with E-cadherin, thus mediating disassembly
CC adherens junctions.
CC -!- SIMILARITY: Belongs to the beta-catenin family.
CC -!- SIMILARITY: Contains 12 ARM repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06739.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; M90364; AAA37280.1; -; mRNA.
DR EMBL; AK035311; BAC29027.1; -; mRNA.
DR EMBL; AK018515; BAB31250.1; -; mRNA.
DR EMBL; BC006739; AAH06739.1; ALT_INIT; mRNA.
DR EMBL; BC048153; AAH48153.1; -; mRNA.
DR EMBL; BC053065; AAH53065.1; -; mRNA.
DR IPI; IPI00125899; -.
DR PIR; S35091; S35091.
DR RefSeq; NP_001159374.1; NM_001165902.1.
DR RefSeq; NP_031640.1; NM_007614.3.
DR UniGene; Mm.291928; -.
DR PDB; 1DOW; X-ray; 1.80 A; B=118-149.
DR PDB; 1I7W; X-ray; 2.00 A; A/C=134-671.
DR PDB; 1I7X; X-ray; 3.00 A; A/C=134-671.
DR PDB; 1JPP; X-ray; 3.10 A; A/B=134-671.
DR PDB; 1M1E; X-ray; 2.10 A; A=134-671.
DR PDB; 1V18; X-ray; 2.10 A; A=134-671.
DR PDB; 2BCT; X-ray; 2.90 A; A=150-665.
DR PDB; 3BCT; X-ray; 2.10 A; A=193-662.
DR PDB; 3OUW; X-ray; 2.91 A; A=134-671.
DR PDB; 3OUX; X-ray; 2.40 A; A=134-671.
DR PDBsum; 1DOW; -.
DR PDBsum; 1I7W; -.
DR PDBsum; 1I7X; -.
DR PDBsum; 1JPP; -.
DR PDBsum; 1M1E; -.
DR PDBsum; 1V18; -.
DR PDBsum; 2BCT; -.
DR PDBsum; 3BCT; -.
DR PDBsum; 3OUW; -.
DR PDBsum; 3OUX; -.
DR DisProt; DP00341; -.
DR ProteinModelPortal; Q02248; -.
DR SMR; Q02248; 19-44, 99-665.
DR DIP; DIP-31560N; -.
DR IntAct; Q02248; 38.
DR MINT; MINT-103426; -.
DR PhosphoSite; Q02248; -.
DR PaxDb; Q02248; -.
DR PRIDE; Q02248; -.
DR Ensembl; ENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932.
DR Ensembl; ENSMUST00000178812; ENSMUSP00000136294; ENSMUSG00000006932.
DR GeneID; 12387; -.
DR KEGG; mmu:12387; -.
DR UCSC; uc009scu.2; mouse.
DR CTD; 1499; -.
DR MGI; MGI:88276; Ctnnb1.
DR eggNOG; NOG297695; -.
DR GeneTree; ENSGT00680000099702; -.
DR HOGENOM; HOG000230958; -.
DR HOVERGEN; HBG000919; -.
DR InParanoid; Q02248; -.
DR KO; K02105; -.
DR OMA; QLSQTRS; -.
DR OrthoDB; EOG4FN4H2; -.
DR ChiTaRS; CTNNB1; mouse.
DR EvolutionaryTrace; Q02248; -.
DR NextBio; 281106; -.
DR PMAP-CutDB; Q02248; -.
DR ArrayExpress; Q02248; -.
DR Bgee; Q02248; -.
DR CleanEx; MM_CTNNB1; -.
DR Genevestigator; Q02248; -.
DR GermOnline; ENSMUSG00000006932; Mus musculus.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
DR GO; GO:0070369; C:beta-catenin-TCF7L2 complex; ISS:UniProtKB.
DR GO; GO:0016342; C:catenin complex; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005924; C:cell-substrate adherens junction; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043198; C:dendritic shaft; IBA:RefGenome.
DR GO; GO:0030057; C:desmosome; IBA:RefGenome.
DR GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR GO; GO:0009898; C:internal side of plasma membrane; IBA:RefGenome.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0031528; C:microvillus membrane; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
DR GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IDA:BHF-UCL.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:RefGenome.
DR GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0005915; C:zonula adherens; IBA:RefGenome.
DR GO; GO:0045294; F:alpha-catenin binding; IDA:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; IBA:RefGenome.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR GO; GO:0005198; F:structural molecule activity; IBA:RefGenome.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:MGI.
DR GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0045453; P:bone resorption; IMP:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR GO; GO:0044336; P:canonical Wnt receptor signaling pathway involved in negative regulation of apoptotic process; IEA:Compara.
DR GO; GO:0061324; P:canonical Wnt receptor signaling pathway involved in positive regulation of cardiac outflow tract cell proliferation; IMP:BHF-UCL.
DR GO; GO:0044334; P:canonical Wnt receptor signaling pathway involved in positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; TAS:DFLAT.
DR GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR GO; GO:0048469; P:cell maturation; IDA:MGI.
DR GO; GO:0016337; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071681; P:cellular response to indole-3-methanol; ISS:UniProtKB.
DR GO; GO:0022009; P:central nervous system vasculogenesis; IMP:MGI.
DR GO; GO:0060982; P:coronary artery morphogenesis; TAS:DFLAT.
DR GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IBA:RefGenome.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:MGI.
DR GO; GO:0007398; P:ectoderm development; IMP:MGI.
DR GO; GO:0000578; P:embryonic axis specification; IDA:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:MGI.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IDA:MGI.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0036023; P:embryonic skeletal limb joint morphogenesis; IGI:BHF-UCL.
DR GO; GO:0001711; P:endodermal cell fate commitment; IMP:MGI.
DR GO; GO:0061154; P:endothelial tube morphogenesis; ISS:UniProtKB.
DR GO; GO:0060983; P:epicardium-derived cardiac vascular smooth muscle cell differentiation; TAS:DFLAT.
DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IMP:MGI.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0061198; P:fungiform papilla formation; IMP:MGI.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR GO; GO:0035112; P:genitalia morphogenesis; IMP:MGI.
DR GO; GO:0007403; P:glial cell fate determination; IDA:MGI.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR GO; GO:0060789; P:hair follicle placode formation; IMP:MGI.
DR GO; GO:0030902; P:hindbrain development; IBA:RefGenome.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0001889; P:liver development; IBA:RefGenome.
DR GO; GO:0060479; P:lung cell differentiation; IMP:MGI.
DR GO; GO:0060492; P:lung induction; IMP:MGI.
DR GO; GO:0060484; P:lung-associated mesenchyme development; IMP:MGI.
DR GO; GO:0030539; P:male genitalia development; IMP:MGI.
DR GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IMP:MGI.
DR GO; GO:0003337; P:mesenchymal to epithelial transition involved in metanephros morphogenesis; IDA:MGI.
DR GO; GO:0072132; P:mesenchyme morphogenesis; TAS:DFLAT.
DR GO; GO:0007494; P:midgut development; IEA:Compara.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Compara.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IGI:MGI.
DR GO; GO:0003136; P:negative regulation of heart induction by canonical Wnt receptor signaling pathway; IBA:RefGenome.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IMP:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR GO; GO:0072079; P:nephron tubule formation; IMP:MGI.
DR GO; GO:0001840; P:neural plate development; IDA:MGI.
DR GO; GO:0001764; P:neuron migration; IGI:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0048599; P:oocyte development; IGI:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
DR GO; GO:0060066; P:oviduct development; IMP:MGI.
DR GO; GO:0031016; P:pancreas development; IMP:MGI.
DR GO; GO:0001569; P:patterning of blood vessels; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0061047; P:positive regulation of branching involved in lung morphogenesis; IMP:MGI.
DR GO; GO:2000017; P:positive regulation of determination of dorsal identity; IDA:MGI.
DR GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IMP:MGI.
DR GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0010909; P:positive regulation of heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IGI:MGI.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IGI:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; IEA:Compara.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
DR GO; GO:0090279; P:regulation of calcium ion import; ISS:UniProtKB.
DR GO; GO:0030997; P:regulation of centriole-centriole cohesion; ISS:UniProtKB.
DR GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; IMP:BHF-UCL.
DR GO; GO:0031641; P:regulation of myelination; IMP:MGI.
DR GO; GO:0072182; P:regulation of nephron tubule epithelial cell differentiation; IMP:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0003266; P:regulation of secondary heart field cardioblast proliferation; IDA:MGI.
DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0042129; P:regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0072053; P:renal inner medulla development; IMP:MGI.
DR GO; GO:0072054; P:renal outer medulla development; IMP:MGI.
DR GO; GO:0072033; P:renal vesicle formation; IMP:MGI.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Compara.
DR GO; GO:0034097; P:response to cytokine stimulus; IEA:Compara.
DR GO; GO:0042493; P:response to drug; IEA:Compara.
DR GO; GO:0032355; P:response to estradiol stimulus; ISS:UniProtKB.
DR GO; GO:0014010; P:Schwann cell proliferation; IBA:RefGenome.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
DR GO; GO:0060440; P:trachea formation; IMP:MGI.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; TAS:DFLAT.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR013284; Beta-catenin.
DR Pfam; PF00514; Arm; 4.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 12.
DR SUPFAM; SSF48371; ARM-type_fold; 1.
DR PROSITE; PS50176; ARM_REPEAT; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cell adhesion; Cell junction; Cell membrane;
KW Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; S-nitrosylation;
KW Transcription; Transcription regulation; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1 781 Catenin beta-1.
FT /FTId=PRO_0000064272.
FT REPEAT 151 191 ARM 1.
FT REPEAT 193 234 ARM 2.
FT REPEAT 235 276 ARM 3.
FT REPEAT 277 318 ARM 4.
FT REPEAT 319 360 ARM 5.
FT REPEAT 361 389 ARM 6.
FT REPEAT 400 441 ARM 7.
FT REPEAT 442 484 ARM 8.
FT REPEAT 489 530 ARM 9.
FT REPEAT 531 571 ARM 10.
FT REPEAT 594 636 ARM 11.
FT REPEAT 637 666 ARM 12.
FT REGION 1 23 Interaction with VCL.
FT REGION 772 781 Interaction with SCRIB.
FT MOD_RES 23 23 Phosphoserine; by GSK3-beta (By
FT similarity).
FT MOD_RES 29 29 Phosphoserine; by GSK3-beta (By
FT similarity).
FT MOD_RES 33 33 Phosphoserine; by GSK3-beta and HIPK2.
FT MOD_RES 37 37 Phosphoserine; by GSK3-beta and HIPK2.
FT MOD_RES 41 41 Phosphothreonine; by GSK3-beta (By
FT similarity).
FT MOD_RES 45 45 Phosphoserine (By similarity).
FT MOD_RES 64 64 Phosphotyrosine; by PTK6 (By similarity).
FT MOD_RES 86 86 Phosphotyrosine; by CSK (By similarity).
FT MOD_RES 142 142 Phosphotyrosine; by FYN and PTK6.
FT MOD_RES 191 191 Phosphoserine; by CDK5 (By similarity).
FT MOD_RES 246 246 Phosphoserine; by CDK5 (By similarity).
FT MOD_RES 331 331 Phosphotyrosine (By similarity).
FT MOD_RES 551 551 Phosphothreonine.
FT MOD_RES 552 552 Phosphoserine; by AMPK.
FT MOD_RES 556 556 Phosphothreonine.
FT MOD_RES 619 619 S-nitrosocysteine.
FT MOD_RES 654 654 Phosphotyrosine.
FT MOD_RES 675 675 Phosphoserine.
FT MUTAGEN 8 8 M->P: Loss of interaction with VCL.
FT MUTAGEN 33 33 S->A: Abolished HIPK2-mediated
FT proteasomal degradation.
FT MUTAGEN 37 37 S->A: Abolished HIPK2-mediated
FT proteasomal degradation.
FT MUTAGEN 552 552 S->A: Abolishes AMPK-mediated
FT phosphorylation.
FT CONFLICT 371 371 T -> I (in Ref. 2; BAB31250).
FT CONFLICT 478 478 A -> T (in Ref. 2; BAB31250).
FT CONFLICT 487 487 L -> F (in Ref. 2; BAB31250).
FT HELIX 121 141
FT TURN 145 148
FT TURN 150 152
FT HELIX 153 160
FT STRAND 161 164
FT HELIX 165 180
FT HELIX 182 189
FT HELIX 192 204
FT HELIX 208 221
FT HELIX 225 233
FT HELIX 236 242
FT HELIX 243 245
FT HELIX 249 265
FT HELIX 269 275
FT HELIX 278 284
FT HELIX 285 287
FT HELIX 291 305
FT HELIX 309 317
FT HELIX 320 330
FT HELIX 334 347
FT HELIX 353 359
FT HELIX 362 367
FT TURN 368 371
FT HELIX 375 389
FT HELIX 399 408
FT HELIX 414 428
FT HELIX 432 440
FT HELIX 443 454
FT HELIX 458 471
FT STRAND 473 475
FT HELIX 478 487
FT HELIX 491 496
FT HELIX 504 517
FT HELIX 521 523
FT HELIX 524 529
FT HELIX 532 547
FT HELIX 566 580
FT HELIX 584 592
FT HELIX 596 602
FT HELIX 608 621
FT HELIX 625 632
FT TURN 633 636
FT HELIX 637 643
FT HELIX 649 661
SQ SEQUENCE 781 AA; 85471 MW; D708F170A3FBED6E CRC64;
MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTS
QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT
NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK
KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL
VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA
GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA
AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM
AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL
VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV
QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF
RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEALGYR QDDPSYRSFH
SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD
L
//
