ID ERBIN_HUMAN Reviewed; 1412 AA. AC Q96RT1; A0AVR1; B4E3F1; B7ZLV9; E7EQW9; E9PCR8; Q1RMD0; Q86W38; Q9NR18; AC Q9NW48; Q9ULJ5; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 210. DE RecName: Full=Erbin {ECO:0000303|PubMed:10878805}; DE AltName: Full=Densin-180-like protein; DE AltName: Full=Erbb2-interacting protein {ECO:0000303|PubMed:10878805}; DE AltName: Full=Protein LAP2; GN Name=ERBIN {ECO:0000303|PubMed:10878805}; GN Synonyms=ERBB2IP {ECO:0000303|PubMed:10878805}, KIAA1225 GN {ECO:0000312|EMBL:BAA86539.2}, LAP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH ERBB2, TISSUE RP SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION. RC TISSUE=B-cell; RX PubMed=10878805; DOI=10.1038/35017038; RA Borg J.-P., Marchetto S., Le Bivic A., Ollendorff V., Jaulin-Bastard F., RA Saito H., Fournier E., Adelaide J., Margolis B., Birnbaum D.; RT "ERBIN: a basolateral PDZ protein that interacts with the mammalian RT ERBB2/HER2 receptor."; RL Nat. Cell Biol. 2:407-414(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7), INTERACTION RP WITH BPAG1; DST AND ITGB4, SUBCELLULAR LOCATION, AND VARIANT GLU-1207. RX PubMed=11375975; DOI=10.1074/jbc.m011005200; RA Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F., Saurat J.-H., RA Sonnenberg A., Borradori L.; RT "The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin RT beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative RT splice variants of ERBIN and analysis of their tissue expression."; RL J. Biol. Chem. 276:32427-32436(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=10574462; DOI=10.1093/dnares/6.5.337; RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:337-345(1999). RN [4] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 601-1206 (ISOFORM 1). RC TISSUE=Teratocarcinoma, and Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 8 AND 9), AND VARIANTS RP LEU-274 AND VAL-313. RC TISSUE=Cerebellum, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP INTERACTION WITH DELTA CATENIN AND ARVCF. RX PubMed=11821434; DOI=10.1074/jbc.m200818200; RA Laura R.P., Witt A.S., Held H.A., Gerstner R., Deshayes K., Koehler M.F.T., RA Kosik K.S., Sidhu S.S., Lasky L.A.; RT "The Erbin PDZ domain binds with high affinity and specificity to the RT carboxyl termini of delta-catenin and ARVCF."; RL J. Biol. Chem. 277:12906-12914(2002). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-920, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [10] RP FUNCTION, INTERACTION WITH NOD2, SUBCELLULAR LOCATION, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RX PubMed=16203728; DOI=10.1074/jbc.m508538200; RA McDonald C., Chen F.F., Ollendorff V., Ogura Y., Marchetto S., Lecine P., RA Borg J.P., Nunez G.; RT "A role for Erbin in the regulation of Nod2-dependent NF-kappaB RT signaling."; RL J. Biol. Chem. 280:40301-40309(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-972, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-857; THR-917 AND RP SER-1286, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872; THR-917; SER-931 AND RP SER-1158, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-602 AND SER-603, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485; SER-620; SER-872; RP SER-1158 AND SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485 AND SER-852, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1321-1412 IN COMPLEX WITH ERBB2 RP C-TERMINUS. RX PubMed=12444095; DOI=10.1074/jbc.c200571200; RA Birrane G., Chung J., Ladias J.A.; RT "Novel mode of ligand recognition by the Erbin PDZ domain."; RL J. Biol. Chem. 278:1399-1402(2003). RN [22] RP STRUCTURE BY NMR OF 1314-1412 IN COMPLEX WITH PHAGE-DERIVED PEPTIDE. RX PubMed=12446668; DOI=10.1074/jbc.m209751200; RA Skelton N.J., Koehler M.F.T., Zobel K., Wong W.L., Yeh S., Pisabarro M.T., RA Yin J.P., Lasky L.A., Sidhu S.S.; RT "Origins of PDZ domain ligand specificity. Structure determination and RT mutagenesis of the Erbin PDZ domain."; RL J. Biol. Chem. 278:7645-7654(2003). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 1314-1412. RX PubMed=16737969; DOI=10.1074/jbc.m602901200; RA Appleton B.A., Zhang Y., Wu P., Yin J.P., Hunziker W., Skelton N.J., RA Sidhu S.S., Wiesmann C.; RT "Comparative structural analysis of the erbin PDZ domain and the first PDZ RT domain of ZO-1. Insights into determinants of PDZ domain specificity."; RL J. Biol. Chem. 281:22312-22320(2006). CC -!- FUNCTION: Acts as an adapter for the receptor ERBB2, in epithelia. By CC binding the unphosphorylated 'Tyr-1248' of receptor ERBB2, it may CC contribute to stabilize this unphosphorylated state (PubMed:16203728). CC Inhibits NOD2-dependent NF-kappa-B signaling and pro-inflammatory CC cytokine secretion (PubMed:16203728). {ECO:0000269|PubMed:10878805, CC ECO:0000269|PubMed:16203728}. CC -!- SUBUNIT: Interacts with ERBB2, BPAG1 and ITGB4 (PubMed:10878805, CC PubMed:11375975, PubMed:12444095). May favor the localization of ERBB2, CC by restricting its presence to the basolateral membrane of epithelial CC cells. Also found to interact with ARVCF and delta catenin CC (PubMed:11821434). Interacts (via C-terminus) with DST Isoform 3 (via CC N-terminus) (PubMed:11375975). Interacts with NOD2 (via CARD domain) CC (PubMed:16203728). {ECO:0000269|PubMed:10878805, CC ECO:0000269|PubMed:11375975, ECO:0000269|PubMed:11821434, CC ECO:0000269|PubMed:12444095, ECO:0000269|PubMed:12446668, CC ECO:0000269|PubMed:16203728}. CC -!- INTERACTION: CC Q96RT1; Q9HC29: NOD2; NbExp=5; IntAct=EBI-993903, EBI-7445625; CC Q96RT1; Q99569: PKP4; NbExp=4; IntAct=EBI-993903, EBI-726447; CC Q96RT1-2; Q9HC29: NOD2; NbExp=5; IntAct=EBI-8449250, EBI-7445625; CC Q96RT1-2; Q99569: PKP4; NbExp=4; IntAct=EBI-8449250, EBI-726447; CC -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome CC {ECO:0000269|PubMed:10878805, ECO:0000269|PubMed:11375975}. Nucleus CC membrane {ECO:0000250}. Basolateral cell membrane CC {ECO:0000269|PubMed:16203728}. Note=Found in hemidesmosomes, which are CC cell-substrate adhesion complexes in stratified epithelia. In CC transfected cells, either diffusely distributed over the cytoplasm or CC concentrated at the basolateral membrane. Colocalizes with the CC adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of CC cardiac myocytes (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; CC IsoId=Q96RT1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96RT1-2; Sequence=VSP_010802; CC Name=3; CC IsoId=Q96RT1-3; Sequence=VSP_010802, VSP_010804; CC Name=4; CC IsoId=Q96RT1-4; Sequence=VSP_010802, VSP_010807; CC Name=5; CC IsoId=Q96RT1-5; Sequence=VSP_010802, VSP_010803; CC Name=6; CC IsoId=Q96RT1-6; Sequence=VSP_010802, VSP_010806; CC Name=7; CC IsoId=Q96RT1-7; Sequence=VSP_010802, VSP_010803, VSP_010804, CC VSP_010805; CC Name=8; CC IsoId=Q96RT1-8; Sequence=VSP_044536; CC Name=9; CC IsoId=Q96RT1-9; Sequence=VSP_047389, VSP_010802; CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney, muscle CC and stomach, followed by liver, spleen and intestine. CC {ECO:0000269|PubMed:10878805}. CC -!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH50692.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA91538.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF263744; AAF77048.1; -; mRNA. DR EMBL; AF276423; AAK69431.1; -; mRNA. DR EMBL; AB033051; BAA86539.2; -; mRNA. DR EMBL; AK001180; BAA91538.1; ALT_INIT; mRNA. DR EMBL; AK304693; BAG65463.1; -; mRNA. DR EMBL; AC010359; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC025442; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC050692; AAH50692.1; ALT_SEQ; mRNA. DR EMBL; BC115012; AAI15013.1; -; mRNA. DR EMBL; BC126464; AAI26465.1; -; mRNA. DR EMBL; BC144075; AAI44076.1; -; mRNA. DR CCDS; CCDS34172.1; -. [Q96RT1-7] DR CCDS; CCDS3990.1; -. [Q96RT1-2] DR CCDS; CCDS58951.1; -. [Q96RT1-9] DR CCDS; CCDS58952.1; -. [Q96RT1-8] DR CCDS; CCDS58953.1; -. [Q96RT1-1] DR CCDS; CCDS58954.1; -. [Q96RT1-4] DR RefSeq; NP_001006600.1; NM_001006600.2. [Q96RT1-7] DR RefSeq; NP_001240626.1; NM_001253697.1. [Q96RT1-1] DR RefSeq; NP_001240627.1; NM_001253698.1. [Q96RT1-4] DR RefSeq; NP_001240628.1; NM_001253699.1. [Q96RT1-8] DR RefSeq; NP_001240630.1; NM_001253701.1. [Q96RT1-9] DR RefSeq; NP_061165.1; NM_018695.3. [Q96RT1-2] DR PDB; 1MFG; X-ray; 1.25 A; A=1321-1412. DR PDB; 1MFL; X-ray; 1.88 A; A=1321-1412. DR PDB; 1N7T; NMR; -; A=1314-1412. DR PDB; 2H3L; X-ray; 1.00 A; A/B=1314-1412. DR PDB; 2QBW; X-ray; 1.80 A; A=1330-1410. DR PDB; 3CH8; X-ray; 1.90 A; A=1330-1410. DR PDB; 6Q0M; X-ray; 1.20 A; A/B=1321-1410. DR PDB; 6Q0N; X-ray; 1.18 A; A/B=1321-1410. DR PDB; 6Q0U; X-ray; 1.89 A; A/B=1321-1410. DR PDB; 6UBH; X-ray; 1.80 A; A/B/C/D=1321-1412. DR PDB; 7LUL; X-ray; 1.65 A; A=1321-1412. DR PDBsum; 1MFG; -. DR PDBsum; 1MFL; -. DR PDBsum; 1N7T; -. DR PDBsum; 2H3L; -. DR PDBsum; 2QBW; -. DR PDBsum; 3CH8; -. DR PDBsum; 6Q0M; -. DR PDBsum; 6Q0N; -. DR PDBsum; 6Q0U; -. DR PDBsum; 6UBH; -. DR PDBsum; 7LUL; -. DR AlphaFoldDB; Q96RT1; -. DR BMRB; Q96RT1; -. DR SMR; Q96RT1; -. DR BioGRID; 120997; 258. DR ELM; Q96RT1; -. DR IntAct; Q96RT1; 177. DR MINT; Q96RT1; -. DR STRING; 9606.ENSP00000426632; -. DR GlyGen; Q96RT1; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q96RT1; -. DR MetOSite; Q96RT1; -. DR PhosphoSitePlus; Q96RT1; -. DR SwissPalm; Q96RT1; -. DR BioMuta; ERBIN; -. DR DMDM; 116242614; -. DR EPD; Q96RT1; -. DR jPOST; Q96RT1; -. DR MassIVE; Q96RT1; -. DR MaxQB; Q96RT1; -. DR PaxDb; 9606-ENSP00000426632; -. DR PeptideAtlas; Q96RT1; -. DR ProteomicsDB; 17666; -. DR ProteomicsDB; 19501; -. DR ProteomicsDB; 78021; -. [Q96RT1-1] DR ProteomicsDB; 78022; -. [Q96RT1-2] DR ProteomicsDB; 78023; -. [Q96RT1-3] DR ProteomicsDB; 78024; -. [Q96RT1-4] DR ProteomicsDB; 78025; -. [Q96RT1-5] DR ProteomicsDB; 78026; -. [Q96RT1-6] DR ProteomicsDB; 78027; -. [Q96RT1-7] DR Pumba; Q96RT1; -. DR Antibodypedia; 23812; 239 antibodies from 32 providers. DR DNASU; 55914; -. DR Ensembl; ENST00000284037.10; ENSP00000284037.4; ENSG00000112851.16. [Q96RT1-1] DR Ensembl; ENST00000380938.6; ENSP00000370325.2; ENSG00000112851.16. [Q96RT1-4] DR Ensembl; ENST00000380943.6; ENSP00000370330.2; ENSG00000112851.16. [Q96RT1-2] DR Ensembl; ENST00000506030.6; ENSP00000426632.1; ENSG00000112851.16. [Q96RT1-8] DR Ensembl; ENST00000508515.2; ENSP00000422015.1; ENSG00000112851.16. [Q96RT1-7] DR Ensembl; ENST00000511297.5; ENSP00000422766.1; ENSG00000112851.16. [Q96RT1-9] DR Ensembl; ENST00000699000.1; ENSP00000514078.1; ENSG00000112851.16. [Q96RT1-2] DR Ensembl; ENST00000699001.1; ENSP00000514079.1; ENSG00000112851.16. [Q96RT1-7] DR GeneID; 55914; -. DR KEGG; hsa:55914; -. DR MANE-Select; ENST00000284037.10; ENSP00000284037.4; NM_001253697.2; NP_001240626.1. DR UCSC; uc003jui.3; human. [Q96RT1-1] DR AGR; HGNC:15842; -. DR CTD; 55914; -. DR DisGeNET; 55914; -. DR GeneCards; ERBIN; -. DR HGNC; HGNC:15842; ERBIN. DR HPA; ENSG00000112851; Low tissue specificity. DR MIM; 606944; gene. DR neXtProt; NX_Q96RT1; -. DR OpenTargets; ENSG00000112851; -. DR PharmGKB; PA27845; -. DR VEuPathDB; HostDB:ENSG00000112851; -. DR eggNOG; KOG0619; Eukaryota. DR GeneTree; ENSGT00940000159526; -. DR HOGENOM; CLU_004220_1_0_1; -. DR InParanoid; Q96RT1; -. DR OMA; QLPETIX; -. DR OrthoDB; 2909504at2759; -. DR PhylomeDB; Q96RT1; -. DR TreeFam; TF351429; -. DR PathwayCommons; Q96RT1; -. DR Reactome; R-HSA-1227986; Signaling by ERBB2. DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013026; RHOB GTPase cycle. DR Reactome; R-HSA-9013106; RHOC GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013404; RAC2 GTPase cycle. DR Reactome; R-HSA-9013408; RHOG GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR Reactome; R-HSA-9634285; Constitutive Signaling by Overexpressed ERBB2. DR Reactome; R-HSA-9652282; Drug-mediated inhibition of ERBB2 signaling. DR Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants. DR Reactome; R-HSA-9665233; Resistance of ERBB2 KD mutants to trastuzumab. DR Reactome; R-HSA-9665244; Resistance of ERBB2 KD mutants to sapitinib. DR Reactome; R-HSA-9665245; Resistance of ERBB2 KD mutants to tesevatinib. DR Reactome; R-HSA-9665246; Resistance of ERBB2 KD mutants to neratinib. DR Reactome; R-HSA-9665247; Resistance of ERBB2 KD mutants to osimertinib. DR Reactome; R-HSA-9665249; Resistance of ERBB2 KD mutants to afatinib. DR Reactome; R-HSA-9665250; Resistance of ERBB2 KD mutants to AEE788. DR Reactome; R-HSA-9665251; Resistance of ERBB2 KD mutants to lapatinib. DR Reactome; R-HSA-9665348; Signaling by ERBB2 ECD mutants. DR Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants. DR Reactome; R-HSA-9665737; Drug resistance in ERBB2 TMD/JMD mutants. DR SignaLink; Q96RT1; -. DR SIGNOR; Q96RT1; -. DR BioGRID-ORCS; 55914; 13 hits in 1147 CRISPR screens. DR ChiTaRS; ERBIN; human. DR EvolutionaryTrace; Q96RT1; -. DR GeneWiki; Erbin_(protein); -. DR GenomeRNAi; 55914; -. DR Pharos; Q96RT1; Tbio. DR PRO; PR:Q96RT1; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q96RT1; Protein. DR Bgee; ENSG00000112851; Expressed in corpus callosum and 210 other cell types or tissues. DR ExpressionAtlas; Q96RT1; baseline and differential. DR GO; GO:0009925; C:basal plasma membrane; NAS:UniProtKB. DR GO; GO:0005604; C:basement membrane; TAS:ProtInc. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB. DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0099572; C:postsynaptic specialization; IEA:Ensembl. DR GO; GO:0005176; F:ErbB-2 class receptor binding; TAS:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB. DR GO; GO:0045175; P:basal protein localization; NAS:UniProtKB. DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:UniProtKB. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:UniProtKB. DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; NAS:UniProtKB. DR GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; NAS:UniProtKB. DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IEA:Ensembl. DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB. DR GO; GO:0070433; P:negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB. DR GO; GO:0006605; P:protein targeting; IEA:Ensembl. DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB. DR GO; GO:0032495; P:response to muramyl dipeptide; IMP:UniProtKB. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3. DR IDEAL; IID00494; -. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR PANTHER; PTHR23119; DISCS LARGE; 1. DR PANTHER; PTHR23119:SF46; ERBB2-INTERACTING PROTEIN; 1. DR Pfam; PF13855; LRR_8; 3. DR Pfam; PF00595; PDZ; 1. DR SMART; SM00364; LRR_BAC; 9. DR SMART; SM00365; LRR_SD22; 7. DR SMART; SM00369; LRR_TYP; 12. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF52058; L domain-like; 2. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR PROSITE; PS51450; LRR; 15. DR PROSITE; PS50106; PDZ; 1. DR Genevisible; Q96RT1; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; KW Leucine-rich repeat; Membrane; Nucleus; Phosphoprotein; Reference proteome; KW Repeat. FT CHAIN 1..1412 FT /note="Erbin" FT /id="PRO_0000188301" FT REPEAT 23..44 FT /note="LRR 1" FT REPEAT 47..68 FT /note="LRR 2" FT REPEAT 70..91 FT /note="LRR 3" FT REPEAT 93..114 FT /note="LRR 4" FT REPEAT 116..137 FT /note="LRR 5" FT REPEAT 139..161 FT /note="LRR 6" FT REPEAT 162..183 FT /note="LRR 7" FT REPEAT 185..206 FT /note="LRR 8" FT REPEAT 208..229 FT /note="LRR 9" FT REPEAT 231..252 FT /note="LRR 10" FT REPEAT 254..275 FT /note="LRR 11" FT REPEAT 277..298 FT /note="LRR 12" FT REPEAT 300..321 FT /note="LRR 13" FT REPEAT 323..344 FT /note="LRR 14" FT REPEAT 346..367 FT /note="LRR 15" FT REPEAT 369..391 FT /note="LRR 16" FT REPEAT 392..413 FT /note="LRR 17" FT DOMAIN 1321..1410 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT REGION 464..489 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 506..542 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 615..681 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 803..867 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 997..1021 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1075..1192 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 464..478 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 506..530 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 631..645 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 646..681 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 811..831 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 846..867 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1075..1092 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1126..1175 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 440 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 444 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80TH2" FT MOD_RES 483 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q80TH2" FT MOD_RES 485 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 569 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 598 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80TH2" FT MOD_RES 602 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 603 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 620 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 715 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80TH2" FT MOD_RES 852 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 857 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 872 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 917 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 920 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15144186" FT MOD_RES 931 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 972 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 1104 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q80TH2" FT MOD_RES 1158 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1179 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1286 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 531..534 FT /note="Missing (in isoform 9)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_047389" FT VAR_SEQ 1212..1252 FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform FT 5, isoform 6, isoform 7 and isoform 9)" FT /evidence="ECO:0000303|PubMed:10574462, FT ECO:0000303|PubMed:10878805, ECO:0000303|PubMed:11375975, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_010802" FT VAR_SEQ 1212..1252 FT /note="KHPQTSSSGDPCQDGIFISGQQNYSSATLSHKDVPPDSLMK -> SMLSRSF FT NSNFTTVSSFHCGSSRDLHGSQGSLALSVADRRGSGGHIFR (in isoform 8)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_044536" FT VAR_SEQ 1253..1267 FT /note="Missing (in isoform 5 and isoform 7)" FT /evidence="ECO:0000303|PubMed:11375975" FT /id="VSP_010803" FT VAR_SEQ 1268..1278 FT /note="Missing (in isoform 3 and isoform 7)" FT /evidence="ECO:0000303|PubMed:11375975" FT /id="VSP_010804" FT VAR_SEQ 1279..1321 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:11375975" FT /id="VSP_010805" FT VAR_SEQ 1322..1352 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:11375975" FT /id="VSP_010806" FT VAR_SEQ 1353..1377 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11375975, FT ECO:0000303|PubMed:14702039" FT /id="VSP_010807" FT VARIANT 274 FT /note="S -> L (in dbSNP:rs3213837)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_019346" FT VARIANT 313 FT /note="A -> V (in dbSNP:rs191137999)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_068905" FT VARIANT 746 FT /note="K -> E (in dbSNP:rs16894812)" FT /id="VAR_028304" FT VARIANT 914 FT /note="K -> R (in dbSNP:rs34521887)" FT /id="VAR_046673" FT VARIANT 1089 FT /note="G -> V (in dbSNP:rs35601230)" FT /id="VAR_046674" FT VARIANT 1112 FT /note="S -> L (in dbSNP:rs3805466)" FT /id="VAR_019347" FT VARIANT 1207 FT /note="K -> E" FT /evidence="ECO:0000269|PubMed:11375975" FT /id="VAR_019348" FT CONFLICT 271 FT /note="T -> P (in Ref. 7; AAI15013)" FT /evidence="ECO:0000305" FT CONFLICT 547 FT /note="D -> G (in Ref. 7; AAI15013)" FT /evidence="ECO:0000305" FT CONFLICT 805 FT /note="E -> G (in Ref. 5; BAA91538)" FT /evidence="ECO:0000305" FT CONFLICT 813 FT /note="Y -> C (in Ref. 2; AAK69431)" FT /evidence="ECO:0000305" FT CONFLICT 848 FT /note="G -> C (in Ref. 5; BAG65463)" FT /evidence="ECO:0000305" FT CONFLICT 1047 FT /note="R -> S (in Ref. 5; BAG65463)" FT /evidence="ECO:0000305" FT CONFLICT 1205 FT /note="E -> G (in Ref. 7; AAI15013)" FT /evidence="ECO:0000305" FT CONFLICT 1267 FT /note="Q -> P (in Ref. 7; AAI15013)" FT /evidence="ECO:0000305" FT CONFLICT 1328 FT /note="K -> R (in Ref. 7; AAI15013)" FT /evidence="ECO:0000305" FT STRAND 1318..1327 FT /evidence="ECO:0007829|PDB:2H3L" FT STRAND 1329..1331 FT /evidence="ECO:0007829|PDB:2H3L" FT STRAND 1333..1338 FT /evidence="ECO:0007829|PDB:2H3L" FT TURN 1339..1342 FT /evidence="ECO:0007829|PDB:2H3L" FT STRAND 1346..1348 FT /evidence="ECO:0007829|PDB:2H3L" FT STRAND 1353..1359 FT /evidence="ECO:0007829|PDB:2H3L" FT TURN 1364..1368 FT /evidence="ECO:0007829|PDB:2H3L" FT STRAND 1374..1378 FT /evidence="ECO:0007829|PDB:2H3L" FT HELIX 1388..1397 FT /evidence="ECO:0007829|PDB:2H3L" FT STRAND 1400..1410 FT /evidence="ECO:0007829|PDB:2H3L" SQ SEQUENCE 1412 AA; 158298 MW; 304DFC81578CF671 CRC64; MTTKRSLFVR LVPCRCLRGE EETVTTLDYS HCSLEQVPKE IFTFEKTLEE LYLDANQIEE LPKQLFNCQS LHKLSLPDND LTTLPASIAN LINLRELDVS KNGIQEFPEN IKNCKVLTIV EASVNPISKL PDGFSQLLNL TQLYLNDAFL EFLPANFGRL TKLQILELRE NQLKMLPKTM NRLTQLERLD LGSNEFTEVP EVLEQLSGLK EFWMDANRLT FIPGFIGSLK QLTYLDVSKN NIEMVEEGIS TCENLQDLLL SSNSLQQLPE TIGSLKNITT LKIDENQLMY LPDSIGGLIS VEELDCSFNE VEALPSSIGQ LTNLRTFAAD HNYLQQLPPE IGSWKNITVL FLHSNKLETL PEEMGDMQKL KVINLSDNRL KNLPFSFTKL QQLTAMWLSD NQSKPLIPLQ KETDSETQKM VLTNYMFPQQ PRTEDVMFIS DNESFNPSLW EEQRKQRAQV AFECDEDKDE REAPPREGNL KRYPTPYPDE LKNMVKTVQT IVHRLKDEET NEDSGRDLKP HEDQQDINKD VGVKTSESTT TVKSKVDERE KYMIGNSVQK ISEPEAEISP GSLPVTANMK ASENLKHIVN HDDVFEESEE LSSDEEMKMA EMRPPLIETS INQPKVVALS NNKKDDTKET DSLSDEVTHN SNQNNSNCSS PSRMSDSVSL NTDSSQDTSL CSPVKQTHID INSKIRQEDE NFNSLLQNGD ILNSSTEEKF KAHDKKDFNL PEYDLNVEER LVLIEKSVDS TATADDTHKL DHINMNLNKL ITNDTFQPEI MERSKTQDIV LGTSFLSINS KEETEHLENG NKYPNLESVN KVNGHSEETS QSPNRTEPHD SDCSVDLGIS KSTEDLSPQK SGPVGSVVKS HSITNMEIGG LKIYDILSDN GPQQPSTTVK ITSAVDGKNI VRSKSATLLY DQPLQVFTGS SSSSDLISGT KAIFKFDSNH NPEEPNIIRG PTSGPQSAPQ IYGPPQYNIQ YSSSAAVKDT LWHSKQNPQI DHASFPPQLL PRSESTENQS YAKHSANMNF SNHNNVRANT AYHLHQRLGP ARHGEMWAIS PNDRLIPAVT RSTIQRQSSV SSTASVNLGD PGSTRRAQIP EGDYLSYREF HSAGRTPPMM PGSQRPLSAR TYSIDGPNAS RPQSARPSIN EIPERTMSVS DFNYSRTSPS KRPNARVGSE HSLLDPPGKS KVPRDWREQV LRHIEAKKLE KKHPQTSSSG DPCQDGIFIS GQQNYSSATL SHKDVPPDSL MKMPLSNGQM GQPLRPQANY SQIHHPPQAS VARHPSREQL IDYLMLKVAH QPPYTQPHCS PRQGHELAKQ EIRVRVEKDP ELGFSISGGV GGRGNPFRPD DDGIFVTRVQ PEGPASKLLQ PGDKIIQANG YSFINIEHGQ AVSLLKTFQN TVELIIVREV SS //