ID PTN23_MOUSE Reviewed; 1692 AA. AC Q6PB44; Q69ZJ0; Q8R1Z5; Q923E6; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 2. DT 27-MAR-2024, entry version 156. DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 23; DE EC=3.1.3.48; GN Name=Ptpn23; Synonyms=Kiaa1471; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-193. RC TISSUE=Dendritic cell; 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., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., 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., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-438. RC TISSUE=Fetal brain, and Fetal eye; RG The MGC Project Team; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 394-1692 (ISOFORM 1), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1183-1692 (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Brain, Eye, and Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 712-1439. RC TISSUE=Thymus; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-744, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Plays a role in sorting of endocytic ubiquitinated cargos CC into multivesicular bodies (MVBs) via its interaction with the ESCRT-I CC complex (endosomal sorting complex required for transport I), and CC possibly also other ESCRT complexes. May act as a negative regulator of CC Ras-mediated mitogenic activity. Plays a role in ciliogenesis (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044}; CC -!- SUBUNIT: Interacts with GRAP2 and GRB2. Interacts with UBAP1 and CHMP4B CC (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q6PB44; Q8BR07: Bicd1; NbExp=7; IntAct=EBI-4284816, EBI-11569902; CC Q6PB44; O89100: Grap2; NbExp=3; IntAct=EBI-4284816, EBI-642151; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. CC Cytoplasmic vesicle {ECO:0000250}. Endosome {ECO:0000250}. Cytoplasm, CC cytoskeleton, cilium basal body {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6PB44-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6PB44-2; Sequence=VSP_014195; CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD32456.1; Type=Erroneous initiation; 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; BY750106; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CF734421; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CB248963; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC006582; AAH06582.1; -; mRNA. DR EMBL; BC022721; AAH22721.1; -; mRNA. DR EMBL; BC059902; AAH59902.1; -; mRNA. DR EMBL; AK173178; BAD32456.1; ALT_INIT; mRNA. DR CCDS; CCDS40780.1; -. [Q6PB44-1] DR RefSeq; NP_001074512.1; NM_001081043.1. [Q6PB44-1] DR PDB; 2W10; X-ray; 1.90 A; C/D=719-730. DR PDBsum; 2W10; -. DR AlphaFoldDB; Q6PB44; -. DR SMR; Q6PB44; -. DR BioGRID; 222711; 54. DR DIP; DIP-48351N; -. DR IntAct; Q6PB44; 45. DR MINT; Q6PB44; -. DR STRING; 10090.ENSMUSP00000039580; -. DR GlyGen; Q6PB44; 9 sites, 1 O-linked glycan (9 sites). DR iPTMnet; Q6PB44; -. DR PhosphoSitePlus; Q6PB44; -. DR SwissPalm; Q6PB44; -. DR EPD; Q6PB44; -. DR jPOST; Q6PB44; -. DR MaxQB; Q6PB44; -. DR PaxDb; 10090-ENSMUSP00000039580; -. DR PeptideAtlas; Q6PB44; -. DR ProteomicsDB; 301939; -. [Q6PB44-1] DR ProteomicsDB; 301940; -. [Q6PB44-2] DR Pumba; Q6PB44; -. DR Antibodypedia; 12918; 187 antibodies from 25 providers. DR DNASU; 104831; -. DR Ensembl; ENSMUST00000040021.12; ENSMUSP00000039580.8; ENSMUSG00000036057.12. [Q6PB44-1] DR GeneID; 104831; -. DR KEGG; mmu:104831; -. DR UCSC; uc009rty.1; mouse. [Q6PB44-1] DR UCSC; uc012hbi.1; mouse. [Q6PB44-2] DR AGR; MGI:2144837; -. DR CTD; 25930; -. DR MGI; MGI:2144837; Ptpn23. DR VEuPathDB; HostDB:ENSMUSG00000036057; -. DR eggNOG; KOG0789; Eukaryota. DR eggNOG; KOG2220; Eukaryota. DR GeneTree; ENSGT00940000157687; -. DR HOGENOM; CLU_001129_0_0_1; -. DR InParanoid; Q6PB44; -. DR OMA; GPTQLMQ; -. DR OrthoDB; 53884at2759; -. DR PhylomeDB; Q6PB44; -. DR TreeFam; TF323502; -. DR BioGRID-ORCS; 104831; 12 hits in 79 CRISPR screens. DR ChiTaRS; Ptpn23; mouse. DR EvolutionaryTrace; Q6PB44; -. DR PRO; PR:Q6PB44; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q6PB44; Protein. DR Bgee; ENSMUSG00000036057; Expressed in internal carotid artery and 161 other cell types or tissues. DR ExpressionAtlas; Q6PB44; baseline and differential. DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0005769; C:early endosome; ISS:UniProtKB. DR GO; GO:0005768; C:endosome; ISS:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0016604; C:nuclear body; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI. DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:MGI. DR GO; GO:0032456; P:endocytic recycling; ISO:MGI. DR GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:MGI. DR GO; GO:1903393; P:positive regulation of adherens junction organization; ISO:MGI. DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:MGI. DR GO; GO:1903387; P:positive regulation of homophilic cell adhesion; ISO:MGI. DR GO; GO:0061357; P:positive regulation of Wnt protein secretion; ISO:MGI. DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central. DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB. DR CDD; cd09239; BRO1_HD-PTP_like; 1. DR CDD; cd14539; PTP-N23; 1. DR CDD; cd09234; V_HD-PTP_like; 1. DR Gene3D; 1.20.120.560; alix/aip1 in complex with the ypdl late domain; 1. DR Gene3D; 1.20.140.50; alix/aip1 like domains; 1. DR Gene3D; 1.25.40.280; alix/aip1 like domains; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR IDEAL; IID50093; -. DR InterPro; IPR025304; ALIX_V_dom. DR InterPro; IPR045251; BRO1-like. DR InterPro; IPR004328; BRO1_dom. DR InterPro; IPR038499; BRO1_sf. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000242; PTP_cat. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; Tyr_Pase_dom. DR PANTHER; PTHR23030; PCD6 INTERACTING PROTEIN-RELATED; 1. DR PANTHER; PTHR23030:SF30; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 23; 1. DR Pfam; PF13949; ALIX_LYPXL_bnd; 1. DR Pfam; PF03097; BRO1; 1. DR Pfam; PF00102; Y_phosphatase; 1. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM01041; BRO1; 1. DR SMART; SM00194; PTPc; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS51180; BRO1; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. DR Genevisible; Q6PB44; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Cilium; KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle; KW Cytoskeleton; Endosome; Hydrolase; Methylation; Nucleus; Phosphoprotein; KW Protein phosphatase; Protein transport; Reference proteome; Repeat; KW TPR repeat; Transport. FT CHAIN 1..1692 FT /note="Tyrosine-protein phosphatase non-receptor type 23" FT /id="PRO_0000094778" FT DOMAIN 8..394 FT /note="BRO1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526" FT REPEAT 250..283 FT /note="TPR 1" FT REPEAT 374..407 FT /note="TPR 2" FT REPEAT 977..978 FT /note="1" FT REPEAT 979..980 FT /note="2" FT REPEAT 981..982 FT /note="3" FT REPEAT 983..984 FT /note="4" FT REPEAT 985..986 FT /note="5" FT REPEAT 987..988 FT /note="6" FT REPEAT 989..990 FT /note="7" FT REPEAT 991..992 FT /note="8" FT REPEAT 993..994 FT /note="9" FT REPEAT 995..996 FT /note="10" FT REPEAT 997..998 FT /note="11" FT REPEAT 999..1000 FT /note="12" FT REPEAT 1001..1002 FT /note="13" FT REPEAT 1003..1004 FT /note="14" FT REPEAT 1005..1006 FT /note="15" FT REPEAT 1007..1008 FT /note="16" FT REPEAT 1009..1010 FT /note="17" FT REPEAT 1011..1012 FT /note="18" FT REPEAT 1013..1014 FT /note="19" FT REPEAT 1015..1016 FT /note="20" FT REPEAT 1017..1018 FT /note="21" FT DOMAIN 1248..1508 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 711..788 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 773..1186 FT /note="His" FT REGION 884..923 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 944..1199 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 977..1018 FT /note="21 X 2 AA approximate tandem repeats of P-Q" FT REGION 1574..1638 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 552..639 FT /evidence="ECO:0000255" FT COMPBIAS 728..744 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 895..923 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 978..1033 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1042..1066 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1079..1164 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1579..1625 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1448 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160, FT ECO:0000255|PROSITE-ProRule:PRU10044" FT MOD_RES 744 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 974 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9H3S7" FT MOD_RES 1178 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H3S7" FT MOD_RES 1179 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H3S7" FT MOD_RES 1187 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9H3S7" FT MOD_RES 1671 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9H3S7" FT VAR_SEQ 1352..1353 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014195" FT CONFLICT 1353..1354 FT /note="Missing (in Ref. 3; AAH06582)" FT /evidence="ECO:0000305" SQ SEQUENCE 1692 AA; 185216 MW; 331363C917E9C4D2 CRC64; MEAVPRMPMI WLDLKEAGDF HFQSAVKKFV LKNYGENPEA YNEELKKLEL LRQNAIRVAR DFEGCSVLRK YLGQLHYLQS RVPMGSGQEA AVAVTWTEIF SGKSVSHEDI KYEQACILYN LGALHSMLGA MDKRVSEEGM KVSCTHFQCA AGAFAYLREH FPQAFSVDMS RQILTLNVNL MLGQAQECLL EKSMLDNRKS FLVARISAQV VDYYKEACRA LENPDTASLL GRIQKDWKKL VQMKIYYFAA VAHLHMGKQA EEQQKFGERV AYFQSALDKL NEAIKLAKGQ PDTVQDALRF AMDVIGGKYN SAKKDNDFIY HEAVPALDTL QPVKGAPLVK PLPVNPTDPA VTGPDIFAKL VPMAAHEASS LYSEEKAKLL REMLAKIEDK NEVLDQFMDS MQLDPETVDN LDAYNHIPPQ LMEKCAALSV RPDTVKNLVQ SMQVLSGVFT DVEASLKDIR DLLEEDELQE QKLQETLGQA GAGPGPSVAK AELAEVRREW AKYMEVHEKA SFTNSELHRA MNLHVGNLRL LSGPLDQVRA ALPTPALTPE DKAVLQNLKR ILAKVQEMRD QRVSLEQQLR ELIQKDDITA SLVTTDHSEM KKLFEEQLKK YDQLKVYLEQ NLAAQDNVLR ALTEANVQYA AVRRVLSELD QKWNSTLQTL VASYEAYEDL MKKSQEGKDF YADLESKVAT LLERAQSICR AQEAARQQLL DRELKKKAPP PRPTAPKPLL SRREEGEAVE AGDTPEELRS LPPDMMVGPR LPDPFLGTTA PLHFSPGPFP SSTGPATHYL SGPLPPGTYS GPTQLMQPRA AVPMAPATVL YPAPAYTSEL GLVPRSSPQH GIVSSPYAGV GPPQPVVGLP SAPPPQLSGP ELAMTVRPAT TTVDSVQAPI SSHTAPRPNP TPALPQPCFP VPQPVPQSVP QPQPLPVPYT YSIGTKQPLP APYTYSIGTK QHLTGPLPQH QFPPGIPTGF PVPRTGPQAQ AQPQPQPQPQ PQPQPQPQPQ PQPQSQSQPQ PQPQPQPQRP AFGPQPTQQP LPFQHPHLFP SQAPGILPPP PPTPYHFTPQ PGVLGQPPPT LHTQLYPGPS QDPLPPHSGA LPFPSPGPPH PHPTLAYGPA PSPRPLGPQA TPVSIRGPPP ASQPTPSPHL VPSPAPSPGP GPVPSRPPTA EPPPCLRRGA AAADLLSSSP ESQHGGTQPP GGGQPLLQPT KVDAAEGRRP QALRLIEQDP YEHPERLQQL QQELEAFRGQ LGDAGALDAI WRELQEAQEH DARGRSIAIA RCYSLKNRHQ DVMPYDSNRV VLRSGKDDYI NASCVEGLSP YCPPLVATQA PLPGTAADFW LMVHEQKVSV IVMLVSEAEM EKQKVARYFP TERGQPMVHG ALSVALSSIR TTETHVERVL SLQFRDQSLK RSLVHLHFPT WPELGLPDSP GNLLRFIQEV HAHYLHQRPL HTPIVVHCSS GVGRTGAFAL LYAAVQEVEA GNGIPELPQL VRRMRQQRKH MLQEKLHLKF CHEALVRHVE QVLQRHGVPP PGKPVASVNI SQKNHLPQDS QDLVLGGDVP ISSIQATIAK LSIRPLGGLD SPAASLPGLV EPPGLPPASL PESTPVPSSS PPPLSSPLPE APQPEEEPSV PEAPSLGPPS SSLELLASLT PEAFSLDSSL RGKQRMSKQN FLQAHNGQGL RAAQPTDDPL SLLDPLWTLN KT //