PTN23_MOUSE
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 03-AUG-2022, entry version 147.
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, Pancreas,
RC 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; 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};
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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; 53.
DR DIP; DIP-48351N; -.
DR IntAct; Q6PB44; 43.
DR STRING; 10090.ENSMUSP00000039580; -.
DR iPTMnet; Q6PB44; -.
DR PhosphoSitePlus; Q6PB44; -.
DR SwissPalm; Q6PB44; -.
DR EPD; Q6PB44; -.
DR jPOST; Q6PB44; -.
DR MaxQB; Q6PB44; -.
DR PaxDb; Q6PB44; -.
DR PeptideAtlas; Q6PB44; -.
DR PRIDE; Q6PB44; -.
DR ProteomicsDB; 301939; -. [Q6PB44-1]
DR ProteomicsDB; 301940; -. [Q6PB44-2]
DR Antibodypedia; 12918; 151 antibodies from 25 providers.
DR DNASU; 104831; -.
DR Ensembl; ENSMUST00000040021; ENSMUSP00000039580; ENSMUSG00000036057. [Q6PB44-1]
DR GeneID; 104831; -.
DR KEGG; mmu:104831; -.
DR UCSC; uc009rty.1; mouse. [Q6PB44-1]
DR UCSC; uc012hbi.1; mouse. [Q6PB44-2]
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; 550620at2759; -.
DR PhylomeDB; Q6PB44; -.
DR TreeFam; TF323502; -.
DR BioGRID-ORCS; 104831; 10 hits in 74 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 158 other tissues.
DR ExpressionAtlas; Q6PB44; baseline and differential.
DR Genevisible; Q6PB44; MM.
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: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:0006470; P:protein dephosphorylation; IEA:InterPro.
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 Gene3D; 1.25.40.280; -; 1.
DR Gene3D; 3.90.190.10; -; 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; PTHR23030; 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; SSF52799; 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.
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
