PTPRU_MOUSE
ID PTPRU_MOUSE Reviewed; 1446 AA.
AC B1AUH1; O35564; P70125; Q3V312; Q66JV9;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase U;
DE Short=R-PTP-U;
DE EC=3.1.3.48;
DE AltName: Full=Ftp-1;
DE AltName: Full=Pancreatic carcinoma phosphatase 2;
DE Short=PCP-2;
DE AltName: Full=Protein-tyrosine phosphatase-lamda;
DE Short=PTP-lambda;
DE Short=PTPlambda;
DE AltName: Full=Receptor-type protein-tyrosine phosphatase psi;
DE Short=R-PTP-psi;
DE Flags: Precursor;
GN Name=Ptpru; Synonyms=Pcp2, Ptpf;
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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal liver;
RX PubMed=9272866; DOI=10.1016/s0378-1119(97)00174-1;
RA Yoneya T., Yamada Y., Kakeda M., Osawa M., Arai E., Hayashi K., Nishi N.,
RA Inoue H., Nishikawa M.;
RT "Molecular cloning of a novel receptor-type protein tyrosine phosphatase
RT from murine fetal liver.";
RL Gene 194:241-247(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), HOMOOLIGOMERIZATION, INTERACTION
RP WITH CTNNB1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PROTEOLYTIC
RP PROCESSING.
RC TISSUE=Lung;
RX PubMed=9054423; DOI=10.1074/jbc.272.11.7264;
RA Cheng J., Wu K., Armanini M., O'Rourke N., Dowbenko D., Lasky L.A.;
RT "A novel protein-tyrosine phosphatase related to the homotypically adhering
RT kappa and mu receptors.";
RL J. Biol. Chem. 272:7264-7277(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1286 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-911 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=15040814; DOI=10.1186/1471-2164-5-14;
RA Besco J., Popesco M.C., Davuluri R.V., Frostholm A., Rotter A.;
RT "Genomic structure and alternative splicing of murine R2B receptor protein
RT tyrosine phosphatases (PTPkappa, mu, rho and PCP-2).";
RL BMC Genomics 5:14-14(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-853; SER-863 AND TYR-865, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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: Tyrosine-protein phosphatase which dephosphorylates CTNNB1.
CC Regulates CTNNB1 function both in cell adhesion and signaling. May
CC function in cell proliferation and migration and play a role in the
CC maintenance of epithelial integrity. May play a role in
CC megakaryocytopoiesis (By 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: Forms homooligomeric complexes which mediate cell homotypic
CC adhesion (Probable). Interacts (via the cytoplasmic juxtamembrane
CC domain) with CTNNB1; may mediate interaction with the cadherin/catenin
CC adhesion complex. Interacts with KIT (By similarity). May interact with
CC AP3B1 (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B1AUH1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B1AUH1-2; Sequence=VSP_037086;
CC -!- TISSUE SPECIFICITY: Transcripts of different sizes are differentially
CC expressed in a subset of tissues. Detected in brain, lung, skeletal
CC muscle, heart, kidney and placenta. In brain; expressed in olfactory
CC bulb, cerebral cortex, hippocampus and cerebellum.
CC {ECO:0000269|PubMed:15040814, ECO:0000269|PubMed:9054423,
CC ECO:0000269|PubMed:9272866}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development. First
CC detected at 7 dpc. {ECO:0000269|PubMed:9054423}.
CC -!- PTM: The extracellular domain is proteolytically processed through
CC cleavage within the fibronectin type-III 4 domain. In addition to the
CC 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa
CC and 73 kDa are observed (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues upon activation of KIT with
CC stem cell factor (SCF). The 73 kDa proteolytic product is not
CC phosphorylated (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH80736.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH80736.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAE43351.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; D88187; BAA23475.1; -; mRNA.
DR EMBL; U55057; AAB17895.1; -; mRNA.
DR EMBL; AL670959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30128.1; -; Genomic_DNA.
DR EMBL; AK052720; BAE43351.1; ALT_SEQ; mRNA.
DR EMBL; BC080736; AAH80736.1; ALT_SEQ; mRNA.
DR CCDS; CCDS18714.1; -. [B1AUH1-2]
DR CCDS; CCDS38896.1; -. [B1AUH1-1]
DR RefSeq; NP_001076588.1; NM_001083119.2. [B1AUH1-1]
DR RefSeq; NP_035344.2; NM_011214.2. [B1AUH1-2]
DR AlphaFoldDB; B1AUH1; -.
DR SMR; B1AUH1; -.
DR BioGRID; 202501; 11.
DR STRING; 10090.ENSMUSP00000030741; -.
DR GlyConnect; 2427; 2 N-Linked glycans (2 sites). [B1AUH1-2]
DR GlyGen; B1AUH1; 4 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; B1AUH1; -.
DR PhosphoSitePlus; B1AUH1; -.
DR MaxQB; B1AUH1; -.
DR PaxDb; B1AUH1; -.
DR PRIDE; B1AUH1; -.
DR ProteomicsDB; 301978; -. [B1AUH1-1]
DR ProteomicsDB; 301979; -. [B1AUH1-2]
DR Antibodypedia; 31032; 42 antibodies from 17 providers.
DR DNASU; 19273; -.
DR Ensembl; ENSMUST00000030741; ENSMUSP00000030741; ENSMUSG00000028909. [B1AUH1-1]
DR Ensembl; ENSMUST00000105987; ENSMUSP00000101607; ENSMUSG00000028909. [B1AUH1-2]
DR GeneID; 19273; -.
DR KEGG; mmu:19273; -.
DR UCSC; uc008vaa.1; mouse. [B1AUH1-1]
DR UCSC; uc008vab.1; mouse. [B1AUH1-2]
DR CTD; 10076; -.
DR MGI; MGI:1321151; Ptpru.
DR VEuPathDB; HostDB:ENSMUSG00000028909; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000157151; -.
DR HOGENOM; CLU_001645_0_2_1; -.
DR InParanoid; B1AUH1; -.
DR OMA; WEQVRSH; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; B1AUH1; -.
DR TreeFam; TF312900; -.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR BioGRID-ORCS; 19273; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ptpru; mouse.
DR PRO; PR:B1AUH1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1AUH1; protein.
DR Bgee; ENSMUSG00000028909; Expressed in ventricular zone and 179 other tissues.
DR ExpressionAtlas; B1AUH1; baseline and differential.
DR Genevisible; B1AUH1; MM.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008013; F:beta-catenin binding; IPI:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:MGI.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR CDD; cd00063; FN3; 3.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR000998; MAM_dom.
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 Pfam; PF00041; fn3; 2.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00020; MAMDOMAIN.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 1.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Differentiation; Disulfide bond; Glycoprotein; Hydrolase;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Protein phosphatase;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1446
FT /note="Receptor-type tyrosine-protein phosphatase U"
FT /id="PRO_0000371659"
FT TOPO_DOM 19..749
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 771..1446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..188
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 190..275
FT /note="Ig-like C2-type"
FT DOMAIN 288..383
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 386..484
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 485..591
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 592..668
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 888..1144
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1176..1439
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 771..887
FT /note="Mediates interaction with CTNNB1"
FT /evidence="ECO:0000269|PubMed:9054423"
FT REGION 830..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1085
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1380
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1053
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 1085..1091
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92729"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 865
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 210..264
FT /evidence="ECO:0000255"
FT VAR_SEQ 774..783
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9054423,
FT ECO:0000303|PubMed:9272866"
FT /id="VSP_037086"
FT CONFLICT 80
FT /note="A -> T (in Ref. 2; AAB17895)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="Y -> F (in Ref. 2; AAB17895)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="V -> A (in Ref. 6; AAH80736)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="P -> S (in Ref. 6; AAH80736)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="K -> R (in Ref. 6; AAH80736)"
FT /evidence="ECO:0000305"
FT CONFLICT 1158
FT /note="K -> R (in Ref. 2; AAB17895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1446 AA; 162494 MW; CBF639D8150D0D0B CRC64;
MARAQALVLA LTFQFCAPET ETPAAGCTFE EASDPVVPCE FSQAQYDDFQ WEQVRIHPGT
RTPEDLPHGA YLMVNASQHA PGQRAHIIFQ TLSENDTHCV QFSYFLYSRD GHSPGTLGVY
VRVNGGPLGS AVWNMTGSHG RQWHQAELAV STFWPNEYQV LFEALISPDH KGYIGLDDIL
LFSYPCAKAP HFSRLGDVEV NAGQNASFQC MAAGRAAEAE HFFLQRQSGV LVPAAGVRHI
SHRRFLATFP LASVGRSEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT
YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVNLQ TYKLWHLDPD TEYEISVLLT
RPGDGGTGRP GPPLISRTKC AEPTRAPKGL AFAEIQARQL TLQWEPLGYN VTRCHTYAVS
LCYRYTLGGS HNQTIRECVK MERGASRYTI KNLLPFRNIH VRLILTNPEG RKEGKEVTFQ
TDEDVPGGIA AESLTFTPLE DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR
RTISKLRNET YHVFSNLHPG TTYLFSVRAR TSKGFGQAAL TEITTNISAP SFDYADMPSP
LGESENTITV LLRPAQGRGA PISVYQVVVE EERPRRLRRE PGAQDCFSVP LTFETALARG
LVHYFGAELA ASSLLEAMPF TVGDNQTYRG FWNPPLEPRK AYLIYFQAAS HLKGETRLNC
IRIARKAACK ESKRPLEVSQ RSEEMGLILG ICAGGLAVLI LLLGAIIVII RKGRDRYAYS
YYPKPVNMTK ATVNYRQEKT HMMSAVDRSF TDQSTLQEDE RLGLSFMDAP GYSPRGDQRS
GGVTEASSLL GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES
FFEGWDATKK KDKLKGGRQE PVSAYDRHHV KLHPMLADPD ADYISANYID GYHRSNHFIA
TQGPKPEMIY DFWRMVWQEQ CASIVMITKL VEVGRVKCSR YWPEDSDMYG DIKITLVKTE
TLAEYVVRTF ALERRGYSAR HEVRQFHFTA WPEHGVPYHA TGLLAFIRRV KASTPPDAGP
IVIHCSAGTG RTGCYIVLDV MLDMAECEGV VDIYNCVKTL CSRRVNMIQT EEQYIFIHDA
ILEACLCGET TIPVNEFKAT YREMIRIDPQ SNSSQLREEF QTLNSVTPPL DVEECSIALL
PRNRDKNRSM DVLPPDRCLP FLISSDGDPN NYINAALTDS YTRSAAFIVT LHPLQSTTPD
FWRLVYDYGC TSIVMLNQLN QSNSAWPCLQ YWPEPGRQQY GLMEVEFVSG TANEDLVSRV
FRVQNSSRLQ EGHLLVRHFQ FLRWSAYRDT PDSRKAFLHL LAEVDKWQAE SGDGRTVVHC
LNGGGRSGTF CACATVLEMI RCHSLVDVFF AAKTLRNYKP NMVETMDQYH FCYDVALEYL
EALELR
