ID PTN22_MOUSE Reviewed; 802 AA. AC P29352; Q7TMP9; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 24-JAN-2024, entry version 187. DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 22; DE EC=3.1.3.48 {ECO:0000269|PubMed:1373816, ECO:0000269|PubMed:27043286}; DE AltName: Full=Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP; DE AltName: Full=PEST-domain phosphatase; DE Short=PEP; GN Name=Ptpn22; Synonyms=Ptpn8; 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], CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY. RX PubMed=1373816; DOI=10.1128/mcb.12.5.2396-2405.1992; RA Matthews R.J., Bowne D.B., Flores E., Thomas M.L.; RT "Characterization of hematopoietic intracellular protein tyrosine RT phosphatases: description of a phosphatase containing an SH2 domain and RT another enriched in proline-, glutamic acid-, serine-, and threonine-rich RT sequences."; RL Mol. Cell. Biol. 12:2396-2405(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 495-789, FUNCTION, SUBCELLULAR LOCATION, AND RP INTERACTION WITH CSK. RC TISSUE=Splenocyte; RX PubMed=8890164; DOI=10.1002/j.1460-2075.1996.tb00871.x; RA Cloutier J.-F., Veillette A.; RT "Association of inhibitory tyrosine protein kinase p50csk with protein RT tyrosine phosphatase PEP in T cells and other hemopoietic cells."; RL EMBO J. 15:4909-4918(1996). RN [4] RP INTERACTION WITH LPXN. RX PubMed=15786712; DOI=10.1007/s11010-005-2149-6; RA Watanabe N., Amano N., Ishizuka H., Mashima K.; RT "Leupaxin binds to PEST domain tyrosine phosphatase PEP."; RL Mol. Cell. Biochem. 269:13-17(2005). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=16938887; DOI=10.1073/pnas.0601832103; RA Liu J., Wang L., Harvey-White J., Osei-Hyiaman D., Razdan R., Gong Q., RA Chan A.C., Zhou Z., Huang B.X., Kim H.Y., Kunos G.; RT "A biosynthetic pathway for anandamide."; RL Proc. Natl. Acad. Sci. U.S.A. 103:13345-13350(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634; SER-680 AND SER-687, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452 AND SER-687, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Spleen; 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). RN [8] RP FUNCTION, AND INTERACTION WITH TRAF3. RX PubMed=23871208; DOI=10.1016/j.immuni.2013.06.013; RA Wang Y., Shaked I., Stanford S.M., Zhou W., Curtsinger J.M., Mikulski Z., RA Shaheen Z.R., Cheng G., Sawatzke K., Campbell A.M., Auger J.L., Bilgic H., RA Shoyama F.M., Schmeling D.O., Balfour H.H. Jr., Hasegawa K., Chan A.C., RA Corbett J.A., Binstadt B.A., Mescher M.F., Ley K., Bottini N., RA Peterson E.J.; RT "The autoimmunity-associated gene PTPN22 potentiates toll-like receptor- RT driven, type 1 interferon-dependent immunity."; RL Immunity 39:111-122(2013). RN [9] RP FUNCTION. RX PubMed=23991106; DOI=10.1371/journal.pone.0072384; RA Spalinger M.R., Lang S., Vavricka S.R., Fried M., Rogler G., Scharl M.; RT "Protein tyrosine phosphatase non-receptor type 22 modulates NOD2-induced RT cytokine release and autophagy."; RL PLoS ONE 8:E72384-E72384(2013). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=27043286; DOI=10.1172/jci83669; RA Spalinger M.R., Kasper S., Gottier C., Lang S., Atrott K., Vavricka S.R., RA Scharl S., Raselli T., Frey-Wagner I., Gutte P.M., Gruetter M.G., RA Beer H.D., Contassot E., Chan A.C., Dai X., Rawlings D.J., Mair F., RA Becher B., Falk W., Fried M., Rogler G., Scharl M.; RT "NLRP3 tyrosine phosphorylation is controlled by protein tyrosine RT phosphatase PTPN22."; RL J. Clin. Invest. 126:1783-1800(2016). RN [11] RP STRUCTURE BY NMR OF 612-629 IN COMPLEX WITH CSK. RX PubMed=11685249; DOI=10.1038/nsb1101-998; RA Ghose R., Shekhtman A., Goger M.J., Ji H., Cowburn D.; RT "A novel, specific interaction involving the Csk SH3 domain and its natural RT ligand."; RL Nat. Struct. Biol. 8:998-1004(2001). CC -!- FUNCTION: Acts as a negative regulator of T-cell receptor (TCR) CC signaling by direct dephosphorylation of the Src family kinases LCK and CC FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and CC other key signaling molecules (By similarity). Associates with and CC probably dephosphorylates CBL (By similarity). Dephosphorylates LCK at CC its activating 'Tyr-394' residue (By similarity). Dephosphorylates CC ZAP70 at its activating 'Tyr-492' residue (By similarity). CC Dephosphorylates the immune system activator SKAP2 (By similarity). CC Positively regulates toll-like receptor (TLR)-induced type 1 interferon CC production (PubMed:23871208). Promotes host antiviral responses CC mediated by type 1 interferon (PubMed:23871208). Regulates NOD2-induced CC pro-inflammatory cytokine secretion and autophagy (PubMed:23991106). CC Acts as an activator of NLRP3 inflammasome assembly by mediating CC dephosphorylation of 'Tyr-861' of NLRP3 (PubMed:27043286). CC Dephosphorylates phospho-anandamide (p-AEA), an endocannabinoid to CC anandamide (also called N-arachidonoylethanolamide) (PubMed:16938887). CC {ECO:0000250|UniProtKB:Q9Y2R2, ECO:0000269|PubMed:16938887, CC ECO:0000269|PubMed:23871208, ECO:0000269|PubMed:23991106, CC ECO:0000269|PubMed:27043286}. 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, ECO:0000269|PubMed:1373816, CC ECO:0000269|PubMed:27043286}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine CC phosphate = N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + CC phosphate; Xref=Rhea:RHEA:56532, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:131894; CC Evidence={ECO:0000269|PubMed:16938887}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56533; CC Evidence={ECO:0000305|PubMed:16938887}; CC -!- SUBUNIT: Interacts with CBL (By similarity). Interacts with CSK CC (PubMed:8890164, PubMed:11685249). Interacts with LPXN CC (PubMed:15786712). Interacts with TRAF3 (via MATH domain); the CC interaction promotes TRAF3 polyubiquitination (PubMed:23871208). CC {ECO:0000250|UniProtKB:Q9Y2R2, ECO:0000269|PubMed:11685249, CC ECO:0000269|PubMed:15786712, ECO:0000269|PubMed:23871208, CC ECO:0000269|PubMed:8890164}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8890164}. CC -!- TISSUE SPECIFICITY: Brain (at protein level) (PubMed:16938887). Spleen, CC thymus, lymph node and bone marrow (PubMed:1373816). CC {ECO:0000269|PubMed:1373816, ECO:0000269|PubMed:16938887}. CC -!- INDUCTION: By lipopolysaccharides (LPS). {ECO:0000269|PubMed:16938887}. CC -!- PTM: Phosphorylation on Ser-35 by PKC/PRKCD abrogates its ability to CC dephosphorylate and inactivate the SRC family kinases. CC {ECO:0000250|UniProtKB:Q9Y2R2}. CC -!- DISRUPTION PHENOTYPE: Knockout reduces the conversion of CC phosphoanandamide (p-AEA) to AEA in the brain. CC {ECO:0000269|PubMed:16938887}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class 4 subfamily. {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; M90388; AAA39994.1; -; mRNA. DR EMBL; BC055377; AAH55377.1; -; mRNA. DR CCDS; CCDS38577.1; -. DR PIR; B44390; B44390. DR RefSeq; NP_033005.1; NM_008979.2. DR RefSeq; XP_006501211.1; XM_006501148.3. DR RefSeq; XP_006501212.1; XM_006501149.3. DR RefSeq; XP_006501213.1; XM_006501150.2. DR RefSeq; XP_011238343.1; XM_011240041.2. DR RefSeq; XP_011238344.1; XM_011240042.2. DR PDB; 1JEG; NMR; -; B=605-629. DR PDBsum; 1JEG; -. DR AlphaFoldDB; P29352; -. DR SMR; P29352; -. DR ELM; P29352; -. DR IntAct; P29352; 3. DR MINT; P29352; -. DR STRING; 10090.ENSMUSP00000029433; -. DR ChEMBL; CHEMBL2157855; -. DR SwissLipids; SLP:000001911; -. DR iPTMnet; P29352; -. DR PhosphoSitePlus; P29352; -. DR EPD; P29352; -. DR jPOST; P29352; -. DR MaxQB; P29352; -. DR PaxDb; 10090-ENSMUSP00000029433; -. DR ProteomicsDB; 291630; -. DR Antibodypedia; 33846; 359 antibodies from 34 providers. DR DNASU; 19260; -. DR Ensembl; ENSMUST00000029433.9; ENSMUSP00000029433.8; ENSMUSG00000027843.14. DR GeneID; 19260; -. DR KEGG; mmu:19260; -. DR UCSC; uc008qtv.2; mouse. DR AGR; MGI:107170; -. DR CTD; 26191; -. DR MGI; MGI:107170; Ptpn22. DR VEuPathDB; HostDB:ENSMUSG00000027843; -. DR eggNOG; KOG0789; Eukaryota. DR GeneTree; ENSGT00940000160958; -. DR HOGENOM; CLU_015557_1_0_1; -. DR InParanoid; P29352; -. DR OMA; MMNQQSK; -. DR OrthoDB; 5489271at2759; -. DR PhylomeDB; P29352; -. DR TreeFam; TF351977; -. DR Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse. DR BioGRID-ORCS; 19260; 2 hits in 78 CRISPR screens. DR ChiTaRS; Ptpn22; mouse. DR EvolutionaryTrace; P29352; -. DR PRO; PR:P29352; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; P29352; Protein. DR Bgee; ENSMUSG00000027843; Expressed in thymus and 94 other cell types or tissues. DR ExpressionAtlas; P29352; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL. DR GO; GO:0019900; F:kinase binding; IPI:BHF-UCL. DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IBA:GO_Central. DR GO; GO:0016791; F:phosphatase activity; ISO:MGI. DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB. DR GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0071225; P:cellular response to muramyl dipeptide; IDA:UniProtKB. DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:MGI. DR GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB. DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:UniProtKB. DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IMP:UniProtKB. DR GO; GO:0070433; P:negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:UniProtKB. DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IMP:UniProtKB. DR GO; GO:0050868; P:negative regulation of T cell activation; IMP:BHF-UCL. DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB. DR GO; GO:0035644; P:phosphoanandamide dephosphorylation; IDA:BHF-UCL. DR GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; IMP:UniProtKB. DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0071663; P:positive regulation of granzyme B production; IMP:UniProtKB. DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IMP:UniProtKB. DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB. DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB. DR GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; IMP:UniProtKB. DR GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; IMP:UniProtKB. DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IMP:UniProtKB. DR GO; GO:0034157; P:positive regulation of toll-like receptor 7 signaling pathway; IMP:UniProtKB. DR GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; IMP:UniProtKB. DR GO; GO:0032481; P:positive regulation of type I interferon production; ISO:MGI. DR GO; GO:0032729; P:positive regulation of type II interferon production; ISO:MGI. DR GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB. DR GO; GO:1903169; P:regulation of calcium ion transmembrane transport; ISO:MGI. DR GO; GO:0002685; P:regulation of leukocyte migration; IMP:UniProtKB. DR GO; GO:0032817; P:regulation of natural killer cell proliferation; ISS:BHF-UCL. DR GO; GO:1901222; P:regulation of non-canonical NF-kappaB signal transduction; IMP:UniProtKB. DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:MGI. DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI. DR GO; GO:0030217; P:T cell differentiation; IMP:MGI. DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI. DR CDD; cd14602; PTPc-N22; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR047170; PTN12/18/22. DR InterPro; IPR047253; PTN22_cat. DR InterPro; IPR000242; PTP_cat. DR InterPro; IPR016276; PTPN22. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; Tyr_Pase_dom. DR PANTHER; PTHR45983; TYROSINE PHOSPHATSE N18, PUTATIVE-RELATED; 1. DR PANTHER; PTHR45983:SF1; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 22; 1. DR Pfam; PF00102; Y_phosphatase; 1. DR PIRSF; PIRSF000930; PTPN8_PTPN22; 1. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00194; PTPc; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. DR Genevisible; P29352; MM. PE 1: Evidence at protein level; KW 3D-structure; Autophagy; Cytoplasm; Hydrolase; Immunity; Lipid metabolism; KW Phosphoprotein; Protein phosphatase; Reference proteome. FT CHAIN 1..802 FT /note="Tyrosine-protein phosphatase non-receptor type 22" FT /id="PRO_0000094776" FT DOMAIN 24..289 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 330..358 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 536..564 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 597..619 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 613..621 FT /note="Interaction with CSK" FT /evidence="ECO:0000269|PubMed:8890164" FT REGION 653..695 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 713..802 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 334..358 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 653..674 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 713..783 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 227 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160, FT ECO:0000255|PROSITE-ProRule:PRU10044" FT BINDING 227..233 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9Y2R2" FT BINDING 274 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q9Y2R2" FT MOD_RES 35 FT /note="Phosphoserine; by PKC/PRKCD" FT /evidence="ECO:0000250|UniProtKB:Q9Y2R2" FT MOD_RES 452 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 634 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT MOD_RES 680 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT MOD_RES 687 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT CONFLICT 91 FT /note="K -> Q (in Ref. 2; AAH55377)" FT /evidence="ECO:0000305" FT CONFLICT 141 FT /note="R -> H (in Ref. 2; AAH55377)" FT /evidence="ECO:0000305" FT HELIX 621..624 FT /evidence="ECO:0007829|PDB:1JEG" SQ SEQUENCE 802 AA; 89714 MW; 0F1E45339BD4613E CRC64; MDQREILQQL LKEAQKKKLN SEEFASEFLK LKRQSTKYKA DKIYPTTVAQ RPKNIKKNRY KDILPYDHSL VELSLLTSDE DSSYINASFI KGVYGPKAYI ATQGPLSTTL LDFWRMIWEY RILVIVMACM EFEMGKKKCE RYWAEPGETQ LQFGPFSISC EAEKKKSDYK IRTLKAKFNN ETRIIYQFHY KNWPDHDVPS SIDPILQLIW DMRCYQEDDC VPICIHCSAG CGRTGVICAV DYTWMLLKDG IIPKNFSVFN LIQEMRTQRP SLVQTQEQYE LVYSAVLELF KRHMDVISDN HLGREIQAQC SIPEQSLTVE ADSCPLDLPK NAMRDVKTTN QHSKQGAEAE STGGSSLGLR TSTMNAEEEL VLHSAKSSPS FNCLELNCGC NNKAVITRNG QARASPVVGE PLQKYQSLDF GSMLFGSCPS ALPINTADRY HNSKGPVKRT KSTPFELIQQ RKTNDLAVGD GFSCLESQLH EHYSLRELQV QRVAHVSSEE LNYSLPGACD ASCVPRHSPG ALRVHLYTSL AEDPYFSSSP PNSADSKMSF DLPEKQDGAT SPGALLPASS TTSFFYSNPH DSLVMNTLTS FSPPLNQETA VEAPSRRTDD EIPPPLPERT PESFIVVEEA GEPSPRVTES LPLVVTFGAS PECSGTSEMK SHDSVGFTPS KNVKLRSPKS DRHQDGSPPP PLPERTLESF FLADEDCIQA QAVQTSSTSY PETTENSTSS KQTLRTPGKS FTRSKSLKIF RNMKKSVCNS SSPSKPTERV QPKNSSSFLN FGFGNRFSKP KGPRNPPSAW NM //