PTN22_MOUSE
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 03-AUG-2022, entry version 179.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 22;
DE EC=3.1.3.48 {ECO:0000269|PubMed:1373816};
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 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 negative regulator of T-cell receptor (TCR) signaling
CC by direct dephosphorylation of the Src family kinases LCK and FYN,
CC ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key
CC signaling molecules (By similarity). Associates with and probably
CC dephosphorylates CBL (By similarity). Dephosphorylates LCK at its
CC activating 'Tyr-394' residue (By similarity). Dephosphorylates ZAP70 at
CC its activating 'Tyr-492' residue (By similarity). Dephosphorylates the
CC immune system activator SKAP2 (By similarity). Positively regulates
CC toll-like receptor (TLR)-induced type 1 interferon production
CC (PubMed:23871208). Promotes host antiviral responses mediated by type 1
CC interferon (PubMed:23871208). Regulates NOD2-induced pro-inflammatory
CC cytokine secretion and autophagy (PubMed:23991106). Dephosphorylates
CC phospho-anandamide (p-AEA), an endocannabinoid to anandamide (also
CC called N-arachidonoylethanolamide) (PubMed:16938887).
CC {ECO:0000250|UniProtKB:Q9Y2R2, ECO:0000269|PubMed:16938887,
CC ECO:0000269|PubMed:23871208, ECO:0000269|PubMed:23991106}.
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 -!- 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}.
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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; P29352; -.
DR PRIDE; P29352; -.
DR ProteomicsDB; 291630; -.
DR Antibodypedia; 33846; 310 antibodies from 34 providers.
DR DNASU; 19260; -.
DR Ensembl; ENSMUST00000029433; ENSMUSP00000029433; ENSMUSG00000027843.
DR GeneID; 19260; -.
DR KEGG; mmu:19260; -.
DR UCSC; uc008qtv.2; mouse.
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; LELNYDC; -.
DR OrthoDB; 411281at2759; -.
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 73 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 91 other tissues.
DR ExpressionAtlas; P29352; baseline and differential.
DR Genevisible; P29352; MM.
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; ISS: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:0043508; P:negative regulation of JUN kinase activity; ISO:MGI.
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:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GO_Central.
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:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
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: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 NIK/NF-kappaB signaling; 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 Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
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 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; SSF52799; 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; 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 195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227..233
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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
