ID SSH3_HUMAN Reviewed; 659 AA. AC Q8TE77; Q6PK42; Q76I75; Q8N9L8; Q8WYL0; Q9NV45; Q9NWZ7; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 2. DT 27-MAR-2024, entry version 175. DE RecName: Full=Protein phosphatase Slingshot homolog 3; DE EC=3.1.3.16; DE EC=3.1.3.48; DE AltName: Full=SSH-like protein 3; DE Short=SSH-3L; DE Short=hSSH-3L; GN Name=SSH3; Synonyms=SSH3L; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=11832213; DOI=10.1016/s0092-8674(01)00638-9; RA Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T.; RT "Control of actin reorganization by Slingshot, a family of phosphatases RT that dephosphorylate ADF/cofilin."; RL Cell 108:233-246(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=14531860; DOI=10.1046/j.1365-2443.2003.00678.x; RA Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A., Shima Y., RA Niwa R., Uemura T., Mizuno K.; RT "Differential activities, subcellular distribution and tissue expression RT patterns of three members of Slingshot family phosphatases that RT dephosphorylate cofilin."; RL Genes Cells 8:811-824(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5). RC TISSUE=Cerebellum, and Ovarian carcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-87, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-37, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-37 AND SER-87, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Protein phosphatase which may play a role in the regulation CC of actin filament dynamics. Can dephosphorylate and activate the actin CC binding/depolymerizing factor cofilin, which subsequently binds to CC actin filaments and stimulates their disassembly (By similarity). CC {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 -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC -!- SUBUNIT: Does not bind to, or colocalize with, filamentous actin. CC {ECO:0000250}. CC -!- INTERACTION: CC Q8TE77; O43639: NCK2; NbExp=3; IntAct=EBI-8743776, EBI-713635; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=L; CC IsoId=Q8TE77-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8TE77-2; Sequence=VSP_016335, VSP_016336; CC Name=3; CC IsoId=Q8TE77-3; Sequence=VSP_016331, VSP_016332; CC Name=4; CC IsoId=Q8TE77-4; Sequence=VSP_016333; CC Name=5; CC IsoId=Q8TE77-5; Sequence=VSP_016330, VSP_016334, VSP_016335, CC VSP_016336; CC -!- MISCELLANEOUS: Tyrosine phosphatase activity has not been demonstrated CC for this protein to date. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC {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; AB072360; BAB84119.3; -; mRNA. DR EMBL; AB099291; BAC97814.1; -; mRNA. DR EMBL; AK000522; BAA91228.1; -; mRNA. DR EMBL; AK001790; BAA91913.1; -; mRNA. DR EMBL; AK074432; BAB85080.1; -; mRNA. DR EMBL; AK094226; BAC04314.1; -; mRNA. DR EMBL; BC007709; AAH07709.1; -; mRNA. DR CCDS; CCDS8157.1; -. [Q8TE77-1] DR RefSeq; NP_060327.3; NM_017857.3. [Q8TE77-1] DR AlphaFoldDB; Q8TE77; -. DR SMR; Q8TE77; -. DR BioGRID; 120299; 79. DR IntAct; Q8TE77; 26. DR MINT; Q8TE77; -. DR STRING; 9606.ENSP00000312081; -. DR DEPOD; SSH3; -. DR GlyGen; Q8TE77; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8TE77; -. DR PhosphoSitePlus; Q8TE77; -. DR BioMuta; SSH3; -. DR DMDM; 82582268; -. DR CPTAC; CPTAC-591; -. DR CPTAC; CPTAC-592; -. DR EPD; Q8TE77; -. DR jPOST; Q8TE77; -. DR MassIVE; Q8TE77; -. DR MaxQB; Q8TE77; -. DR PaxDb; 9606-ENSP00000312081; -. DR PeptideAtlas; Q8TE77; -. DR ProteomicsDB; 74414; -. [Q8TE77-1] DR ProteomicsDB; 74415; -. [Q8TE77-2] DR ProteomicsDB; 74416; -. [Q8TE77-3] DR ProteomicsDB; 74417; -. [Q8TE77-4] DR ProteomicsDB; 74418; -. [Q8TE77-5] DR Pumba; Q8TE77; -. DR Antibodypedia; 16449; 265 antibodies from 32 providers. DR DNASU; 54961; -. DR Ensembl; ENST00000308127.9; ENSP00000312081.4; ENSG00000172830.13. [Q8TE77-1] DR Ensembl; ENST00000376757.9; ENSP00000365948.6; ENSG00000172830.13. [Q8TE77-3] DR Ensembl; ENST00000532881.5; ENSP00000431788.2; ENSG00000172830.13. [Q8TE77-2] DR GeneID; 54961; -. DR KEGG; hsa:54961; -. DR MANE-Select; ENST00000308127.9; ENSP00000312081.4; NM_017857.4; NP_060327.3. DR UCSC; uc001okj.4; human. [Q8TE77-1] DR AGR; HGNC:30581; -. DR CTD; 54961; -. DR DisGeNET; 54961; -. DR GeneCards; SSH3; -. DR HGNC; HGNC:30581; SSH3. DR HPA; ENSG00000172830; Low tissue specificity. DR MIM; 606780; gene. DR neXtProt; NX_Q8TE77; -. DR OpenTargets; ENSG00000172830; -. DR PharmGKB; PA134929326; -. DR VEuPathDB; HostDB:ENSG00000172830; -. DR eggNOG; KOG1716; Eukaryota. DR GeneTree; ENSGT00940000160322; -. DR HOGENOM; CLU_006650_3_1_1; -. DR InParanoid; Q8TE77; -. DR OMA; WATHYQE; -. DR OrthoDB; 5490735at2759; -. DR PhylomeDB; Q8TE77; -. DR TreeFam; TF319444; -. DR PathwayCommons; Q8TE77; -. DR SignaLink; Q8TE77; -. DR SIGNOR; Q8TE77; -. DR BioGRID-ORCS; 54961; 14 hits in 1179 CRISPR screens. DR ChiTaRS; SSH3; human. DR GeneWiki; SSH3; -. DR GenomeRNAi; 54961; -. DR Pharos; Q8TE77; Tbio. DR PRO; PR:Q8TE77; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q8TE77; Protein. DR Bgee; ENSG00000172830; Expressed in lower esophagus mucosa and 181 other cell types or tissues. DR ExpressionAtlas; Q8TE77; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IBA:GO_Central. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro. DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IBA:GO_Central. DR CDD; cd14571; DSP_slingshot_3; 1. DR CDD; cd11652; SSH-N; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR014876; DEK_C. DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom. DR InterPro; IPR043587; Phosphatase_SSH-like. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR043588; SSH-N. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR000387; Tyr_Pase_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR45864:SF4; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 3; 1. DR PANTHER; PTHR45864; SLINGSHOT PROTEIN PHOSPHATASE HOMOLOG; 1. DR Pfam; PF08766; DEK_C; 1. DR Pfam; PF00782; DSPc; 1. DR SMART; SM00195; DSPc; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR SUPFAM; SSF109715; DEK C-terminal domain; 1. DR PROSITE; PS51998; DEK_C; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. DR Genevisible; Q8TE77; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; Hydrolase; KW Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q8K330" FT CHAIN 2..659 FT /note="Protein phosphatase Slingshot homolog 3" FT /id="PRO_0000094845" FT DOMAIN 269..324 FT /note="DEK-C" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342" FT DOMAIN 328..469 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 46..96 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 482..534 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 547..603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 617..638 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 60..78 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 491..505 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 509..530 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 547..563 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 617..635 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 413 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q8K330" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 37 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 85 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 87 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..330 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016330" FT VAR_SEQ 1..146 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016331" FT VAR_SEQ 147..154 FT /note="LGVDFPDS -> MAFPLSPA (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016332" FT VAR_SEQ 283..547 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016333" FT VAR_SEQ 331..360 FT /note="RIFPHLYLGSEWNAANLEELQRNRVTHILN -> MEGTMMMQQRPVLSQQHP FT SFILNSSPAHSP (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016334" FT VAR_SEQ 470..471 FT /note="SR -> RT (in isoform 2 and isoform 5)" FT /evidence="ECO:0000303|PubMed:11832213, FT ECO:0000303|PubMed:14702039" FT /id="VSP_016335" FT VAR_SEQ 472..659 FT /note="Missing (in isoform 2 and isoform 5)" FT /evidence="ECO:0000303|PubMed:11832213, FT ECO:0000303|PubMed:14702039" FT /id="VSP_016336" FT VARIANT 239 FT /note="E -> V (in dbSNP:rs7114712)" FT /id="VAR_057132" FT VARIANT 600 FT /note="R -> H (in dbSNP:rs1573536)" FT /id="VAR_057133" FT CONFLICT 58 FT /note="A -> V (in Ref. 1 and 2)" FT /evidence="ECO:0000305" FT CONFLICT 509 FT /note="E -> G (in Ref. 3; BAC04314)" FT /evidence="ECO:0000305" FT CONFLICT 641 FT /note="F -> S (in Ref. 3; BAB85080)" FT /evidence="ECO:0000305" SQ SEQUENCE 659 AA; 72996 MW; 0D96F86EAFE81D3B CRC64; MALVTVSRSP PGSGASTPVG PWDQAVQRRS RLQRRQSFAV LRGAVLGLQD GGDNDDAAEA SSEPTEKAPS EEELHGDQTD FGQGSQSPQK QEEQRQHLHL MVQLLRPQDD IRLAAQLEAP RPPRLRYLLV VSTREGEGLS QDETVLLGVD FPDSSSPSCT LGLVLPLWSD TQVYLDGDGG FSVTSGGQSR IFKPISIQTM WATLQVLHQA CEAALGSGLV PGGSALTWAS HYQERLNSEQ SCLNEWTAMA DLESLRPPSA EPGGSSEQEQ MEQAIRAELW KVLDVSDLES VTSKEIRQAL ELRLGLPLQQ YRDFIDNQML LLVAQRDRAS RIFPHLYLGS EWNAANLEEL QRNRVTHILN MAREIDNFYP ERFTYHNVRL WDEESAQLLP HWKETHRFIE AARAQGTHVL VHCKMGVSRS AATVLAYAMK QYECSLEQAL RHVQELRPIA RPNPGFLRQL QIYQGILTAS RQSHVWEQKV GGVSPEEHPA PEVSTPFPPL PPEPEGGGEE KVVGMEESQA APKEEPGPRP RINLRGVMRS ISLLEPSLEL ESTSETSDMP EVFSSHESSH EEPLQPFPQL ARTKGGQQVD RGPQPALKSR QSVVTLQGSA VVANRTQAFQ EQEQGQGQGQ GEPCISSTPR FRKVVRQASV HDSGEEGEA //