SSH3_HUMAN
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 03-AUG-2022, entry version 166.
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; 55.
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; Q8TE77; -.
DR PeptideAtlas; Q8TE77; -.
DR PRIDE; 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 Antibodypedia; 16449; 233 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 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; QSHIWEQ; -.
DR PhylomeDB; Q8TE77; -.
DR TreeFam; TF319444; -.
DR PathwayCommons; Q8TE77; -.
DR SignaLink; Q8TE77; -.
DR SIGNOR; Q8TE77; -.
DR BioGRID-ORCS; 54961; 12 hits in 1078 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 179 other tissues.
DR ExpressionAtlas; Q8TE77; baseline and differential.
DR Genevisible; Q8TE77; HS.
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:0030837; P:negative regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR CDD; cd11652; SSH-N; 1.
DR Gene3D; 3.90.190.10; -; 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; PTHR45864; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 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.
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
