ID A0A3B3TMK6_9TELE Unreviewed; 1030 AA.
AC A0A3B3TMK6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=SSH1 {ECO:0000313|Ensembl:ENSPLAP00000001526.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000001526.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000001526.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001482};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000256|ARBA:ARBA00009580}.
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DR RefSeq; XP_014874185.1; XM_015018699.1.
DR AlphaFoldDB; A0A3B3TMK6; -.
DR STRING; 48699.ENSPLAP00000001526; -.
DR Ensembl; ENSPLAT00000014589.1; ENSPLAP00000001526.1; ENSPLAG00000002603.1.
DR GeneID; 106937273; -.
DR KEGG; plai:106937273; -.
DR CTD; 101885659; -.
DR GeneTree; ENSGT00940000156133; -.
DR OrthoDB; 5490735at2759; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:InterPro.
DR CDD; cd11652; SSH-N; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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:SF5; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 1; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}.
FT DOMAIN 251..306
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 310..451
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 372..429
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 113254 MW; CF16FAD1B9CA6C15 CRC64;
MALVTLQRSP TPSAASTAST ATTTAGEDFG SDDERRINQS LSESFFMVKG AALFLQQGSS
QQGQKAHPPH KHAGELPQHL QVMINILRSE DRIKLAVRLE SAWSDRVRYM VVVYTSGRQD
TEENILLGID FTNKDCKSCS IGMVLPLWSD TKIHLDGDGG FTVNTAGRTH VFKPVSVQAM
WSALQVLHKA CEVSRRFNYF PGGMALTWMG YYESCIASEQ SCINEWNAMK DLETTRPDSP
IMFVDKPSER ERTECLIKSK LRSIMTSQDL ENVTCKQIRT KLEQHMNCNL KEYKEFIDNE
MLLILGQMDK ATLIFDHVYL GSEWNASNLE ELQETGVGYI LNVTREIDNF FPGTFCYHNI
RVYDEDATDL LAHWNNTYNF IMKAKKNDSK CLVHCKMGVS RSASTVIAYA MKEYGWSLEK
AYNFVKQKRN ITRPNAGFMR QLAEYEGILD ASKQRHNKLW HPDADCEMAE GQQGLTQFCG
GEDGGDPTAD PGMSPCCEEG SSNKGAACSS PCRTVALNID PAYNNYYFRR LSDSALDSEP
STPVRGPPLL GMEKVFIEIE DVERDALLDD EAFHGREGLP LPHFGPTAEG AAAQTCSRGP
EPLEELRLRL EFSTVEEENE EDVQKEEAEM EVLMQPDDRG GGEGDGGETQ DVEVEGDAEG
IGMDLASLND NSNNNNHLSL LQNHKDTSSS FLLQRDASLV SGSHQKERSS SPSSELRLTA
RPPSEVQSAS SRHSQTSTEG VSSSTGLLSP CGPQCDCANC ATCATALSSS EAQRSAEAQD
GSHLLQDGPS ESASDVLPEL MRADFEGETP AVACYLGQQQ ESLLQLRRSG LVRRRAERLE
RLSGMSLQEC QKSKMCPSHS EEKEEFSSFT GDFAKTSTPC QVRLEPLVVP LTNEALLGVV
GSGLLTPTSS PHGSTLTRSS SSDSLRSVRG KPGLVRQRAQ EIETRLRLAG LTVPSRLKRS
NSLAKLGSLN LSSDDLRSAC SSDAGTLLLL SLSPEPDQGL EWDSPTASSL SRPSKNLLTP
ERALPGEPRS
//