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Database: UniProt
Entry: F7CT12_CALJA
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ID   F7CT12_CALJA            Unreviewed;       653 AA.
AC   F7CT12;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=SSH3 {ECO:0000313|EMBL:JAB03582.1,
GN   ECO:0000313|Ensembl:ENSCJAP00000001640.2};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000001640.2, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000001640.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB03582.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Bladder {ECO:0000313|EMBL:JAB03582.1}, Cerebellum
RC   {ECO:0000313|EMBL:JAB49210.1}, Cerebral cortex
RC   {ECO:0000313|EMBL:JAB25845.1}, Hippocampus
RC   {ECO:0000313|EMBL:JAB15979.1}, and Skeletal muscle
RC   {ECO:0000313|EMBL:JAB35635.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
RN   [3] {ECO:0000313|Ensembl:ENSCJAP00000001640.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; GAMT01008279; JAB03582.1; -; mRNA.
DR   EMBL; GAMS01007157; JAB15979.1; -; mRNA.
DR   EMBL; GAMR01008087; JAB25845.1; -; mRNA.
DR   EMBL; GAMQ01006216; JAB35635.1; -; mRNA.
DR   EMBL; GAMP01003545; JAB49210.1; -; mRNA.
DR   RefSeq; XP_017833800.1; XM_017978311.1.
DR   STRING; 9483.ENSCJAP00000001640; -.
DR   Ensembl; ENSCJAT00000001743.4; ENSCJAP00000001640.2; ENSCJAG00000000956.5.
DR   GeneID; 100404317; -.
DR   CTD; 54961; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000160322; -.
DR   OMA; WATHYQE; -.
DR   OrthoDB; 5490735at2759; -.
DR   TreeFam; TF319444; -.
DR   Proteomes; UP000008225; Chromosome 11.
DR   Bgee; ENSCJAG00000000956; Expressed in liver and 6 other cell types or tissues.
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; cd14571; DSP_slingshot_3; 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; 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.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT   DOMAIN          269..324
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   DOMAIN          328..469
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          393..448
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..91
FT                   /note="Polar 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        516..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  72049 MW;  3BA53457EA1DD519 CRC64;
     MALVTVSRSP PGSGASTPVG PRDRGVQRRS RLQRRQSFAV LRGAVLGLQD GGDNDDAAEA
     SPEPSEEPPS EEQPRGDQTD LGQGPQSPQK QEEQRQHLHL MVQLLRAQDD IRLAAQLEAA
     RPPRLRYLLV VSTREGEGLS QDETVLLGVD FPDSSSPSCT LGLVLPLWSD TQVYLDGDGG
     FIVTSGGQSR IFKPISIQTM WATLQVLHQA CEAALGSGLV PGGSALTWAS HYQERLNSNQ
     SCLNEWTAMA DLESLRPPST EPGRPSEQEQ MEQAIRAELR QVLDASNLES VTSKEIRQAL
     ELRLGHPLQQ HRDFIDNQML LLVAQRDRAS RIFPHLYLGS EWNAANLEEL QRNRVTHILN
     MAREIDNFYP ERFTYHNVRL WDEESAQLLP HWKETYRFIE AARAQGTRVL VHCKMGVSRS
     AATVLAYAMK QYGCSLEQAL HHVQGLRPIA RPNPGFLRQL QVYQGILTAS RQSHVWEQKA
     GGVSPEEHPA PEVSTPFPPL PPEPGGGGEE KVVGMEESQA APKEEPGPRP RIDLRGVMRS
     ISLLEPSLEL ESTSDASDMP EVFSSPESSH EEPPQPFLQL ARTKGGQQVG RGPQPALKSR
     QSVVALQSAA LVASRTQAFQ EQRQGEPSIS STPRFRKVVR QASVDDSGEE GEA
//
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