ID A0A2T7PDF2_POMCA Unreviewed; 1461 AA.
AC A0A2T7PDF2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=C0Q70_06859 {ECO:0000313|EMBL:PVD31447.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD31447.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD31447.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD31447.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD31447.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD31447.1}.
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DR EMBL; PZQS01000004; PVD31447.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7PDF2; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg4.
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 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:SF2; PROTEIN PHOSPHATASE SLINGSHOT; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT DOMAIN 216..271
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 275..416
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 337..394
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 67..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1461 AA; 160482 MW; EEB9BC9250B10E5D CRC64;
MCMGIFVVGR EIQRHLQSML YILRPEDKIK VAIRLEGMRE GEHRYMALVS TIGRQDTEES
VILGLDCGTP GSSGTPSPSP VSPVSPVQTT EAGAVLPGHT WLHSATVGLV LPIWMGMKAR
LSGDGGFSIS VDDKSYLFKP VSVQAMWSAI QSLDKSFHIA EQLKYLPEGL THTWVEYYRS
KMDFTDHNRL SIWHQMEDVE VFAPSCLSYK EENESEKLKL VISAKLKEVM MSVDLDEATS
KFLRTEVEKA LGMNLDQYLN YFDEETLRIL GQMDAPSQIL DFLYLGSEWN ASNLEELQRL
GIKYILNVTR EIDNFFTGLF HYCNVRLYDH EDSELMKHWL KTYKFINKAK KHDSKVLVHC
KMGISRSAST VMAYLMKENC WPLDKAFTFV KDRRSCVRPN KGFMEQLQTY EGILNASNMR
KVFLAESEQM FEDESEEGES ERNQQGNFLG DSLFQVMVHS DWPQGEATTE ETTLLRKSYD
NNHEFSGMEA DLETRSADSL EESAADMSFP MLDFTLQADS PTLSVTSAPD FGGDGSTQTK
LTAQRYGDAP GWPGAKEVQL TSRIRPDHSW IKLECSGESS TDITLSEPGA PEGMALQTDL
VLASAADGSP CHRLLPPSSS SGRVASPSLG ISSSNSQGSM RLASLDDAHK IKPDSSWIRL
YSPGESSTDV EEMDTTEAYQ EDASTGDVGR IGSLQDSRPV QFVLGEDEEM TPAVSSPLKI
YAGGKGEGGV LGVDKSTGET LGPRDNSQQV QGVEMGVQQY YSREQIPWSK GKVRNLLIGL
QQGGQMLAVS TEEGQAGLNN RPHQARDEDP CFSESLGMTD MAPMQMLHCQ SCMELSYSQS
EAVDLQDRPS SVNDEQEEIF PTPGTVRRTL QEIEERNRLH KGETIYGMKG VQRSSSFKEG
LSKSSAHNRQ SERRWTCTPI LSPDHSSEDL EGQGFMIATA PVNLGLTTVD SSKDAVKAGT
DMVVDDQQDP VRVYTYKEDA VPVKLGTVWR HTLEIESKAG DGNGRPRALS ESSGGSSDSG
AQVTGSWSPI HGQSPRRNPD IPVLNISLMT SNIPEAKSQR TSSLQQSCVE KPQHAGSAGV
EPECLSSSVQ DNRGLSSSSF RNGDESSTHG KGVMPLGWSF KTEAEDQKKS VSSLSPSTSS
APRKNKGNFD SETLALIREI GSAFVATPTT GKFDDGGGAA KLGLVRHLVK NIEKETNIGK
RERKIVIISK DSAPGQKGVK SESQDCVKSS GPEHQEKRDS QTDMSPEKLV RSSGKSSPEV
LGQSSPHIDE HPPSVVRHLR GKFETRCHAG DGVDDETLTG TVPSIVSNVF QQGDIVCDIP
VVLQERKHDP SGLIMTGIAK AKSFDEQSLD FLAGDLRLQG MQPVMRDQPV SSCTSTQPSR
RPCSANNSSG EGGLAHRYST GGCTTSHFKQ HEERAEDERG GEEVYPAKKL YGKSHPLSKL
QPYQGDCTVS PSPGSRFYPT M
//
