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Database: UniProt
Entry: G5BVP5_HETGA
LinkDB: G5BVP5_HETGA
Original site: G5BVP5_HETGA 
ID   G5BVP5_HETGA            Unreviewed;      1384 AA.
AC   G5BVP5;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=GW7_08206 {ECO:0000313|EMBL:EHB13340.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB13340.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB13340.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
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; JH172092; EHB13340.1; -; Genomic_DNA.
DR   STRING; 10181.G5BVP5; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   InParanoid; G5BVP5; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
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; cd14569; DSP_slingshot_2; 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:SF3; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 2; 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:UP000006813}.
FT   DOMAIN          222..277
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   DOMAIN          281..422
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          346..400
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          586..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          984..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1041..1069
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1104..1141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1341..1384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..872
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..902
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1046..1069
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1104..1126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1384 AA;  155254 MW;  ED721D84FA66A5A8 CRC64;
     MPECRSQPRS ISESFLTVKG AALFLPRGNG SSTPRISHRR NKHAGDLQQH LQAMFILLRP
     EDNIRLAVRL ESTYQNRTRY MVVVSTNGRQ DTEESIVLGM DFSSNDSSTC TMGLVLPLWS
     DTLIHLDGDG GFSVSTDNRV HIFKPVSVQA MWSALQSLHK ACEVARMHNY YPGSLFLTWV
     SYYESHINSD QSSVNEWNAM QDVQSHRPDS PALFTDIPTE RERTERLIKT KLREIMMQKD
     LENITSKEIR TELEMQMVCN LREFKEFIDN EMIVILGQMD SPTQIFEHVF LGSEWNASNL
     EDLQNRGVRY ILNVTREIDN FFPGVFEYHN IRVYDEEATD LLAYWNDTYK FISKAKKHGS
     KCLVHCKMGV SRSASTVIAY AMKEYGWNLD RAYDYVKERR TVTKPNPSFM RQLEEYQGIL
     LASKQRHNKL WRSHSDSDLS DHHEPICKPG LELNKKEITT SADQIAEVKT LESHPSIPPV
     FVEHVVPQDT KERMICLEFT SREFHAGQIE DELNLNDING CSSGFCLNES KFPLDNCHAS
     KALIQPGQVP EMANKFPDLT VEDLETDALK ADINVHLLPM EELTSGLKDL PMSPDPESPS
     PQPSCQAEIS DFSTDRIDFF SALEKFVELS QETRSRSFSH SRMEELGGGR SESCRLSVVE
     VPPSEATTDD QRSSSLSNTP HASEESSMDE EQSKAISELI SPDIFIHSHS ENSISVKEIV
     TEIESISQGV GQMQLKGDMV SNPCHTPKKS TIHELSLERT QAPENKPGHM EQDEGFCPAQ
     PELAKDSGKC NPEDCLTTHS STVDLEEEEP TEGEHELWGP GMHSGAKWCP GSVRRATLEF
     EERLRQEQDH HSPAPVCTSM STRKNSKNDS SVADLAPKGK NDEATEYSFA PKEPEVSKGK
     GKCSKSEAGS LSQCEQNATV PALELLEYHP LAATQEYPRL DIRTKQGVPE EQGTVVPCQG
     SETQDILLPK RIEIIEYTHT VTSLSHTGSG GERATSKEKG DQGLRKVKVE KSVTMLCALD
     ENLNRTLDPS QLSLHPQMLP LLHSSPEQDR PTNPTSMLSS PEDRDNSPLT ALETTAPFIS
     HTTHILPANF DYLHPQTIVH LEGCTEQSST TDSEPSAEQV SWEESQKGHL SGGDEAPHKG
     SQLNCKDLNL ISKLDDNIGE LQKKLDPSQV AWRLPHSSSS ENIKGLSHSP GVVKERAKEI
     ESRVIFQVRI PKPSQMRRSA SLAKLGYLDL CKDCLPERES VSSESPHLKV LQPFIRTDSG
     MHAMEAQAPP ENLDATQNTE PTKYFVEPLK TTECIAQSKP VERPLVQYAK EFGYSQQCLL
     PRVRRELTSS EGGLPLLQTQ GLQDAGPAPG LAMAPRQQHG RTHPLRRLRT NDKKRTTNPF
     YNTM
//
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