ID A0A2I3NFM9_PAPAN Unreviewed; 1347 AA.
AC A0A2I3NFM9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=SSH2 {ECO:0000313|Ensembl:ENSPANP00000046709.2};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000046709.2, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000046709.2, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000046709.2}
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 Ensembl; ENSPANT00000038352.2; ENSPANP00000046709.2; ENSPANG00000023181.3.
DR GeneTree; ENSGT00940000157430; -.
DR Proteomes; UP000028761; Chromosome 17.
DR Bgee; ENSPANG00000023181; Expressed in thymus and 68 other cell types or tissues.
DR ExpressionAtlas; A0A2I3NFM9; baseline.
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 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: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:UP000028761}.
FT DOMAIN 172..227
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 231..372
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 296..350
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 545..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1347 AA; 149740 MW; A01A2016E925D946 CRC64;
MAHPHQESAT DGTNMQAVRL ESTYQNRTRY MVVVSTNGRQ DTEESIVLGM DFSSNDSSTC
TMGLVLPLWS DTLIHLDGDG GFSVSTDNRV HIFKPVSVQA MWSALQSLHK ACEVARAHNY
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
MESHPPIPPV FVEHVVPQDA NQKGLCTKER MICLEFTSTE FHAGQIEDEL NLNDINGCSS
GCCLNESKFP LDNCHASKAL IQPGHVPEMA NKFPDLTVED LETDALKADM NVHLLPMEEL
TSRLKDLPMS PDPESPSPQP SCQTEISDFS TDRIDFFSAL EKFVELSQET RSRSFSHSRM
EELGGGRSES CRLSVVEVAP SKVTTDDQRS SSLSNTPHAS EESSMDEEQS KAISELVSPD
IFMQSHLENA ISVKEIVTEI ESISQGVGQI QLKGDILSNP CHTPKKNSIH ELLFERAQTP
ENKPGHLEQD EGSCTAQPEL AKDSGMCNPE GCLTTRSSTA DLEEGEPAEG EQELQGSGMH
PGAKWYPGSV RRATLEFEER LRQEQEHHGA ASTCTSLSTR KNSKNDSSVA DLAPKGKSDE
ATPEHSFVPR EPEMSKGKGK YSGPEAGSLS HSEQNATVPA PKVLGFDHLP APQEGPGSDT
GTQQEGVLKD LRTVIPYQES ETQAVPLRLP KRVEIIEYTH TVTSPNHTGP GSEIATGEKS
GEQGLRKVNV EKSVTVLCTL DENLNRTLDP NQVSLHPQVL PPPHSSSPEH NRPTDHRTST
LSSPEDRGSS LSTALETAAP FVSHTTHLLS ASLDYLHPQT MVHLEGFTEQ SSTTDEPSAE
QVSWEESQDS PLSSGSEVPY KDSQLSSADL SLISKLGDNT GELQEKLDPL PVACRLPHST
SSENINGLSH SPGVVKERAK EIESRVVFQA GLTKPSQMRR SASLAKLGYL DLCKDCLPER
EPASCESPHL KLLQPFLRTD SGMHAMEDQE SLENPGAPHN PEPTKYFVEQ LTTTECIVQS
KPVERPLVQY AKEFGSSQQC LLPRAGPELT SSEGGLPMLQ TQGLQCACPA PGLAVAPRQQ
HGRTHPLRRL KKANDKKRTT NPFYNTM
//
