ID H2NT70_PONAB Unreviewed; 1429 AA.
AC H2NT70;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 61.
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:ENSPPYP00000009138.2};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000009138.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000009138.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000009138.2}
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 Ensembl; ENSPPYT00000009508.2; ENSPPYP00000009138.2; ENSPPYG00000008128.2.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000157430; -.
DR HOGENOM; CLU_006650_0_0_1; -.
DR InParanoid; H2NT70; -.
DR TreeFam; TF319444; -.
DR Proteomes; UP000001595; Chromosome 17.
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:UP000001595}.
FT DOMAIN 254..309
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 313..454
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 378..432
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 625..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1429 AA; 158857 MW; 25D582BB61891637 CRC64;
MTLSTLARKR KAPLACTCSL GGPDMIPYFS ANAVISQNAI NQLISESFLT VKGAALFLPR
GNGSSTPRIS HRRNKHAGDL QQHLQAMFIL LRPEDNIRLA VRLESTYQNR TRYMVVVSTN
GRQDTEESIV LGMDFSSNDS TCTMGLVLPL WSDTLIHLDG DGGFSVSTDN RVHIFKPVSV
QAMWSALQSL HKACEVARAH NYYPGSLFLT WVSYYESHIN SDQSSVNEWN AMQDVQSHRP
DSPALFTDIP TERERTERLI KTKLREIMMQ KDLENITSKE IRTELEMQMV CNLREFKEFI
DNEMIVILGQ MDSPTQIFEH VFLGSEWNAS NLEDLQNRGV RYILNVTREI DNFFPGVFEY
HNIRVYDEEA TDLLAYWNDT YKFISKAKKH GSKCLVHCKM GVSRSASTVI AYAMKEYGWN
LDRAYDYVKE RRTVTKPNPS FMRQLEEYQG ILLASKQRHN KLWRSHSDSD LSDHHEPICK
PGLELNKKEI TTSADQIAEV KTVESHPPIP PVFVEHMVPQ DANQKGLCTK ERMICLEFTS
REFHAGQIED ELNLNDINGC SSGCCLNESK FPLDNCHASK ALIQPGHVPE MANKFPDLTV
EDLETDALKA DMNVHLLPME ELTSPLKDLP MSPDPESPSP QPSCQTEISD FSTDRIDFFS
ALEKFVELSQ ETRSRSFSHS RMEELGGGRS ENCRLSVVEV APSKVTADDQ RSSSLSNTPH
ASEESSMDEE QSKAISELVS PDIFMQSHSE NAISVKEIVT EIESISQGVG QIQLKGDILP
NPCHTPKKNS IHELLLERAQ TPENKPGHKE QDEGSCTAQP ELAKDSGMCN PEGCLTTHSS
IADLEEGEPA EGEQELQGSG MHPGAKWYPG SVRRATLEFE ERLRQEQEHH GAAPTCTSLS
TRKNSKNDSS VADLAPKGKS DEAPPEHSFI LKEPEMSKGK GKYSGSEAGS LSHSEQNATV
PAPKVLEFDH LPAPQEGPGS DTGTQQEGVL KDLRTVIPYQ ESETQAVPLP LPKRVEIIEY
THIVTSPNHT GPGSEIATGE KSGEQGLRKV NMEKSVTVLC TLDENLNRTL DPNQVSLHPQ
VLPLPHSSSP ERNRPTDHPT SILSSPEDRG SSLSTALETA APFVSHTTHL LSASLDYLHP
QTMVHLEGFT EQSSTTDEPS AEQVSWEESQ ESPLSSGSEV PYKDSQLSSA DLSLISKLGD
NTGELQEKMD PLPVACRLPH SSSSENIKSL SHSPGVVKER AKEIESRVVF QAGLTKPSQM
RRSASLAKLG YLDLCKDCLP EREPASCESP HLKLLKPFLR TDSGMHAMED QESLENPGAP
HNPEPTKYFV EQLTTTECIV QSKPVERLLV QYAKEFGSSQ QCLLPRAGPE LTSSEGGLPV
LQTQGLQCAY PAPGLAVAPR QQHGRTHPLR RLKKANDKKR TTNPFYNTM
//
