ID A0A455BXN0_PHYMC Unreviewed; 1246 AA.
AC A0A455BXN0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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|RefSeq:XP_028353774.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028353774.1};
RN [1] {ECO:0000313|RefSeq:XP_028353774.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028353774.1};
RG RefSeq;
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 RefSeq; XP_028353774.1; XM_028497973.2.
DR AlphaFoldDB; A0A455BXN0; -.
DR OrthoDB; 5490735at2759; -.
DR Proteomes; UP000248484; Chromosome 14.
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:UP000248484}.
FT DOMAIN 72..127
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 131..272
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 196..250
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 446..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1246 AA; 137674 MW; F49A627B378A6A30 CRC64;
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 DHHEPICKAG
LELNKKEITT SADQIAEVKT MESHPPIPPV FVEHVVPQDE NQKGLCTKER MICLEFTSRE
FHAGQIEDEL NLNDINGCSS GCCLNESKFP LDNCPASKAL IQPGQDPEMA NKFPDLTVED
LETDALKADM NVHLLPMEEL TSRLKDLPMS TDPDSPSPQP SCQAEVSDFS TDRIDFFSAL
EKFVELSQET RSRSFSHSRM EELGGGRSES CRLSVVEVTP SEATADDQRS SSRSNTPHAS
EESSIDEEQS KAISELVSPD IFMQSHSENA ISVKEIVTEI ESISQGVGQI QVKGDILSIP
CHTPKKHIIH ELPLERAQAA ENKPGNLEQS EGSCTAQPEL AKDSGKWEPE GCPVAHSSTT
ELEEEEPAEG EQELWGPGVP PGANWYPGSV RRATLEFEER LRQEQEHHGA APACTPSSTR
KNPRNDSSSV ADLAPKGKGD EATLEHAFVP KEPEMSKGKG KCGGSEAGSV PHSEQHAIVP
APELLEPHPL PAPQKCPGSG PRTQQEGVLK EQRTSVSCQG PETPAVPPPL PKKIEIIEYT
HTVTTPDHGP EGETATSEKS GEQGLRKVKV EESITVLCAL DENLNQTLSP DQASLHPRAL
PLPHSSSPER EHGRPAHPAP TLSGREDWGN SPAAALETAA PFVSHSSHVL GASLAYLHPQ
TVVHLEGFTE QSSTTDSEPS AEKGSWEESQ EGPPSRGSEV PYQGSRLSSE DLCLISKPGD
GVGEQREKPG PSPVACQLPH SSSSDGIKGL SRSPRGAKEH AEEIESRAIS QVGLPKPSQM
RRSASLAKLG YLDLCKDCLP ESGPVCSESS HLKLLQPFIR MGSGMEAQGP PENPDAPQNL
EPTKYFIEQL KTTECIAQSK PVERPLVQYA KEFGSSQQCL LPRAGPELTS SEGGLPLVQT
QGLQGAGPAP GLAVVPRQQH GRTHPLRRLR KANDKKRTTN PFYNTM
//
