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Database: UniProt
Entry: A0A2K5LU19_CERAT
LinkDB: A0A2K5LU19_CERAT
Original site: A0A2K5LU19_CERAT 
ID   A0A2K5LU19_CERAT        Unreviewed;      1450 AA.
AC   A0A2K5LU19;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 32.
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:ENSCATP00000016441.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000016441.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000016441.1}
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   RefSeq; XP_011927891.1; XM_012072501.1.
DR   STRING; 9531.ENSCATP00000016441; -.
DR   Ensembl; ENSCATT00000040602.1; ENSCATP00000016441.1; ENSCATG00000032138.1.
DR   GeneID; 105591555; -.
DR   KEGG; caty:105591555; -.
DR   CTD; 85464; -.
DR   GeneTree; ENSGT00940000157430; -.
DR   OMA; EYTHTAT; -.
DR   OrthoDB; 5490735at2759; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000032138; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
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:UP000233060}.
FT   DOMAIN          275..330
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   DOMAIN          332..475
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          399..453
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          905..1007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1045..1069
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1091..1134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1171..1206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..709
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        911..932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..961
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1450 AA;  160944 MW;  B6FDCF1419C3575A CRC64;
     MALVTVQRSP TPSTTSSPCA SSSHLEDSES AALLCCECEE SEIFSDSNEA DSGEEECRSQ
     PRSISESFLT VKGAALFLPR GNGSSTPRIS HRRNKHAGDL QQHLQAMFIL LRPEDNIRLA
     VRLESTYQNR TRYMVVVSTN GRQDTEESIV LGMDFSSNDS STCTMGLVLP LWSDTLIHLD
     GDGGFSVSTD NRVHIFKPVS VQAMWSALQS LHKACEVARA HNYYPGSLFL TWVSYYESHI
     NSDQSSVNEW NAMQDVQSHR PDSPALFTDI PTERERTERL IKTKLREIMM QKDLENITSK
     EIRTELEMQM VCNLKKIKEF IDNEMIVILG QMDSQKKIFE HVFLGSEWNA SNLEDLQNRG
     VRYILNVTRE IDNFFPGVFE YHNIRVYDEE ATDLLAYWND TYKFISKAKK HGSKCLVHCK
     MGVSRSASTV IAYAMKEYGW NLDRAYDYVK ERRTVTKPNP SFMRQLEEYQ GILLASKQRH
     NKLWRSHSDS DLSDHHEPIC KPGLELNKKE ITTSADQIAE VKTMESHPPI PPVFVEHVVP
     QDANQKGLCT KERMICLEFT STEFHAGQIE DELNLNDING CSSGCCLNES KFPLDNCHAS
     KALIQPGHVP EMANKFPDLT VEDLETDALK ADMNVHLLPM EELTSRLKDL PMSPDPESPS
     PQPSCQTEIS DFSTDRIDFF SALEKFVELS QETRSRSFSH SRMEELGGGR SESCRLSVVE
     VAPSKVTTDD QRSSSLSNTP HASEESSMDE EQSKTISELV SPDIFMQSHL ENAISVKEIV
     TEIESISQGV GQIQLKGDIL SNPCHTPKKN SIHELLFERA QTPENKPGHL EQDEGSCTAQ
     PELAKDSGMC NPEGCLTTRS STADLEEGEP AEGEQELQGS GMHPGAKWYP GSVRRATLEF
     EERLRQEQEH HGAASTCTSL STRKNSKNDS SVADLAPKGK SDEATPEHSF VPKEPEMSKG
     KGKYSGPEAG SLSHSEQNAT VPAPKVLGFD HLPAPQEGPG SDTGTQQEGV LKDLRTVIPY
     QESETQAVPL RLPKRVEIIE YTHTVTSPNH TGPGSEIATG EKSGEQGLRK VNVEKSVTVL
     CTLDENLNRT LDPNQVSLHP QVLPPPHSSS PEHNRPTDHR TSTLSGPEDR GSSLSTALET
     AAPFVSHTTH LLSASLDYLH PQTMVHLEGF TEQSSTTDEP SAEQVSWEES QDSPLSSGSE
     VPYKDSQLSS ADLSLISKLG DNTGELQEKL DPLPVACRLP HSSSSENIKG LSHSPGVVKE
     RAKEIESRVV FQAGLTKPSQ MRRSASLAKL GYLDLCKDCL PEREPASCES PHLKLLQPFL
     RTDSGMHAME DQESLENPGA PHNPEPTKYF VEQLTTTECI VQSKPVERPL VQYAKEFGSS
     QQCLLPRAGP ELTSSEGGLP MLQTQGLQCA CPAPGLAVAP RQQHGRTHPL RRLKKANDKK
     RTTNPFYNTM
//
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