GenomeNet

Database: UniProt
Entry: A0A2K5KGT8_COLAP
LinkDB: A0A2K5KGT8_COLAP
Original site: A0A2K5KGT8_COLAP 
ID   A0A2K5KGT8_COLAP        Unreviewed;       657 AA.
AC   A0A2K5KGT8;
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};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000040307.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000040307.1}
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_011797776.1; XM_011942386.1.
DR   AlphaFoldDB; A0A2K5KGT8; -.
DR   STRING; 336983.ENSCANP00000040307; -.
DR   Ensembl; ENSCANT00000063571.1; ENSCANP00000040307.1; ENSCANG00000043834.1.
DR   GeneID; 105512097; -.
DR   KEGG; cang:105512097; -.
DR   CTD; 54961; -.
DR   OMA; PQDDIHL; -.
DR   OrthoDB; 5490735at2759; -.
DR   Proteomes; UP000233080; Unplaced.
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; cd14571; DSP_slingshot_3; 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:SF4; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 3; 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   SUPFAM; SSF109715; DEK C-terminal domain; 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:UP000233080}.
FT   DOMAIN          269..324
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   DOMAIN          328..469
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          393..448
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..74
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..505
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   657 AA;  72676 MW;  C658AC4BD70406F3 CRC64;
     MALVTVSRSP PGSGASTPVG PRDGAVQRRS RLQRRQSFAV LRGAVLGLQD GGDNDDAAEA
     SPEPAEEPPN EEEPGGDQTD FGQGSQSPQK QEEQRRHLHL MVQLLRPQDD IRLAAQLEAA
     RPPRLRYLLV VSTQEGEGLS QDETVLLGVD FPDSSSPSCT LGLVLPLWSD TQVYLDGDGG
     FSVTSGGQSR IFKPISIQTM WATLQVLHQA CEAALGSGLV PGGSALTWAS HYQERLNSDQ
     NCLNEWTAMA DLESLRPPSV EPGRPLEQEQ MEQAIRAELW KVLDASDLES VTSKEIRQAL
     ELRLGLPLQQ YRDFIDNQML LLVAQQDRAS RIFPHLYLGS EWNAANLEEL QRNRVTHILN
     MAREIDNFYP ERFTYHNVRL WDEESAQLLP HWKETHRFIE AARAQGTRVL VHCKMGVSRS
     AATVLAYAMK QYECSLEQAL RHVQELRPIA RPNPGFLRQL QIYQGILTAS RQSHVWEQKV
     GGVSPEERPA PEVSTPFPPL PPEPGGGGEE KVVGMEESQA APKQEPRPRP RINLRGVMRS
     ISLLEPSLEL ESTSEASDMP EVFSSHESSR EEPPQPFPQL ARTEGSQQVG KAPQPALKSC
     QSVVALQGST LVANQTRAFQ EQEQGQGQGE PCISSTPRFR KVVRQASVDD SGEEGEA
//
DBGET integrated database retrieval system