GenomeNet

Database: UniProt
Entry: A0A2U3VX82_ODORO
LinkDB: A0A2U3VX82_ODORO
Original site: A0A2U3VX82_ODORO 
ID   A0A2U3VX82_ODORO        Unreviewed;       188 AA.
AC   A0A2U3VX82;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Dual specificity protein phosphatase 18 {ECO:0000256|ARBA:ARBA00040029};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=DUSP18 {ECO:0000313|RefSeq:XP_004400091.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004400091.1};
RN   [1] {ECO:0000313|RefSeq:XP_004400091.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Can dephosphorylate single and diphosphorylated synthetic
CC       MAPK peptides, with preference for the phosphotyrosine and
CC       diphosphorylated forms over phosphothreonine. In vitro,
CC       dephosphorylates p-nitrophenyl phosphate (pNPP).
CC       {ECO:0000256|ARBA:ARBA00037043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001512};
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004137};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004137};
CC       Intermembrane side {ECO:0000256|ARBA:ARBA00004137}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily.
CC       {ECO:0000256|ARBA:ARBA00008601}.
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_004400091.1; XM_004400034.2.
DR   AlphaFoldDB; A0A2U3VX82; -.
DR   STRING; 9708.A0A2U3VX82; -.
DR   GeneID; 101370210; -.
DR   KEGG; oro:101370210; -.
DR   CTD; 150290; -.
DR   InParanoid; A0A2U3VX82; -.
DR   OrthoDB; 127323at2759; -.
DR   Proteomes; UP000245340; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14573; DUSP18_21; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR020420; Atypical_DUSP_subfamB.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
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; PTHR46495:SF2; DUAL SPECIFICITY PROTEIN PHOSPHATASE 18; 1.
DR   PANTHER; PTHR46495; DUAL SPECIFICITY PROTEIN PHOSPHATASE 21; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   PRINTS; PR01910; ADSPHPHTASEB.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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   Membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245340}.
FT   DOMAIN          19..160
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          80..139
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
SQ   SEQUENCE   188 AA;  21053 MW;  334CB5C51DC2C520 CRC64;
     MTAPLCTFPV QFRQPSVSGL SQITNSLYVS NGVAANNKLM LSSNQITTVI NVSVEVVNTL
     YEDIQYVQVP VADTPISRLC DFFDPIADHI HSVEMKQGRT LLHCAAGVSR SAALCLAYLM
     KYHAMSLLDA HTWTKSCRPI IRPNNGFWEQ LIHYEFQLFG KNTVHMVSSP MGVIPDIYEK
     EVHLMIPL
//
DBGET integrated database retrieval system