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Database: UniProt
Entry: H0VN97_CAVPO
LinkDB: H0VN97_CAVPO
Original site: H0VN97_CAVPO 
ID   H0VN97_CAVPO            Unreviewed;       482 AA.
AC   H0VN97;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=DUSP10 {ECO:0000313|Ensembl:ENSCPOP00000011913.2};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000011913.2, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000011913.2}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000011913.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily.
CC       {ECO:0000256|ARBA:ARBA00008601}.
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DR   EMBL; AAKN02018913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003474555.1; XM_003474507.3.
DR   RefSeq; XP_005005647.1; XM_005005590.2.
DR   RefSeq; XP_013013222.1; XM_013157768.1.
DR   AlphaFoldDB; H0VN97; -.
DR   STRING; 10141.ENSCPOP00000011913; -.
DR   Ensembl; ENSCPOT00000013360.3; ENSCPOP00000011913.2; ENSCPOG00000013232.4.
DR   GeneID; 100733434; -.
DR   KEGG; cpoc:100733434; -.
DR   CTD; 11221; -.
DR   VEuPathDB; HostDB:ENSCPOG00000013232; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000157671; -.
DR   HOGENOM; CLU_027074_0_1_1; -.
DR   InParanoid; H0VN97; -.
DR   OMA; RMTCCPM; -.
DR   OrthoDB; 53899at2759; -.
DR   TreeFam; TF105122; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000013232; Expressed in testis and 7 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0008432; F:JUN kinase binding; IEA:Ensembl.
DR   GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; IEA:Ensembl.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IEA:Ensembl.
DR   GO; GO:0016311; P:dephosphorylation; IEA:Ensembl.
DR   GO; GO:0010633; P:negative regulation of epithelial cell migration; IEA:Ensembl.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:1905042; P:negative regulation of epithelium regeneration; IEA:Ensembl.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:1903753; P:negative regulation of p38MAPK cascade; IEA:Ensembl.
DR   GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IEA:Ensembl.
DR   GO; GO:0002819; P:regulation of adaptive immune response; IEA:Ensembl.
DR   GO; GO:0090335; P:regulation of brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0051403; P:stress-activated MAPK cascade; IEA:Ensembl.
DR   CDD; cd14567; DSP_DUSP10; 1.
DR   CDD; cd01446; DSP_MapKP; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR008343; MKP.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR10159:SF299; DUAL SPECIFICITY PROTEIN PHOSPHATASE 10; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   PRINTS; PR01764; MAPKPHPHTASE.
DR   SMART; SM00195; DSPc; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT   DOMAIN          169..286
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          321..464
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          384..443
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
SQ   SEQUENCE   482 AA;  52326 MW;  B2DF4D488CAF816C CRC64;
     MPPSPLDDRV VVALSRPIRP QDLGLCLDSS SLGSATPGRS SHLSVIATTT TVSLKAANLT
     YMPSPSGSAR SLNCGCSSAS CCSVAAYDKD SQAQTQAIAA GTATTAVGTS TTCPANQMVN
     NNEHTGSLSL SGGVGSPVTG APKQLASIKI IYPNDLAKKM TKGSKSHLPS QSPVIIDCRP
     FMEYNKSHIQ GAVHINCADK ISRRRLQQGK ITVLDLISCR EGKDSFKRIF SKEIIVYDEN
     TNEPSRVMPS QPLHIVLESL KREGKDPLVL KGGLSSFKQN HENLCDNSLQ LQECREAGAA
     AAAPGLLPQP VPSTPDIESA ELTPILPFLF LGNEQDAQDL DTMQRLNIGY VINVTTHLPL
     YHYEKGLLNY KRLPATDSSK QNLRQYFEEA FEFIEEAHQC GKGLLIHCQA GVSRSATIVI
     AYLMKHTWMT MTDAYKFVKG KRPIISPNLN FMGQLLEFEE DLNNGVTPRI LTPKLMGVET
     VV
//
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