ID D2GYL7_AILME Unreviewed; 482 AA.
AC D2GYL7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE Flags: Fragment;
GN Name=DUSP10 {ECO:0000313|Ensembl:ENSAMEP00000007293.1};
GN ORFNames=PANDA_002102 {ECO:0000313|EMBL:EFB24457.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB24457.1};
RN [1] {ECO:0000313|EMBL:EFB24457.1, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000007293.1}
RP IDENTIFICATION.
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; GL192382; EFB24457.1; -; Genomic_DNA.
DR RefSeq; XP_002914228.1; XM_002914182.3.
DR STRING; 9646.ENSAMEP00000007293; -.
DR Ensembl; ENSAMET00000007600.2; ENSAMEP00000007293.1; ENSAMEG00000006928.2.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000157671; -.
DR HOGENOM; CLU_027074_0_1_1; -.
DR OMA; RMTCCPM; -.
DR OrthoDB; 53899at2759; -.
DR TreeFam; TF105122; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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 Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912}.
FT DOMAIN 168..285
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"
FT NON_TER 482
FT /evidence="ECO:0000313|EMBL:EFB24457.1"
SQ SEQUENCE 482 AA; 52363 MW; FE66A2289429BA03 CRC64;
MPPSPLDDRV VVALSRPVRP QDLNLCLDSS YLGSAAPGSN GHPPVIATTV VSLKAANLTY
MPSSSGSARS LNCGCSSASC CTVATYDKDS QAQTQAIAAG TATTTIGTSP ACPANQMVNS
NENAGPLSPS GGVGSPVAGT PKQLASIKII YPNDLAKKMT KCSKSHLPSQ GPVIIDCRPF
MEYNKSHIQG AVHINCADKI SRRRLQQGKI TVLDLISCRE GKDSFKRIFS KEIIVYDENT
NEPSRVMPSQ PLHIVLESLK REGKEPLVLK GGLSSFKQNH ENLCDNSLQL QECREAGGGA
SAASSVLPQS IPTTPDIENA ELTPILPFLF LGNEQDAQDL DTMQRLNIGY VINVTTHLPL
YHYEKGLFNY KRLPATDSNK QNLRQYFEEA FEFIEEAHQC GKGLLIHCQA GVSRSATIVI
AYLMKHTRMT MTDAYKFVKG KRPIISPNLN FMGQLLEFEE DLNNGVTPRI LTPKLMGVET
VV
//
