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Database: UniProt
Entry: F7IJ42_CALJA
LinkDB: F7IJ42_CALJA
Original site: F7IJ42_CALJA 
ID   F7IJ42_CALJA            Unreviewed;       661 AA.
AC   F7IJ42;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=DUSP16 {ECO:0000313|EMBL:JAB13509.1,
GN   ECO:0000313|Ensembl:ENSCJAP00000040282.1};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000040282.1, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000040282.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB13509.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:JAB51310.1}, Cerebral cortex
RC   {ECO:0000313|EMBL:JAB24837.1}, Hippocampus
RC   {ECO:0000313|EMBL:JAB13509.1}, and Skeletal muscle
RC   {ECO:0000313|EMBL:JAB37283.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
RN   [3] {ECO:0000313|Ensembl:ENSCJAP00000040282.1}
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; GAMS01009627; JAB13509.1; -; mRNA.
DR   EMBL; GAMR01009095; JAB24837.1; -; mRNA.
DR   EMBL; GAMQ01004568; JAB37283.1; -; mRNA.
DR   EMBL; GAMP01001445; JAB51310.1; -; mRNA.
DR   RefSeq; XP_002752178.1; XM_002752132.3.
DR   RefSeq; XP_009001556.1; XM_009003308.2.
DR   STRING; 9483.ENSCJAP00000040282; -.
DR   Ensembl; ENSCJAT00000042547.4; ENSCJAP00000040282.1; ENSCJAG00000021639.5.
DR   GeneID; 100388584; -.
DR   KEGG; cjc:100388584; -.
DR   CTD; 80824; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00940000157164; -.
DR   HOGENOM; CLU_027074_16_0_1; -.
DR   OMA; EGIMSEN; -.
DR   OrthoDB; 2901840at2759; -.
DR   TreeFam; TF105122; -.
DR   Proteomes; UP000008225; Chromosome 9.
DR   Bgee; ENSCJAG00000021639; Expressed in testis and 6 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; 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:0016311; P:dephosphorylation; IEA:Ensembl.
DR   GO; GO:0045204; P:MAPK export from nucleus; IEA:Ensembl.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:Ensembl.
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:SF343; DUAL SPECIFICITY PROTEIN PHOSPHATASE 16; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF00581; Rhodanese; 1.
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   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT   DOMAIN          22..137
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          158..300
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          227..281
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          319..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..624
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   661 AA;  72840 MW;  A49BE62265F84A6B CRC64;
     MAHEMIGTQI VTERLVALLE SGTEKVLLID SRPFVEYNTS HILEAININC SKLMKRRLQQ
     DKVLITELIQ HSAKHKVDID CSQKVVVYDQ SSQDVASLSS DCFLTVLLGK LEKSFNSVHL
     LAGGFAEFSR CFPGLCEGKS TLVPSCISQP CLPVANIGPT RILPNLYLGC QRDVLNKELM
     QQNGIGYVLN ASSTCPKPDF IPESHFLRVP VNDSFCEKIL PWLDESVDFI EKAKASNGCV
     LVHCLAGISR SATIAIAYIM KRMDMSLDEA YRFVKEKRPT ISPNFNFLGQ LLDYEKKIKN
     QTGTSGPKSK LKLLHLEKPN DPVPAVSEGG QKSESPLSPP SADSATSEAA GQRPVHPTSM
     PSMQPPLLED SPLVQALSGL HLSTDRLEDS NKLKRSFSLD IKSVSYSASM AASLHGFSSE
     DALEYYKPSS TLDGTNKLCQ FSPVQELSEQ TPETSPDKEE TSIPKKPPTT RPSDSQSKRL
     HSVRTSSSGT TQRSLLSPLH RSGSVEDNYH TSFLFGLSTS QQHLTKSAGL GLKGWHSDIL
     APQTSTPSLT SSWYFATESS HFYSASAIYG GSASYSAYSC SQLPTCGDQV YSVRRRQKPS
     DRADSRRSWH EESPFEKQFK RRSCQMEFGE SIMSENRSRE ELGKVGSQSS FSGSMEIIEV
     S
//
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