ID G5BYF9_HETGA Unreviewed; 662 AA.
AC G5BYF9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:JAO02957.1};
GN ORFNames=GW7_02282 {ECO:0000313|EMBL:EHB14320.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB14320.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB14320.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
RN [2] {ECO:0000313|EMBL:JAO02957.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney {ECO:0000313|EMBL:JAO02957.1};
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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; JH172446; EHB14320.1; -; Genomic_DNA.
DR EMBL; GEBF01000676; JAO02957.1; -; Transcribed_RNA.
DR AlphaFoldDB; G5BYF9; -.
DR STRING; 10181.G5BYF9; -.
DR Ensembl; ENSHGLT00000009831; ENSHGLP00000009723; ENSHGLG00000006977.
DR Ensembl; ENSHGLT00100010769; ENSHGLP00100010644; ENSHGLG00100007910.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; G5BYF9; -.
DR OMA; EGIMSEN; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
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; cd14646; DSP_DUSP16; 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: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 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:UP000006813}.
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 320..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 72820 MW; C71679390E74CDB9 CRC64;
MAHEMIGTQI VTERLVALLE SGTEKVLLID SRPFVEYNTS HILEAININC SKLMKRRLQQ
DKVLITELIQ HSAKQKVDID RSQKVVVYDQ SSQDVASLSS DCFLTVLLGK LGKSFSSVHL
LAGGFAEFSR CFPGLCEGKS TLVPTCISQP CLPVANIGPT RILPNLYLGC QRDVLNKELM
QQNGIGYVLN ASSTCPKPDF IPESHFLRVP VNDSFCEKIL PWLDKSVDFI EKAKASNGCV
LVHCLAGISR SATIAIAYIM KRMDMSVDEA YRFVKEKRPT ISPNFNFLGQ LLDYEKKIKN
QTGASGPKSK LKLLHLEKSN DPVPAASEGG QKSEMSLNPR CAKPGASEAA GQRPLHPASV
PSTQPSLLED SPLVQALNGL HLSSDKLEDS SKLKRSFSLD IKSVSYSASM AASLHGFSSE
DALEYYKPST TLDGTNKLCQ FSPVQEVSEQ TPETSPDKEE AHIPKKAPPA RPPEGQSKRL
HTVRTSSSGA TQRSFLSPLQ RSGSVEDNHH TNFLFGLSTS QQHLTKSAAG LGLKGWHSDI
LAPQTSTPSL TNSWYFATES SHFYSASAIY GGNTSYSAYS CSQLPTCSDQ VYSVRRRQKP
GDRADSRRSW HEESPFEKQF KRRSCQMEFG ESIMSENRSR EELGKVGSQS SFSGSMEIIE
VS
//
