ID   DUS11_RAT               Reviewed;         326 AA.
AC   Q4KM79;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=RNA/RNP complex-1-interacting phosphatase;
DE            EC=3.1.3.-;
DE   AltName: Full=Dual specificity protein phosphatase 11;
DE   AltName: Full=Phosphatase that interacts with RNA/RNP complex 1;
GN   Name=Dusp11; Synonyms=Pir1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Possesses RNA 5'-triphosphatase and diphosphatase activities,
CC       but displays a poor protein-tyrosine phosphatase activity. In addition,
CC       has phosphatase activity with ATP, ADP and O-methylfluorescein
CC       phosphate (in vitro). Binds to RNA. May participate in nuclear mRNA
CC       metabolism. {ECO:0000250|UniProtKB:O75319}.
CC   -!- SUBUNIT: Monomer. May interact with SFRS7 and SFRS9/SRP30C.
CC       {ECO:0000250|UniProtKB:O75319}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75319}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:O75319}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
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DR   EMBL; BC098712; AAH98712.1; -; mRNA.
DR   RefSeq; NP_001020821.1; NM_001025650.1.
DR   RefSeq; XP_008761323.1; XM_008763101.2.
DR   AlphaFoldDB; Q4KM79; -.
DR   SMR; Q4KM79; -.
DR   STRING; 10116.ENSRNOP00000030319; -.
DR   PaxDb; Q4KM79; -.
DR   PRIDE; Q4KM79; -.
DR   Ensembl; ENSRNOT00000057475; ENSRNOP00000054285; ENSRNOG00000045539.
DR   GeneID; 297412; -.
DR   KEGG; rno:297412; -.
DR   UCSC; RGD:1307038; rat.
DR   CTD; 8446; -.
DR   RGD; 1307038; Dusp11.
DR   eggNOG; KOG2386; Eukaryota.
DR   GeneTree; ENSGT00940000155847; -.
DR   HOGENOM; CLU_057587_1_1_1; -.
DR   InParanoid; Q4KM79; -.
DR   OMA; NRIPERW; -.
DR   OrthoDB; 1544021at2759; -.
DR   PRO; PR:Q4KM79; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000022082; Expressed in duodenum and 19 other tissues.
DR   Genevisible; Q4KM79; RN.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; ISS:UniProtKB.
DR   GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:RGD.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; ISO:RGD.
DR   GO; GO:0098507; P:polynucleotide 5' dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; ISO:RGD.
DR   GO; GO:0016070; P:RNA metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.90.190.10; -; 1.
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   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; SSF52799; 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; Nucleus; Protein phosphatase; Reference proteome; RNA-binding.
FT   CHAIN           1..326
FT                   /note="RNA/RNP complex-1-interacting phosphatase"
FT                   /id="PRO_0000379777"
FT   DOMAIN          59..206
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        150
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        156
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         151..156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O75319"
SQ   SEQUENCE   326 AA;  38068 MW;  57633B0179518CB7 CRC64;
     MNQWHYGRYS RGRDFTARAP PKKKGKNQIP ERWKDYLPVG QRMPGTRFIA FKVPLQKKFE
     AKLMPEECFS PLDLFNKIQE QNEELGLIID LTYTQRYYKV EDLPKTISYI KILTVGHQVP
     DSGTIFQFKS AVKEFLKRNK NNDKLIGVHC THGLNRTGYL ICRYLIDVEG MRPDDAIELF
     NRCRGHCIER QNYIENLQKR RVRKNQNASA SRSGGLEDSA HLTEQVHTTN KPVNKGPKKS
     RRGGHLESSQ HVQTQSSAYS FRKWSQNQSV YQRGFVPPPG PAGEDYSQRR FFWSMRPNGS
     QATHHKKWIA ASYQRPFYPA SWEWNV