ID   DUS11_BOVIN             Reviewed;         331 AA.
AC   Q5E999; Q2KJ27;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; BT021021; AAX09038.1; -; mRNA.
DR   EMBL; BC105553; AAI05554.1; -; mRNA.
DR   RefSeq; NP_001014875.1; NM_001014875.1.
DR   AlphaFoldDB; Q5E999; -.
DR   SMR; Q5E999; -.
DR   STRING; 9913.ENSBTAP00000044476; -.
DR   PaxDb; Q5E999; -.
DR   GeneID; 508944; -.
DR   KEGG; bta:508944; -.
DR   CTD; 8446; -.
DR   eggNOG; KOG2386; Eukaryota.
DR   InParanoid; Q5E999; -.
DR   OrthoDB; 1544021at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0098507; P:polynucleotide 5' dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
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..331
FT                   /note="RNA/RNP complex-1-interacting phosphatase"
FT                   /id="PRO_0000094815"
FT   DOMAIN          61..208
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        152
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        158
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         153..158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O75319"
SQ   SEQUENCE   331 AA;  39060 MW;  8417A5DD3F6C943F CRC64;
     MSQWHHVGGH WGQDRVFSGY SSAKKKGGNH IPERWKDYLP VGQRMPGTRF IAFKVPLKKS
     FEKHLAPEEC FSPLDLFNKI QEQNEELGLI IDLTYTRRYY KPEELPENFP YLKIYTVGHQ
     VPDDDTIFKF KNAVNGFLRE NKDNDRLIGV HCTHGVNRTG YLICRYLIDV EGMRPDDAIE
     LFSRCRGHCL ERQNYIDDLR NGPIRKNWDS SVSRTRGFED STHMMEPVFT ATKPVNRRPK
     HNIHQTQGYP EPRHFHTWTQ DLQQSERKFS QNWNIYQRCH VPPPGPPGED YFQRRYSWNV
     KPSAGQGGPN KRFSPGSYYR VPYSAYYRWT K