ID   RPAP2_DANRE             Reviewed;         601 AA.
AC   B0UYH6;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Putative RNA polymerase II subunit B1 CTD phosphatase rpap2;
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:Q8IXW5};
DE   AltName: Full=RNA polymerase II-associated protein 2;
GN   Name=rpap2; ORFNames=si:dkey-63k7.3;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Protein phosphatase that displays CTD phosphatase activity
CC       and regulates transcription of snRNA genes. Recognizes and binds
CC       phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain
CC       (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates
CC       dephosphorylation of 'Ser-5' of the CTD, thereby promoting
CC       transcription of snRNA genes (By similarity). Downstream of
CC       EIF2AK3/PERK, dephosphorylates ERN1, a sensor for the endoplasmic
CC       reticulum unfolded protein response (UPR), to abort failed ER-stress
CC       adaptation and trigger apoptosis (By similarity).
CC       {ECO:0000250|UniProtKB:Q8IXW5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000250|UniProtKB:Q8IXW5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- SUBUNIT: Associates with the RNA polymerase II complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RPAP2 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00812, ECO:0000305}.
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DR   EMBL; CR450845; CAQ13680.1; -; Genomic_DNA.
DR   RefSeq; NP_001264859.1; NM_001277930.1.
DR   AlphaFoldDB; B0UYH6; -.
DR   SMR; B0UYH6; -.
DR   STRING; 7955.ENSDARP00000056033; -.
DR   PaxDb; 7955-ENSDARP00000056033; -.
DR   PeptideAtlas; B0UYH6; -.
DR   GeneID; 554138; -.
DR   KEGG; dre:554138; -.
DR   AGR; ZFIN:ZDB-GENE-050522-420; -.
DR   CTD; 79871; -.
DR   ZFIN; ZDB-GENE-050522-420; rpap2.
DR   eggNOG; KOG4780; Eukaryota.
DR   HOGENOM; CLU_019258_1_0_1; -.
DR   InParanoid; B0UYH6; -.
DR   OMA; ICQNKLE; -.
DR   OrthoDB; 1410801at2759; -.
DR   PhylomeDB; B0UYH6; -.
DR   TreeFam; TF331431; -.
DR   Reactome; R-DRE-6807505; RNA polymerase II transcribes snRNA genes.
DR   PRO; PR:B0UYH6; -.
DR   Proteomes; UP000000437; Chromosome 2.
DR   Bgee; ENSDARG00000038397; Expressed in somite and 28 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0097550; C:transcription preinitiation complex; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0043175; F:RNA polymerase core enzyme binding; IEA:InterPro.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0036499; P:PERK-mediated unfolded protein response; ISS:UniProtKB.
DR   GO; GO:0009301; P:snRNA transcription; ISS:UniProtKB.
DR   Gene3D; 1.25.40.820; -; 1.
DR   InterPro; IPR039693; Rtr1/RPAP2.
DR   InterPro; IPR007308; Rtr1/RPAP2_dom.
DR   InterPro; IPR038534; Rtr1/RPAP2_sf.
DR   PANTHER; PTHR14732:SF0; RNA POLYMERASE II SUBUNIT B1 CTD PHOSPHATASE RPAP2-RELATED; 1.
DR   PANTHER; PTHR14732; UNCHARACTERIZED; 1.
DR   Pfam; PF04181; RPAP2_Rtr1; 1.
DR   PROSITE; PS51479; ZF_RTR1; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..601
FT                   /note="Putative RNA polymerase II subunit B1 CTD
FT                   phosphatase rpap2"
FT                   /id="PRO_0000416289"
FT   ZN_FING         71..154
FT                   /note="RTR1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          24..62
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        228..259
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
SQ   SEQUENCE   601 AA;  67549 MW;  78093E0ED1C0A82F CRC64;
     MDAGEVTRKS RPSKSKKKGG KGTQAISAED EAKRREAVKE QLRQKLELER KARQVVERLL
     EDSVTEEFLM DCAWHITPAN YKDTVEERSI AKLCGYPMCP NKLTNVPTQQ YKISTKTNKV
     YDITERKCFC SNFCYKASKS FELQISKIPL WLRKEESPPE IKLMKQGDGG SSGQEIKLID
     KPITEADIDN PIEDIPESNK DLIQGENGDI EQDFVSSVVS NQHKQVHWGK LPKRDEVSED
     AAEYSHSEHE QRINGENKDE SESSQTPQPQ KDTTDHPALE KNASEIEGTL ELLNQDKSTQ
     QEGENTSSSQ PESDISVPVA GDLNITQVGM SKRSAAGLKG LLKDHHKAKT ASTAISQCLL
     ERLRQAFIEW RTKETMIFLY GPDYASGMQL STAGAWEEEQ LDEDDLDEAE VGVRSAEGGP
     SRTSAPVPDV ETLRKETEML ELRVREFYKG VCVLPEEVET AAVKETEHTQ DSGKDPPLPL
     VDSHAQHQIQ KRIVVEKLSH SLRDIVGPLR LTMSDVINDV NNLVRTFRFT NTNIIHKSPE
     WTLIAVVLLS VLTEVSPLLR ESLASVSSLE YISCFMKELK LEDKDLHNLV LLFKPCVPIQ
     T
//