ID   RPAP2_PONAB             Reviewed;         612 AA.
AC   Q5RA37;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 66.
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;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Interacts with
CC       transcribing RNA polymerase II phosphorylated on 'Ser-7' on CTD (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Shuttles between the cytoplasm and the nucleus in a CRM1-dependent
CC       manner. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RPAP2 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00812, ECO:0000305}.
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DR   EMBL; CR859185; CAH91373.1; -; mRNA.
DR   RefSeq; NP_001125811.1; NM_001132339.1.
DR   AlphaFoldDB; Q5RA37; -.
DR   SMR; Q5RA37; -.
DR   STRING; 9601.ENSPPYP00000001338; -.
DR   GeneID; 100172739; -.
DR   KEGG; pon:100172739; -.
DR   CTD; 79871; -.
DR   eggNOG; KOG4780; Eukaryota.
DR   InParanoid; Q5RA37; -.
DR   OrthoDB; 1410801at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW   Phosphoprotein; Protein phosphatase; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IXW5"
FT   CHAIN           2..612
FT                   /note="Putative RNA polymerase II subunit B1 CTD
FT                   phosphatase RPAP2"
FT                   /id="PRO_0000250650"
FT   ZN_FING         77..160
FT                   /note="RTR1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          33..68
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        201..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   BINDING         136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IXW5"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IXW5"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5I0E6"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IXW5"
FT   MOD_RES         480
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IXW5"
SQ   SEQUENCE   612 AA;  69534 MW;  791442A755D1461E CRC64;
     MADCAGPSSA GRKAGAPRRS RKAAGTKQTS TLKQEDASKR KAELEAAVRK KIEFERKALH
     IVEQLLEENI TEEFLMECGK FITPAHYSDV VDERSIVKLC GYPLCQKKLG IVPKQKYKIS
     TKTNKVYDIT ERKSFCSNFC YQASKFFEAQ IPKTPVWVRE EERHPDFQLL KEQQSGHSGE
     EVQLCSKAIK TSDIDNPSHF EKQYESSSSS THSDSSSDNE QDFVSSILPG NRPNSTSIRP
     QLHQKSIMKK KAGHKANSKH KDKEQTVIDV TEQLGDCKLD SQEKDATCEL PLQKVNTQSS
     SNSTLPERLK ASENSESEYS RSEITLVGIS KKSAEHFKRK FAKSNQVSRS VSSSVQVCPE
     VGKRNLLKIL KETLIEWKTE ETLRFLYGQN YASVCLKPEA SLVKEELDED DIISDPDSHF
     PAWRESQNSL DESLPFRGSG TAIKPLPSYE NLKKETEKLN LRIREFYRGR YVLDEETTKS
     QDSEEHDSTF PLIDSSSQNQ IRKRIVLEKL SKVLPGLLVP LQITLGDIYT QLKNLVRTFR
     LTNRNIIHKP AEWTLIAMVL LSLLTPILGI QKHSQEGMVF TRFLDTLLEE LHLKNEDLES
     LTIVFRTSCL PE
//