ID RPAP2_BOVIN Reviewed; 608 AA. AC F6RRD7; A4FV88; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 16-NOV-2011, sequence version 1. DT 24-JAN-2024, entry version 62. DE RecName: Full=Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2; DE EC=3.1.3.16; DE AltName: Full=RNA polymerase II-associated protein 2; GN Name=RPAP2; 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 GENOMIC DNA]. RC STRAIN=Hereford; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D., RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G., RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Basal ganglia; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (SEP-2006) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DAAA02007907; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC123867; AAI23868.1; -; mRNA. DR RefSeq; NP_001096736.1; NM_001103266.1. DR RefSeq; XP_005204350.1; XM_005204293.3. DR RefSeq; XP_005204351.1; XM_005204294.3. DR RefSeq; XP_010801614.1; XM_010803312.2. DR RefSeq; XP_010801615.1; XM_010803313.2. DR AlphaFoldDB; F6RRD7; -. DR SMR; F6RRD7; -. DR STRING; 9913.ENSBTAP00000066661; -. DR PaxDb; 9913-ENSBTAP00000041791; -. DR GeneID; 529184; -. DR KEGG; bta:529184; -. DR CTD; 79871; -. DR eggNOG; KOG4780; Eukaryota. DR HOGENOM; CLU_019258_1_0_1; -. DR InParanoid; F6RRD7; -. DR TreeFam; TF331431; -. DR Proteomes; UP000009136; 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..608 FT /note="Putative RNA polymerase II subunit B1 CTD FT phosphatase RPAP2" FT /id="PRO_0000416288" FT ZN_FING 77..160 FT /note="RTR1-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812" FT REGION 1..38 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 193..262 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 403..423 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 33..68 FT /evidence="ECO:0000255" FT COMPBIAS 23..37 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 194..208 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 209..233 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 241..256 FT /note="Basic and acidic 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 432 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8IXW5" FT MOD_RES 479 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8IXW5" FT CONFLICT 33 FT /note="N -> I (in Ref. 2; AAI23868)" FT /evidence="ECO:0000305" SQ SEQUENCE 608 AA; 68698 MW; 04EE1D88C5404049 CRC64; MADWVGPCSA GRKARRSRAS RDVAGTKQTS ALNQEDASQR KAELEAAVRK KIEFERKALH IVEQLLEENI SEEFLRECGK FITPAHYSDV VDERSIIKLC GYPLCQNKLG IVPKQKYKIS TKTNKVYDIT ERKCFCSNFC YKASKFFEAQ IPKSPVWIRE EERHPDFQLL QDGQSGPSGE EIQLCSKAIK TSDIDSPGHF EKHYESSSSS SHSDSSSDNE QDFVSSILPG NRPNATRPQL HEKSIMKKKA GQKVNSQHES KEQTVVDVIE QLGNCRLDNQ EKATACELPL QNVNTQISSN SSLQKKLEAS EISDIKYSSS KVTLVGISKK SAEHFKRKFA KSNQVSGSAS SSLQVCPEIA KANLLKALKE TLIEWKTEET LRFLYGQNYA SVCLKSSSTP LVKEEELDED DMNSDPDSHS PALQELNSLD ESLPFRASDT AIKPLPSYEN LKKETETLNL RIREFYRGRY VLNEETTKSQ DSEEHDPTFP LIDSSSQNQI RKRIVLEKLN KVLPGLLGPL QITLGDIYTQ LKNLVHTFRL TNRNIIHKPA EWTLIALVLL SILTSTLGIQ KLSQENVMFT QFMTTLLEEL HLKNEDLESL TIIFRTSC //