RPAP2_BOVIN
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 03-AUG-2022, entry version 57.
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. {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 -!- 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; 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.ENSBTAP00000041791; -.
DR PaxDb; F6RRD7; -.
DR PRIDE; F6RRD7; -.
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 OrthoDB; 1506260at2759; -.
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:0016591; C:RNA polymerase II, holoenzyme; 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: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:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; 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; PTHR14732; 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
