RPAP2_ARATH
ID RPAP2_ARATH Reviewed; 735 AA.
AC F4K1B1; O04626; Q5XF30;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 homolog;
DE EC=3.1.3.16;
DE AltName: Full=RNA polymerase II-associated protein 2 homolog;
GN OrderedLocusNames=At5g26760; ORFNames=F2P16.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Putative RNA polymerase II subunit B1 C-terminal domain (CTD)
CC phosphatase involved in RNA polymerase II transcription regulation.
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4K1B1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4K1B1-2; Sequence=VSP_042606;
CC -!- SIMILARITY: Belongs to the RPAP2 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00812, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61054.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF007270; AAB61054.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93597.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93598.1; -; Genomic_DNA.
DR EMBL; BT015786; AAU90076.1; -; mRNA.
DR PIR; T01757; T01757.
DR RefSeq; NP_198028.2; NM_122558.4. [F4K1B1-2]
DR RefSeq; NP_974839.1; NM_203110.2. [F4K1B1-1]
DR AlphaFoldDB; F4K1B1; -.
DR SMR; F4K1B1; -.
DR BioGRID; 18009; 1.
DR STRING; 3702.AT5G26760.2; -.
DR iPTMnet; F4K1B1; -.
DR PaxDb; F4K1B1; -.
DR PRIDE; F4K1B1; -.
DR ProteomicsDB; 228204; -. [F4K1B1-1]
DR EnsemblPlants; AT5G26760.1; AT5G26760.1; AT5G26760. [F4K1B1-2]
DR EnsemblPlants; AT5G26760.2; AT5G26760.2; AT5G26760. [F4K1B1-1]
DR GeneID; 832734; -.
DR Gramene; AT5G26760.1; AT5G26760.1; AT5G26760. [F4K1B1-2]
DR Gramene; AT5G26760.2; AT5G26760.2; AT5G26760. [F4K1B1-1]
DR KEGG; ath:AT5G26760; -.
DR Araport; AT5G26760; -.
DR TAIR; locus:2148438; AT5G26760.
DR eggNOG; KOG4780; Eukaryota.
DR HOGENOM; CLU_008740_0_0_1; -.
DR InParanoid; F4K1B1; -.
DR OMA; ACGYPAC; -.
DR OrthoDB; 1506260at2759; -.
DR PhylomeDB; F4K1B1; -.
DR PRO; PR:F4K1B1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K1B1; baseline and differential.
DR Genevisible; F4K1B1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IMP:TAIR.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
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 Alternative splicing; Hydrolase; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..735
FT /note="Putative RNA polymerase II subunit B1 CTD
FT phosphatase RPAP2 homolog"
FT /id="PRO_0000416291"
FT ZN_FING 33..118
FT /note="RTR1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT REGION 179..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00812"
FT VAR_SEQ 1..305
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_042606"
SQ SEQUENCE 735 AA; 81058 MW; E782F1B107D5D5B7 CRC64;
MAKDNEAIAI NDAVHKLQLY MLENTTDQNQ LFAARKLMSR SDYEDVVTER AIAKLCGYTL
CQRFLPSDVS RRGKYRISLK DHKVYDLQET SKFCSAGCLI DSKTFSGSLQ EARTLEFDSV
KLNEILDLFG DSLEVKGSLD VNKDLDLSKL MIKENFGVRG EELSLEKWMG PSNAVEGYVP
FDRSKSSNDS KATTQSNQEK HEMDFTSTVI MPDVNSVSKL PPQTKQASTV VESVDGKGKT
VLKEQTVVPP TKKVSRFRRE KEKEKKTFGV DGMGCAQEKT TVLPRKILSF CNEIEKDFKN
FGFDEMGLAS SAMMSDGYGV EYSVSKQPQC SMEDSLSCKL KGDLQTLDGK NTLSGSSSGS
NTKGSKTKPE KSRKKIISVE YHANSYEDGE EILAAESYER HKAQDVCSSS EIVTKSCLKI
SGSKKLSRSV TWADQNDGRG DLCEVRNNDN AAGPSLSSND IEDVNSLSRL ALAEALATAL
SQAAEAVSSG NSDASDATAK AGIILLPSTH QLDEEVTEEH SEEEMTEEEP TLLKWPNKPG
IPDSDLFDRD QSWFDGPPEG FNLTLSNFAV MWDSLFGWVS SSSLAYIYGK EESAHEEFLL
VNGKEYPRRI IMVDGLSSEI KQTIAGCLAR ALPRVVTHLR LPIAISELEK GLGSLLETMS
LTGAVPSFRV KEWLVIVLLF LDALSVSRIP RIAPYISNRD KILEGSGIGN EEYETMKDIL
LPLGRVPQFA TRSGA
