PBRP1_ARATH
ID PBRP1_ARATH Reviewed; 503 AA.
AC O23215;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Plant-specific TFIIB-related protein 1 {ECO:0000305};
DE AltName: Full=Plant-specific TFIIB-related protein {ECO:0000303|PubMed:12697827};
DE Short=AtPBRP {ECO:0000303|PubMed:12697827};
DE AltName: Full=TFIIB-related protein PBRP1 {ECO:0000305};
GN Name=PBRP1 {ECO:0000305}; Synonyms=PBRP {ECO:0000303|PubMed:12697827};
GN OrderedLocusNames=At4g36650 {ECO:0000312|Araport:AT4G36650};
GN ORFNames=C7A10.710 {ECO:0000312|EMBL:CAB16810.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=12697827; DOI=10.1128/mcb.23.9.3274-3286.2003;
RA Lagrange T., Hakimi M.A., Pontier D., Courtois F., Alcaraz J.P.,
RA Grunwald D., Lam E., Lerbs-Mache S.;
RT "Transcription factor IIB (TFIIB)-related protein (pBrp), a plant-specific
RT member of the TFIIB-related protein family.";
RL Mol. Cell. Biol. 23:3274-3286(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Lawit S.J., Gurley W.B.;
RT "Binary protein-protein interactions of Arabidopsis thaliana general
RT transcription factors TFIIa, TFIIb, TFIId, TFIIe, and TFIIf.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP FUNCTION.
RX PubMed=18668124; DOI=10.1038/emboj.2008.151;
RA Imamura S., Hanaoka M., Tanaka K.;
RT "The plant-specific TFIIB-related protein, pBrp, is a general transcription
RT factor for RNA polymerase I.";
RL EMBO J. 27:2317-2327(2008).
CC -!- FUNCTION: Plant-specific TFIIB-related protein that may be involved in
CC an intracellular signaling pathway between plastids and the nucleus
CC (PubMed:12697827). May act as general transcription factor (GTF) of RNA
CC polymerase I-dependent transcription and rRNA synthesis. Forms a
CC ternary complex with TBP2 and the rDNA promoter region
CC (PubMed:18668124). {ECO:0000269|PubMed:12697827,
CC ECO:0000269|PubMed:18668124}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:12697827}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000269|PubMed:12697827}. Nucleus
CC {ECO:0000269|PubMed:12697827}. Note=Localizes to the nucleus under
CC conditions of proteasome inhibition. {ECO:0000269|PubMed:12697827}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=O23215-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12697827}.
CC -!- PTM: Ubiquinated. Subsequent degradation by the proteasome pathway.
CC {ECO:0000305|PubMed:12697827}.
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DR EMBL; AJ295068; CAC82714.1; -; mRNA.
DR EMBL; AY463603; AAR28005.1; -; mRNA.
DR EMBL; Z99708; CAB16810.1; -; Genomic_DNA.
DR EMBL; AL161589; CAB80331.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86682.1; -; Genomic_DNA.
DR EMBL; BT006470; AAP21278.1; -; mRNA.
DR PIR; G85432; G85432.
DR RefSeq; NP_195383.1; NM_119828.6. [O23215-1]
DR AlphaFoldDB; O23215; -.
DR SMR; O23215; -.
DR STRING; 3702.AT4G36650.1; -.
DR iPTMnet; O23215; -.
DR PaxDb; O23215; -.
DR PRIDE; O23215; -.
DR ProteomicsDB; 236842; -. [O23215-1]
DR EnsemblPlants; AT4G36650.1; AT4G36650.1; AT4G36650. [O23215-1]
DR GeneID; 829817; -.
DR Gramene; AT4G36650.1; AT4G36650.1; AT4G36650. [O23215-1]
DR KEGG; ath:AT4G36650; -.
DR Araport; AT4G36650; -.
DR TAIR; locus:2115255; AT4G36650.
DR eggNOG; KOG1597; Eukaryota.
DR HOGENOM; CLU_031240_1_0_1; -.
DR InParanoid; O23215; -.
DR OMA; FHIRAQD; -.
DR OrthoDB; 729732at2759; -.
DR PhylomeDB; O23215; -.
DR PRO; PR:O23215; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23215; baseline and differential.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009527; C:plastid outer membrane; IDA:TAIR.
DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000182; F:rDNA binding; IDA:TAIR.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR000812; TFIIB.
DR InterPro; IPR013150; TFIIB_cyclin.
DR PANTHER; PTHR11618; PTHR11618; 1.
DR Pfam; PF00382; TFIIB; 2.
DR PRINTS; PR00685; TIFACTORIIB.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Membrane; Metal-binding; Nucleus;
KW Plastid; Plastid outer membrane; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..503
FT /note="Plant-specific TFIIB-related protein 1"
FT /id="PRO_0000436814"
FT ZN_FING 1..33
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT REGION 328..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 55672 MW; 865481B0CB013DF2 CRC64;
MKCPYCSSAQ GRCTTTSSGR SITECSSCGR VMEERQTQNH HLFHLRAQDT PLCLVTSDLQ
TAAQPSPEDE EDPFEPTGFI TAFSTWSLEP SPIFARSSLS FSGHLAELER TLELASSTSN
SNSSTVVVDN LRAYMQIIDV ASILGLDCDI SEHAFQLFRD CCSATCLRNR SVEALATACL
VQAIREAQEP RTLQEISIAA NVQQKEIGKY IKILGEALQL SQPINSNSIS VHMPRFCTLL
QLNKSAQELA THIGEVVINK CFCTRRNPIS ISAAAIYLAC QLEDKRKTQA EICKITGLTE
VTLRKVYKEL LENWDDLLPS NYTPAVPPEK AFPTTTISTT RSTTPRAVDP PEPSFVEKDK
PSAKPIETFD HTYQQPKGKE DKQPKFRQPW LFGTASVMNP AEMISEPAKP NAMDYEKQQL
DKQQQQQLGD KETLPIYLRD HNPFPSNPSP STGISTINWS FRPSVVPGSS SNLPVIHPPK
LPPGYAEIRG SGSRNADNPH GDF
