PRFB1_ARATH
ID PRFB1_ARATH Reviewed; 456 AA.
AC Q9LVY0; Q9C5B2;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Peptide chain release factor PrfB1, chloroplastic {ECO:0000303|PubMed:21771930};
DE Short=AtPrfB1 {ECO:0000303|PubMed:21771930};
DE AltName: Full=AtPrfB {ECO:0000303|PubMed:12468741};
DE AltName: Full=Protein HIGH CHLOROPHYLL FLUORESCENCE 109 {ECO:0000303|PubMed:12468741};
DE Flags: Precursor;
GN Name=PRFB1 {ECO:0000303|PubMed:21771930};
GN Synonyms=HCF109 {ECO:0000303|PubMed:12468741},
GN RF2 {ECO:0000303|PubMed:12468741};
GN OrderedLocusNames=At5g36170 {ECO:0000312|Araport:AT5G36170};
GN ORFNames=MAB16.12 {ECO:0000312|EMBL:BAA96892.1};
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] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INDUCTION BY LIGHT, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=12468741; DOI=10.1105/tpc.006809;
RA Meurer J., Lezhneva L., Amann K., Godel M., Bezhani S., Sherameti I.,
RA Oelmuller R.;
RT "A peptide chain release factor 2 affects the stability of UGA-containing
RT transcripts in Arabidopsis chloroplasts.";
RL Plant Cell 14:3255-3269(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=21771930; DOI=10.1105/tpc.111.085324;
RA Stoppel R., Lezhneva L., Schwenkert S., Torabi S., Felder S., Meierhoff K.,
RA Westhoff P., Meurer J.;
RT "Recruitment of a ribosomal release factor for light- and stress-dependent
RT regulation of petB transcript stability in Arabidopsis chloroplasts.";
RL Plant Cell 23:2680-2695(2011).
CC -!- FUNCTION: Directs the termination of translation in response to the
CC peptide chain termination codon UGA. Required for the proper
CC translation, stability and normal processing of UGA-containing
CC polycistronic transcripts in chloroplasts.
CC {ECO:0000269|PubMed:12468741}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:12468741, ECO:0000269|PubMed:21771930}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LVY0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LVY0-2; Sequence=VSP_057112;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers.
CC {ECO:0000269|PubMed:12468741}.
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:12468741}.
CC -!- DISRUPTION PHENOTYPE: High chlorophyll fluorescence phenotype (hcf) and
CC severe lesions in thylakoid membrane complexes, predominantly in
CC photosystem II. {ECO:0000269|PubMed:12468741}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000305}.
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DR EMBL; AJ298098; CAC36322.1; -; mRNA.
DR EMBL; AB018112; BAA96892.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94051.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94053.1; -; Genomic_DNA.
DR EMBL; AY056234; AAL07083.1; -; mRNA.
DR EMBL; AY117253; AAM51328.1; -; mRNA.
DR EMBL; AY084711; AAM61285.1; -; mRNA.
DR RefSeq; NP_851096.1; NM_180765.2. [Q9LVY0-1]
DR RefSeq; NP_851097.1; NM_180766.1. [Q9LVY0-2]
DR AlphaFoldDB; Q9LVY0; -.
DR SMR; Q9LVY0; -.
DR STRING; 3702.AT5G36170.1; -.
DR PaxDb; Q9LVY0; -.
DR PRIDE; Q9LVY0; -.
DR ProteomicsDB; 234871; -. [Q9LVY0-1]
DR EnsemblPlants; AT5G36170.1; AT5G36170.1; AT5G36170. [Q9LVY0-1]
DR EnsemblPlants; AT5G36170.2; AT5G36170.2; AT5G36170. [Q9LVY0-2]
DR GeneID; 833614; -.
DR Gramene; AT5G36170.1; AT5G36170.1; AT5G36170. [Q9LVY0-1]
DR Gramene; AT5G36170.2; AT5G36170.2; AT5G36170. [Q9LVY0-2]
DR KEGG; ath:AT5G36170; -.
DR Araport; AT5G36170; -.
DR TAIR; locus:2158936; AT5G36170.
DR eggNOG; KOG2726; Eukaryota.
DR InParanoid; Q9LVY0; -.
DR OMA; YVFHPYQ; -.
DR PhylomeDB; Q9LVY0; -.
DR PRO; PR:Q9LVY0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVY0; baseline and differential.
DR Genevisible; Q9LVY0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:InterPro.
DR GO; GO:0009657; P:plastid organization; IMP:TAIR.
DR GO; GO:0006396; P:RNA processing; IMP:TAIR.
DR GO; GO:0006415; P:translational termination; IMP:TAIR.
DR HAMAP; MF_00094; Rel_fac_2; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004374; PrfB.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
DR TIGRFAMs; TIGR00020; prfB; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Plastid; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 59..456
FT /note="Peptide chain release factor PrfB1, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430964"
FT VAR_SEQ 57
FT /note="Missing (in isoform 2)"
FT /id="VSP_057112"
SQ SEQUENCE 456 AA; 50977 MW; A4B7493945782B27 CRC64;
MSMELTVLGP LAGRSFAIAG KPKLLLLRPT NLPLLRLSLP LSLPNFSSSS RFNSPIVFAA
QESNLSVSNE NETSEWLMQD FYTLRKDVEI ASARVEEIRA SANLQQLEQE ITNLESKATD
TSFWDDRTKA QETLSSLNDL KDRMRLLSEF KTMVEDAETI VKLTEEMDST DVSLLEEAMG
IIKELNKSLD KFELTQLLSG PYDKEGAVVY ITAGAGGTDA QDWADMLLRM YMRWGEKQRY
KTKVVEMSNG EEAGIKSATL EIEGRYAYGY ISGEKGTHRI VRQSPFNSKG LRQTSFSGVE
VMPLLPEEAV GIEIPEEDLD ISFTRAGGKG GQNVNKVETA VRITHIPTGV AVRCTEERSQ
LANKTRALIR LKAKLMVIAE EQRATEIKEI RGDAVKAEWG QQIRNYVFHP YKLVKDVRTG
HETSDITSVM DGDLDPFIKA YLKHKYTLAM ASAVTN
