CF107_ARATH
ID CF107_ARATH Reviewed; 652 AA.
AC Q8RWG2; Q9LSP3;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Protein high chlorophyll fluorescent 107 {ECO:0000312|EMBL:AEE75897.1};
DE Flags: Precursor;
GN Name=HCF107 {ECO:0000312|EMBL:AEE75897.1};
GN Synonyms=MBB1 {ECO:0000303|PubMed:15505214};
GN OrderedLocusNames=At3g17040 {ECO:0000312|Araport:AT3G17040};
GN ORFNames=K14A17.11 {ECO:0000312|EMBL:BAA94982.1};
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 {ECO:0000312|EMBL:AAM13111.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11549768; DOI=10.2307/3871432;
RA Felder S., Meierhoff K., Sane A.P., Meurer J., Driemel C., Pluecken H.,
RA Klaff P., Stein B., Bechtold N., Westhoff P.;
RT "The nucleus-encoded HCF107 gene of Arabidopsis provides a link between
RT intercistronic RNA processing and the accumulation of translation-competent
RT psbH transcripts in chloroplasts.";
RL Plant Cell 13:2127-2141(2001).
RN [5]
RP INDUCTION BY RED LIGHT.
RX PubMed=15505214; DOI=10.1073/pnas.0407107101;
RA Monte E., Tepperman J.M., Al-Sady B., Kaczorowski K.A., Alonso J.M.,
RA Ecker J.R., Li X., Zhang Y., Quail P.H.;
RT "The phytochrome-interacting transcription factor, PIF3, acts early,
RT selectively, and positively in light-induced chloroplast development.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16091-16098(2004).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ALA-244, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=15918885; DOI=10.1111/j.1365-313x.2005.02409.x;
RA Sane A.P., Stein B., Westhoff P.;
RT "The nuclear gene HCF107 encodes a membrane-associated R-TPR (RNA
RT tetratricopeptide repeat)-containing protein involved in expression of the
RT plastidial psbH gene in Arabidopsis.";
RL Plant J. 42:720-730(2005).
RN [7]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=22451905; DOI=10.1073/pnas.1200318109;
RA Hammani K., Cook W.B., Barkan A.;
RT "RNA binding and RNA remodeling activities of the half-a-tetratricopeptide
RT (HAT) protein HCF107 underlie its effects on gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5651-5656(2012).
CC -!- FUNCTION: Involved, directly or indirectly, in the processing of
CC chloroplast encoded mRNAs. Exhibits sequence-specific RNA binding and
CC RNA remodeling activities, probably leading to the activation of
CC translation of the target gene cluster psbB-psbT-psbH-petB-petD
CC (PubMed:22451905). Blocks 5'-3' and 3'-5' exoribonucleases (e.g.
CC polynucleotide phosphorylase (PNPase), RNase R) in vitro
CC (PubMed:22451905). Necessary for intercistronic RNA processing of the
CC psbH 5' untranslated region or the stabilization of 5' processed psbH
CC RNAs. Also required for the synthesis of psbB (PubMed:11549768,
CC PubMed:15918885, PubMed:22451905). {ECO:0000269|PubMed:11549768,
CC ECO:0000269|PubMed:15918885, ECO:0000269|PubMed:22451905}.
CC -!- SUBUNIT: May form homomultimers (PubMed:22451905). Part of a multi-
CC subunit complex in the range of 60-190 and 600-800 kDa in chloroplast
CC membranes (PubMed:15918885). {ECO:0000269|PubMed:15918885,
CC ECO:0000269|PubMed:22451905}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. Plastid,
CC chloroplast membrane {ECO:0000269|PubMed:15918885}; Peripheral membrane
CC protein {ECO:0000269|PubMed:15918885}; Stromal side
CC {ECO:0000269|PubMed:15918885}. Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:15918885}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist. {ECO:0000305};
CC Name=1;
CC IsoId=Q8RWG2-1; Sequence=Displayed;
CC -!- INDUCTION: By continuous red light (Rc at 8 umol.m-2.s-1).
CC {ECO:0000269|PubMed:15505214}.
CC -!- DISRUPTION PHENOTYPE: In hcf107-2, reduced accumulation of 5'-end-
CC processed psbH transcript, as well as psbB translation, resulting in
CC disruption of photosystem II (PSII) and seedling lethal plants.
CC Specific loss of processed RNAs with a 5' end 44nt upstream of the psbH
CC start codon in the psbB-psbT-psbH-petB-petD gene cluster.
CC {ECO:0000269|PubMed:11549768, ECO:0000269|PubMed:15918885,
CC ECO:0000269|PubMed:22451905}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA94982.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB026636; BAA94982.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75897.1; -; Genomic_DNA.
DR EMBL; AY093112; AAM13111.1; -; mRNA.
DR EMBL; BT008405; AAP37764.1; -; mRNA.
DR RefSeq; NP_188329.1; NM_112580.5. [Q8RWG2-1]
DR AlphaFoldDB; Q8RWG2; -.
DR SMR; Q8RWG2; -.
DR STRING; 3702.AT3G17040.1; -.
DR iPTMnet; Q8RWG2; -.
DR PaxDb; Q8RWG2; -.
DR ProteomicsDB; 224484; -. [Q8RWG2-1]
DR EnsemblPlants; AT3G17040.1; AT3G17040.1; AT3G17040. [Q8RWG2-1]
DR GeneID; 820961; -.
DR Gramene; AT3G17040.1; AT3G17040.1; AT3G17040. [Q8RWG2-1]
DR KEGG; ath:AT3G17040; -.
DR Araport; AT3G17040; -.
DR TAIR; locus:2086132; AT3G17040.
DR eggNOG; KOG1124; Eukaryota.
DR InParanoid; Q8RWG2; -.
DR OrthoDB; 1390778at2759; -.
DR PhylomeDB; Q8RWG2; -.
DR PRO; PR:Q8RWG2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RWG2; baseline and differential.
DR Genevisible; Q8RWG2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:TAIR.
DR GO; GO:0006397; P:mRNA processing; IMP:TAIR.
DR GO; GO:1901918; P:negative regulation of exoribonuclease activity; IDA:TAIR.
DR GO; GO:0009657; P:plastid organization; IMP:TAIR.
DR GO; GO:0006417; P:regulation of translation; IMP:UniProtKB.
DR GO; GO:0010114; P:response to red light; IEP:UniProtKB.
DR GO; GO:0006396; P:RNA processing; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR044624; Mbb1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44917; PTHR44917; 1.
DR SMART; SM00386; HAT; 9.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Membrane; mRNA processing; Plastid;
KW Reference proteome; Repeat; RNA-binding; TPR repeat; Transit peptide.
FT TRANSIT 1..68
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 69..652
FT /note="Protein high chlorophyll fluorescent 107"
FT /id="PRO_0000433486"
FT REPEAT 168..201
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 202..235
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 237..270
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 271..304
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 305..338
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 339..372
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 374..406
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REPEAT 407..440
FT /note="TPR 8"
FT /evidence="ECO:0000255"
FT REPEAT 441..474
FT /note="TPR 9"
FT /evidence="ECO:0000255"
FT REPEAT 478..511
FT /note="TPR 10"
FT /evidence="ECO:0000255"
FT REPEAT 543..576
FT /note="TPR 11"
FT /evidence="ECO:0000255"
FT REPEAT 598..631
FT /note="TPR 12"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 244
FT /note="A->T: In hcf107-1; reduced accumulation of 5'-end-
FT processed psbH transcript and reduced psbB translation,
FT resulting in disruption of photosystem II (PSII) and
FT seedling lethal plants."
FT /evidence="ECO:0000269|PubMed:15918885"
SQ SEQUENCE 652 AA; 73471 MW; 6342D043BD93034C CRC64;
MHFFFVPNSS SSSPSPANTS SFSLSFLTPQ IPENLCKSPT KIHIGTHGIS GQSFLSHPTF
SSKNTYLYAV VDRSSSGVFS PQKESANGEG EESNTEEGVL VVRRPLLENS DKESSEEEGK
KYPARIDAGL SNIAKKMPIF EPERSESSSS SSAAAAARAQ ERPLAVNLDL SLYKAKVLAR
NFRYKDAEKI LEKCIAYWPE DGRPYVALGK ILSKQSKLAE ARILYEKGCQ STQGENSYIW
QCWAVLENRL GNVRRARELF DAATVADKKH VAAWHGWANL EIKQGNISKA RNLLAKGLKF
CGRNEYIYQT LALLEAKAGR YEQARYLFKQ ATICNSRSCA SWLAWAQLEI QQERYPAARK
LFEKAVQASP KNRFAWHVWG VFEAGVGNVE RGRKLLKIGH ALNPRDPVLL QSLGLLEYKH
SSANLARALL RRASELDPRH QPVWIAWGWM EWKEGNTTTA RELYQRALSI DANTESASRC
LQAWGVLEQR AGNLSAARRL FRSSLNINSQ SYVTWMTWAQ LEEDQGDTER AEEIRNLYFQ
QRTEVVDDAS WVTGFLDIID PALDTVKRLL NFGQNNDNNR LTTTLRNMNR TKDSQSNQQP
ESSAGREDIE TGSGFNLDVF LRSKLSLDPL KLDVNLDSKR LERFTRGRIN GA
