PTA14_ARATH
ID PTA14_ARATH Reviewed; 483 AA.
AC Q84JF5; O49439; O49440; Q0WLK1; Q56YC9;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein PLASTID TRANSCRIPTIONALLY ACTIVE 14 {ECO:0000303|PubMed:16326926};
DE Short=pTAC14 {ECO:0000303|PubMed:16326926};
DE EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU00190};
DE AltName: Full=Plastid-encoded RNA polymerase-associated protein 7 {ECO:0000303|PubMed:21949211};
DE Short=PEP-associated protein 7 {ECO:0000303|PubMed:21949211};
DE Flags: Precursor;
GN Name=PTAC14 {ECO:0000303|PubMed:16326926};
GN Synonyms=PAP7 {ECO:0000303|PubMed:21949211},
GN TAC14 {ECO:0000303|PubMed:16326926};
GN OrderedLocusNames=At4g20130 {ECO:0000312|Araport:AT4G20130};
GN ORFNames=F18F4 {ECO:0000312|EMBL:CAA16620.1},
GN F1C12.4 {ECO:0000312|EMBL:CAB79012.1};
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:AAO42203.1};
RN [1]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NOMENCLATURE.
RX PubMed=16326926; DOI=10.1105/tpc.105.036392;
RA Pfalz J., Liere K., Kandlbinder A., Dietz K.-J., Oelmueller R.;
RT "pTAC2, -6, and -12 are components of the transcriptionally active plastid
RT chromosome that are required for plastid gene expression.";
RL Plant Cell 18:176-197(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=21949211; DOI=10.1104/pp.111.184515;
RA Steiner S., Schroeter Y., Pfalz J., Pfannschmidt T.;
RT "Identification of essential subunits in the plastid-encoded RNA polymerase
RT complex reveals building blocks for proper plastid development.";
RL Plant Physiol. 157:1043-1055(2011).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PTAC12, INDUCTION BY
RP LIGHT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=22010110; DOI=10.1104/pp.111.184762;
RA Gao Z.-P., Yu Q.-B., Zhao T.-T., Ma Q., Chen G.-X., Yang Z.-N.;
RT "A functional component of the transcriptionally active chromosome complex,
RT Arabidopsis pTAC14, interacts with pTAC12/HEMERA and regulates plastid gene
RT expression.";
RL Plant Physiol. 157:1733-1745(2011).
RN [8]
RP REVIEW.
RX PubMed=22902688; DOI=10.4161/psb.21618;
RA Gao Z.-P., Chen G.-X., Yang Z.-N.;
RT "Regulatory role of Arabidopsis pTAC14 in chloroplast development and
RT plastid gene expression.";
RL Plant Signal. Behav. 7:1354-1356(2012).
RN [9]
RP INTERACTION WITH PTAC7.
RX PubMed=23082802; DOI=10.1111/j.1399-3054.2012.01718.x;
RA Yu Q.-B., Lu Y., Ma Q., Zhao T.-T., Huang C., Zhao H.-F., Zhang X.-L.,
RA Lv R.-H., Yang Z.-N.;
RT "TAC7, an essential component of the plastid transcriptionally active
RT chromosome complex, interacts with FLN1, TAC10, TAC12 and TAC14 to regulate
RT chloroplast gene expression in Arabidopsis thaliana.";
RL Physiol. Plantarum 148:408-421(2013).
CC -!- FUNCTION: Essential for chloroplast development, especially for
CC thylakoid formation. Involved in plastid gene expression, probably by
CC maintaining plastid-encoded RNA polymerase (PEP) activity.
CC {ECO:0000269|PubMed:22010110}.
CC -!- SUBUNIT: Component of the transcriptionally active chromosome (TAC)
CC complexes. Interacts with PTAC12 and PTAC7.
CC {ECO:0000269|PubMed:22010110, ECO:0000269|PubMed:23082802}.
CC -!- INTERACTION:
CC Q84JF5; Q9LRH6: GATA25; NbExp=3; IntAct=EBI-7890317, EBI-2460434;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid
CC {ECO:0000269|PubMed:22010110}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, flowers and seedlings,
CC and, to a lower extent, in stems and roots.
CC {ECO:0000269|PubMed:22010110}.
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:22010110}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethal, even with Suc as a carbon
CC source. Impaired thylakoid formation in the initial process of
CC chloroplast development leading to albino seedlings unable to grow
CC photoautotrophically. Reduced plastid-encoded RNA polymerase (PEP)
CC activity. {ECO:0000269|PubMed:22010110}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16620.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA16621.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79012.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79013.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021637; CAA16620.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL021637; CAA16621.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161552; CAB79012.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161552; CAB79013.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84278.1; -; Genomic_DNA.
DR EMBL; BT004184; AAO42203.1; -; mRNA.
DR EMBL; BT005475; AAO63895.1; -; mRNA.
DR EMBL; AK221394; BAD94330.1; -; mRNA.
DR EMBL; AK230198; BAF02006.1; -; mRNA.
DR EMBL; AK230206; BAF02014.1; -; mRNA.
DR PIR; T04896; T04896.
DR PIR; T04897; T04897.
DR RefSeq; NP_193746.3; NM_118132.5.
DR AlphaFoldDB; Q84JF5; -.
DR SMR; Q84JF5; -.
DR IntAct; Q84JF5; 2.
DR MINT; Q84JF5; -.
DR STRING; 3702.AT4G20130.1; -.
DR PaxDb; Q84JF5; -.
DR PRIDE; Q84JF5; -.
DR ProteomicsDB; 248777; -.
DR EnsemblPlants; AT4G20130.1; AT4G20130.1; AT4G20130.
DR GeneID; 827759; -.
DR Gramene; AT4G20130.1; AT4G20130.1; AT4G20130.
DR KEGG; ath:AT4G20130; -.
DR Araport; AT4G20130; -.
DR TAIR; locus:2119822; AT4G20130.
DR eggNOG; KOG1337; Eukaryota.
DR HOGENOM; CLU_027029_1_0_1; -.
DR InParanoid; Q84JF5; -.
DR OMA; FWERNWH; -.
DR OrthoDB; 1209399at2759; -.
DR PhylomeDB; Q84JF5; -.
DR PRO; PR:Q84JF5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84JF5; baseline and differential.
DR Genevisible; Q84JF5; AT.
DR GO; GO:0042644; C:chloroplast nucleoid; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; IDA:UniProtKB.
DR GO; GO:0000427; C:plastid-encoded plastid RNA polymerase complex; IDA:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR GO; GO:0042793; P:plastid transcription; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:UniProtKB.
DR Gene3D; 3.90.1420.10; -; 1.
DR InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF09273; Rubis-subs-bind; 1.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF81822; SSF81822; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Methyltransferase; Plastid; Reference proteome;
KW S-adenosyl-L-methionine; Thylakoid; Transcription;
KW Transcription regulation; Transferase; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..483
FT /note="Protein PLASTID TRANSCRIPTIONALLY ACTIVE 14"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433436"
FT DOMAIN 80..325
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 324
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT CONFLICT 119
FT /note="I -> V (in Ref. 4; BAD94330)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="K -> R (in Ref. 4; BAD94330)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="R -> S (in Ref. 4; BAF02006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 55611 MW; BECC74FDB3BDF1CA CRC64;
MASSVSLQFL TNTFISKPQG FCNGIVSAPR PRSNLLRDRQ NGVRPIKVAS IETQPFPLFQ
SPASEESSSS ELETADPDFY KIGYVRSVRA YGVEFKEGPD GFGVYASKDI EPRRRARVIM
EIPLELMITI RQKHPWMFFP DIVPIGHPIF DIINSTDPEI DWDIRLACLL LFSFDRDDHF
WRLYGDFLPA ADECSSLLLA TEEDLAELQD PDLVSTIRQQ QKRILDFWEK NWHSGVPLKI
KRLAEDPERF IWAVSMAQTR CISMQTRVGA LVQELNMMIP YADMLNHSFE PNCFLHWRPK
DRMLEVMSNA GQDIKKGEEM TINYMPGQKN NMLMERYGFS TPVNPWDAIK FSGDSRIHLN
SFLSVFNIYG LPEEYYHDSE LSRGDTFVDG AVIAAARTLP TWSDIDLPPI PSAERKAVKE
LQDECRKMLA EYPTTAEQDQ KLLDSMSEAR TTFATAVKYR MHRKMFIGKI IKALDIYQER
LLY
