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Database: UniProt
Entry: Q84JF5
LinkDB: Q84JF5
Original site: Q84JF5 
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   16-JAN-2019, entry version 106.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   Hayashizaki Y., 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
RT   plastid 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
RT   polymerase complex reveals building blocks for proper plastid
RT   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
RT   complex, Arabidopsis pTAC14, interacts with pTAC12/HEMERA and
RT   regulates plastid gene 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
RT   regulate 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
CC       by maintaining plastid-encoded RNA polymerase (PEP) activity.
CC       {ECO:0000269|PubMed:22010110}.
CC   -!- SUBUNIT: Component of the transcriptionally active chromosome
CC       (TAC) complexes. Interacts with PTAC12 and PTAC7.
CC       {ECO:0000269|PubMed:22010110, ECO:0000269|PubMed:23082802}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid
CC       {ECO:0000269|PubMed:22010110}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in leaves, flowers and
CC       seedlings, 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
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       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};
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   UniGene; At.32744; -.
DR   ProteinModelPortal; Q84JF5; -.
DR   IntAct; Q84JF5; 1.
DR   MINT; Q84JF5; -.
DR   STRING; 3702.AT4G20130.1; -.
DR   PaxDb; Q84JF5; -.
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; ENOG410IQFZ; Eukaryota.
DR   eggNOG; ENOG410ZB51; LUCA.
DR   HOGENOM; HOG000005778; -.
DR   InParanoid; Q84JF5; -.
DR   OMA; IWAMSIA; -.
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:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009534; C:chloroplast thylakoid; IDA:UniProtKB.
DR   GO; GO:0009295; C:nucleoid; IDA:TAIR.
DR   GO; GO:0009508; C:plastid chromosome; IDA:TAIR.
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   Pfam; PF09273; Rubis-subs-bind; 1.
DR   Pfam; PF00856; SET; 1.
DR   SUPFAM; SSF81822; SSF81822; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Complete proteome; Methyltransferase; Plastid;
KW   Reference proteome; S-adenosyl-L-methionine; Thylakoid; Transcription;
KW   Transcription regulation; Transferase; Transit peptide.
FT   TRANSIT       1     62       Chloroplast. {ECO:0000255}.
FT   CHAIN        63    483       Protein PLASTID TRANSCRIPTIONALLY ACTIVE
FT                                14. {ECO:0000255}.
FT                                /FTId=PRO_0000433436.
FT   DOMAIN       80    325       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   BINDING     324    324       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   CONFLICT    119    119       I -> V (in Ref. 4; BAD94330).
FT                                {ECO:0000305}.
FT   CONFLICT    300    300       K -> R (in Ref. 4; BAD94330).
FT                                {ECO:0000305}.
FT   CONFLICT    415    415       R -> S (in Ref. 4; BAF02006).
FT                                {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
//
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