PTA16_ARATH
ID PTA16_ARATH Reviewed; 510 AA.
AC Q9STF2; Q9ASP7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein PLASTID TRANSCRIPTIONALLY ACTIVE 16, chloroplastic {ECO:0000303|PubMed:16326926};
DE Short=pTAC16 {ECO:0000303|PubMed:16326926};
DE Flags: Precursor;
GN Name=PTAC16 {ECO:0000303|PubMed:16326926};
GN OrderedLocusNames=At3g46780 {ECO:0000312|EMBL:AEE78204.1};
GN ORFNames=T6H20.190 {ECO:0000312|EMBL:CAB51187.1};
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|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 2).
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 SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND THR-451, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, PTM, AND PHOSPHORYLATION AT
RP THR-451.
RC STRAIN=cv. Columbia;
RX PubMed=22616989; DOI=10.1016/j.febslet.2012.03.061;
RA Ingelsson B., Vener A.V.;
RT "Phosphoproteomics of Arabidopsis chloroplasts reveals involvement of the
RT STN7 kinase in phosphorylation of nucleoid protein pTAC16.";
RL FEBS Lett. 586:1265-1271(2012).
RN [7]
RP INTERACTION WITH DEGP1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=21877139; DOI=10.1007/s00425-011-1505-x;
RA Zienkiewicz M., Ferenc A., Wasilewska W., Romanowska E.;
RT "High light stimulates Deg1-dependent cleavage of the minor LHCII antenna
RT proteins CP26 and CP29 and the PsbS protein in Arabidopsis thaliana.";
RL Planta 235:279-288(2012).
RN [8]
RP INTERACTION WITH CSP3.
RX PubMed=23334891; DOI=10.1007/s12192-012-0398-3;
RA Kim M.H., Sonoda Y., Sasaki K., Kaminaka H., Imai R.;
RT "Interactome analysis reveals versatile functions of Arabidopsis COLD SHOCK
RT DOMAIN PROTEIN 3 in RNA processing within the nucleus and cytoplasm.";
RL Cell Stress Chaperones 18:517-525(2013).
CC -!- FUNCTION: Probably involved in the regulation of plastid gene
CC expression. {ECO:0000305}.
CC -!- SUBUNIT: Component of the plastid transcriptionally active chromosome
CC required for plastid gene expression (PubMed:16326926). Interacts with
CC DEGP1 under high light conditions and maybe its degradation target
CC (PubMed:21877139). {ECO:0000269|PubMed:16326926,
CC ECO:0000269|PubMed:21877139}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid
CC {ECO:0000269|PubMed:16326926, ECO:0000269|PubMed:22616989}. Plastid,
CC chloroplast thylakoid membrane {ECO:0000269|PubMed:21877139,
CC ECO:0000269|PubMed:22616989}; Peripheral membrane protein
CC {ECO:0000269|PubMed:22616989}; Stromal side
CC {ECO:0000269|PubMed:22616989}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9STF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9STF2-2; Sequence=VSP_057905, VSP_057906;
CC -!- PTM: Excluded from chloroplast nucleoid when phosphorylated on Thr-451
CC by STN7 that may regulate membrane-anchoring functions of the nucleoid.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype and normal nucleoids.
CC {ECO:0000269|PubMed:22616989}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AL096859; CAB51187.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78204.1; -; Genomic_DNA.
DR EMBL; AF367356; AAK32942.1; -; mRNA.
DR EMBL; AY143885; AAN28824.1; -; mRNA.
DR PIR; T12970; T12970.
DR RefSeq; NP_566886.2; NM_114545.3. [Q9STF2-1]
DR AlphaFoldDB; Q9STF2; -.
DR IntAct; Q9STF2; 3.
DR MINT; Q9STF2; -.
DR STRING; 3702.AT3G46780.1; -.
DR iPTMnet; Q9STF2; -.
DR PaxDb; Q9STF2; -.
DR PRIDE; Q9STF2; -.
DR ProMEX; Q9STF2; -.
DR ProteomicsDB; 248678; -. [Q9STF2-1]
DR EnsemblPlants; AT3G46780.1; AT3G46780.1; AT3G46780. [Q9STF2-1]
DR GeneID; 823831; -.
DR Gramene; AT3G46780.1; AT3G46780.1; AT3G46780. [Q9STF2-1]
DR KEGG; ath:AT3G46780; -.
DR Araport; AT3G46780; -.
DR TAIR; locus:2102842; AT3G46780.
DR eggNOG; KOG1203; Eukaryota.
DR HOGENOM; CLU_043457_0_0_1; -.
DR InParanoid; Q9STF2; -.
DR OMA; PESSYKI; -.
DR OrthoDB; 822727at2759; -.
DR PhylomeDB; Q9STF2; -.
DR PRO; PR:Q9STF2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STF2; baseline and differential.
DR Genevisible; Q9STF2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0042644; C:chloroplast nucleoid; IDA:UniProtKB.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0098572; C:stromal side of plastid thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF13460; NAD_binding_10; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Coiled coil; Membrane; NADP;
KW Phosphoprotein; Plastid; Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..19
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 20..510
FT /note="Protein PLASTID TRANSCRIPTIONALLY ACTIVE 16,
FT chloroplastic"
FT /id="PRO_0000434135"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 354..403
FT /evidence="ECO:0000255"
FT COMPBIAS 39..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94..123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 451
FT /note="Phosphothreonine; by STN7"
FT /evidence="ECO:0000269|PubMed:22616989,
FT ECO:0007744|PubMed:19376835"
FT VAR_SEQ 297
FT /note="P -> M (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_057905"
FT VAR_SEQ 298..510
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_057906"
SQ SEQUENCE 510 AA; 54358 MW; 2A945F30DC9D6B11 CRC64;
MASSSTSFPL TTAPPQGVRF NRRKPRLTVW AKQTAFQLGK TKGDDDSEGK QKGKNPFQFD
FGKLPDMKSL IPVVTNPSTG LVFGNNRKKD PGTIFVAGAT GQAGIRIAQT LLQRGFSVRA
GVPDLGAAQD LARVAATYKI LSNDEVKRLN AVQSPFQDAE SIAKAIGNAT KVVVTVGATE
NGPDAQVSTS DALLVVQAAE LAGVSHVAIV YDGTISGSTY NVLDGITSFF GNLFAKSQPL
TISDLIEKVA QTDVAYTLIK TSLTEDFSPE KAYNVVVSAE GSNSGSGSSS SEAYKVPKLK
IASLVADIFA NTAVAENKVV EVSTDPSAPS RPVDELFSVI PEDGRRKVYA DAIARERAEE
EAKVAADKAR EAAEAAKEFE KQMQKLSEKE AEAASLAEDA QQKADAVGVT VDGLFNKAKD
ISSGLSWNKL GSQFATAIQN ASETPKVQVA TVRGQAKARN LPPKKAVVKQ RPSSPFASKP
KEERPKKPEK EVRKVFGGLF KQETIYIDDD
