PTAC5_ARATH
ID PTAC5_ARATH Reviewed; 387 AA.
AC A1A6M1; A0A1P8B4I4; Q9SVP5;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Protein disulfide isomerase pTAC5, chloroplastic {ECO:0000303|PubMed:23922206};
DE EC=5.3.4.1 {ECO:0000269|PubMed:23922206};
DE AltName: Full=Protein PLASTID TRANSCRIPTIONALLY ACTIVE 5 {ECO:0000303|PubMed:16326926};
DE Short=pTAC5 {ECO:0000303|PubMed:16326926};
DE Flags: Precursor;
GN Name=PTAC5 {ECO:0000303|PubMed:16326926};
GN OrderedLocusNames=At4g13670 {ECO:0000312|Araport:AT4G13670};
GN ORFNames=F18A5.60 {ECO:0000312|EMBL:CAB36831.1};
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 [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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND 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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, INTERACTION WITH HSP21,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23922206; DOI=10.1105/tpc.113.111229;
RA Zhong L., Zhou W., Wang H., Ding S., Lu Q., Wen X., Peng L., Zhang L.,
RA Lu C.;
RT "Chloroplast small heat shock protein HSP21 interacts with plastid nucleoid
RT protein pTAC5 and is essential for chloroplast development in Arabidopsis
RT under heat stress.";
RL Plant Cell 25:2925-2943(2013).
RN [6]
RP INTERACTION WITH FLN2.
RC STRAIN=cv. Columbia;
RX PubMed=24019900; DOI=10.1371/journal.pone.0073092;
RA Huang C., Yu Q.-B., Lv R.-H., Yin Q.-Q., Chen G.-Y., Xu L., Yang Z.-N.;
RT "The reduced plastid-encoded polymerase-dependent plastid gene expression
RT leads to the delayed greening of the Arabidopsis fln2 mutant.";
RL PLoS ONE 8:E73092-E73092(2013).
CC -!- FUNCTION: Exhibits zinc-dependent disulfide isomerase activity.
CC Required for seedling and chloroplast development under heat stress,
CC probably by maintaining plastid-encoded RNA polymerase (PEP)-dependent
CC transcription. {ECO:0000269|PubMed:23922206}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000269|PubMed:23922206};
CC -!- SUBUNIT: Interacts with HSP21; the formed complex associates with the
CC plastid-encoded RNA polymerase (PEP) complex not only during
CC transcription initiation, but also during elongation and termination,
CC and with a stronger efficiency in illuminated chloroplasts. Binds to
CC promoter regions of PEP-dependent genes, especially after a heat stress
CC (PubMed:23922206). Interacts with FLN2 (PubMed:24019900).
CC {ECO:0000269|PubMed:23922206, ECO:0000269|PubMed:24019900}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid
CC {ECO:0000269|PubMed:23922206}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A1A6M1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A1A6M1-2; Sequence=VSP_059090, VSP_059091;
CC -!- DISRUPTION PHENOTYPE: Ivory phenotype under heat stress.
CC {ECO:0000269|PubMed:23922206}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36831.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78409.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035528; CAB36831.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161537; CAB78409.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83311.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66498.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66499.1; -; Genomic_DNA.
DR EMBL; BT029541; ABL66797.1; -; mRNA.
DR PIR; T05236; T05236.
DR RefSeq; NP_001328389.1; NM_001340874.1. [A1A6M1-2]
DR RefSeq; NP_001328390.1; NM_001340872.1. [A1A6M1-2]
DR RefSeq; NP_193103.2; NM_117441.4. [A1A6M1-1]
DR AlphaFoldDB; A1A6M1; -.
DR SMR; A1A6M1; -.
DR IntAct; A1A6M1; 1.
DR MINT; A1A6M1; -.
DR STRING; 3702.AT4G13670.1; -.
DR iPTMnet; A1A6M1; -.
DR PaxDb; A1A6M1; -.
DR PRIDE; A1A6M1; -.
DR ProteomicsDB; 248844; -. [A1A6M1-1]
DR EnsemblPlants; AT4G13670.1; AT4G13670.1; AT4G13670. [A1A6M1-1]
DR EnsemblPlants; AT4G13670.2; AT4G13670.2; AT4G13670. [A1A6M1-2]
DR EnsemblPlants; AT4G13670.4; AT4G13670.4; AT4G13670. [A1A6M1-2]
DR GeneID; 827001; -.
DR Gramene; AT4G13670.1; AT4G13670.1; AT4G13670. [A1A6M1-1]
DR Gramene; AT4G13670.2; AT4G13670.2; AT4G13670. [A1A6M1-2]
DR Gramene; AT4G13670.4; AT4G13670.4; AT4G13670. [A1A6M1-2]
DR KEGG; ath:AT4G13670; -.
DR Araport; AT4G13670; -.
DR TAIR; locus:2119475; AT4G13670.
DR eggNOG; ENOG502QRN0; Eukaryota.
DR HOGENOM; CLU_718478_0_0_1; -.
DR InParanoid; A1A6M1; -.
DR OMA; VEEGAKC; -.
DR OrthoDB; 1216780at2759; -.
DR PhylomeDB; A1A6M1; -.
DR PRO; PR:A1A6M1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; A1A6M1; baseline and differential.
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; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:CACAO.
DR GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
DR GO; GO:0042793; P:plastid transcription; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IDA:UniProtKB.
DR Gene3D; 1.10.101.10; -; 1.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR Pfam; PF01471; PG_binding_1; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF57938; SSF57938; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Coiled coil; Isomerase; Metal-binding;
KW Plastid; Reference proteome; Stress response; Transcription;
KW Transcription regulation; Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 41..387
FT /note="Protein disulfide isomerase pTAC5, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441697"
FT ZN_FING 318..387
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT COILED 72..106
FT /evidence="ECO:0000255"
FT COILED 143..163
FT /evidence="ECO:0000255"
FT VAR_SEQ 262..278
FT /note="EAGNGAVFTSVTQVPEK -> SSYDRIWTPIVCFWQAC (in isoform
FT 2)"
FT /id="VSP_059090"
FT VAR_SEQ 279..387
FT /note="Missing (in isoform 2)"
FT /id="VSP_059091"
SQ SEQUENCE 387 AA; 44020 MW; 989E5E907014342B CRC64;
MASSSLPLSL PFPLRSLTST TRSLPFQCSP LFFSIPSSIV CFSTQNPDRE EVRWLREEQR
WIREEQRWIR EEQRWIRERE SLLQEISDLQ LRIQSLESRN SQLGNSIPDT ISNIAALLQV
LKEKNRISES GLSATPMVLE STREQIVEEV EEEEKRVIIA EEKVRVSEPV KKIKRRILKV
GSEGDDVQAL QEALLKLGFY SGEEDMEFSS FSSGTASAVK TWQASLGVRE DGVMTAELLQ
RLFMDEDVET DKDEASTMKK EEAGNGAVFT SVTQVPEKKQ SIVKDQSDRE VDVTQNRVFL
LGENRWEDPS RLIGRNKPVD RSESTNTKTR CITCRGEGRL MCLECDGTGE PNIEPQFMEW
VGEDTKCPYC EGLGYTVCDV CDGKKNL
