TRL22_ARATH
ID TRL22_ARATH Reviewed; 236 AA.
AC Q8LCT3; Q94F31; Q9SU84;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Thioredoxin-like 2-2, chloroplastic;
DE AltName: Full=Atypical cysteine/histidine-rich thioredoxin 2;
DE Short=AtACHT2;
DE Flags: Precursor;
GN OrderedLocusNames=At4g29670; ORFNames=T16L4.180;
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;
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] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825616; DOI=10.1093/mp/ssn076;
RA Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N.;
RT "Comparative genomic study of the thioredoxin family in photosynthetic
RT organisms with emphasis on Populus trichocarpa.";
RL Mol. Plant 2:308-322(2009).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19109414; DOI=10.1104/pp.108.128314;
RA Dangoor I., Peled-Zehavi H., Levitan A., Pasand O., Danon A.;
RT "A small family of chloroplast atypical thioredoxins.";
RL Plant Physiol. 149:1240-1250(2009).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase that may participate in
CC various redox reactions. Possesses insulin disulfide bonds reducing
CC activity. {ECO:0000269|PubMed:19109414}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19109414}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LCT3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LCT3-2; Sequence=VSP_011555;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC -!- CAUTION: The active site contains a CASC motif wich differs from the
CC conserved CGPC motif. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK62378.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL079344; CAB45327.1; -; Genomic_DNA.
DR EMBL; AL161575; CAB79725.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85659.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85660.1; -; Genomic_DNA.
DR EMBL; AF370616; AAK43935.1; -; mRNA.
DR EMBL; AF386933; AAK62378.1; ALT_INIT; mRNA.
DR EMBL; AY072462; AAL66877.1; -; mRNA.
DR EMBL; AY086416; AAM63418.1; -; mRNA.
DR PIR; T09930; T09930.
DR RefSeq; NP_567831.1; NM_119112.3. [Q8LCT3-2]
DR RefSeq; NP_849469.1; NM_179138.3. [Q8LCT3-1]
DR AlphaFoldDB; Q8LCT3; -.
DR SMR; Q8LCT3; -.
DR STRING; 3702.AT4G29670.2; -.
DR PaxDb; Q8LCT3; -.
DR PRIDE; Q8LCT3; -.
DR ProteomicsDB; 245236; -. [Q8LCT3-1]
DR EnsemblPlants; AT4G29670.1; AT4G29670.1; AT4G29670. [Q8LCT3-2]
DR EnsemblPlants; AT4G29670.2; AT4G29670.2; AT4G29670. [Q8LCT3-1]
DR GeneID; 829088; -.
DR Gramene; AT4G29670.1; AT4G29670.1; AT4G29670. [Q8LCT3-2]
DR Gramene; AT4G29670.2; AT4G29670.2; AT4G29670. [Q8LCT3-1]
DR KEGG; ath:AT4G29670; -.
DR Araport; AT4G29670; -.
DR TAIR; locus:2134443; AT4G29670.
DR eggNOG; KOG0907; Eukaryota.
DR InParanoid; Q8LCT3; -.
DR OMA; IHSTNEF; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q8LCT3; -.
DR PRO; PR:Q8LCT3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LCT3; baseline and differential.
DR Genevisible; Q8LCT3; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:TAIR.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chloroplast; Disulfide bond; Electron transport;
KW Plastid; Redox-active center; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..82
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 83..236
FT /note="Thioredoxin-like 2-2, chloroplastic"
FT /id="PRO_0000034170"
FT DOMAIN 83..220
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT ACT_SITE 138
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT DISULFID 135..138
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 200..236
FT /note="VKKAISVSPFPQLELGITLQTKRTTSLFFFDRIYQIL -> FQKIKDAIQLH
FT NTDRCSLGPAKVPEGLTLAKPAASS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_011555"
FT CONFLICT 85
FT /note="V -> L (in Ref. 4; AAM63418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 26337 MW; 7279192F2BF2A391 CRC64;
MAGVVRLTTT SVQAIRVSSS FSSFATALNP LQPCLPPNSN LNSDKRLRLL SSSPSCSSSH
YHPSSGLGSH LPLRRPKSQV VRVKVDENVA ETEPPKWWER NAPNMVDIHS TEEFLSALSG
AGERLVIVEF YGTWCASCRA LFPKLCKTAV EHPDIVFLKV NFDENKPMCK SLNVRVLPFF
HFYRGADGQL ESFSCSLAKV KKAISVSPFP QLELGITLQT KRTTSLFFFD RIYQIL
