TRL21_ARATH
ID TRL21_ARATH Reviewed; 221 AA.
AC Q8LEK4; Q2HIH3; Q9SZI7; Q9XFI0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Thioredoxin-like 2-1, chloroplastic;
DE AltName: Full=Atypical cysteine/histidine-rich thioredoxin 1;
DE Short=AtACHT1;
DE Flags: Precursor;
GN OrderedLocusNames=At4g26160; ORFNames=F20B18.270;
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].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 3-221.
RX PubMed=10498962; DOI=10.1016/s1360-1385(99)01475-2;
RA Meyer Y., Verdoucq L., Vignols F.;
RT "Plant thioredoxins and glutaredoxins: identity and putative roles.";
RL Trends Plant Sci. 4:388-394(1999).
RN [6]
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19259774; DOI=10.1007/s11103-009-9471-4;
RA Cain P., Hall M., Schroder W.P., Kieselbach T., Robinson C.;
RT "A novel extended family of stromal thioredoxins.";
RL Plant Mol. Biol. 70:273-281(2009).
RN [8]
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 stroma
CC {ECO:0000269|PubMed:19109414, ECO:0000269|PubMed:19259774}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC -!- CAUTION: The active site contains a CGSC motif wich differs from the
CC conserved CGPC motif. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD35006.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL049483; CAB39681.1; -; Genomic_DNA.
DR EMBL; AL161564; CAB79471.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85165.1; -; Genomic_DNA.
DR EMBL; BT024608; ABD43006.1; -; mRNA.
DR EMBL; AY085376; AAM62605.1; -; mRNA.
DR EMBL; AF144388; AAD35006.1; ALT_FRAME; mRNA.
DR PIR; T04271; T04271.
DR RefSeq; NP_194346.1; NM_118749.4.
DR PDB; 6LYW; X-ray; 1.70 A; A/B=74-204.
DR PDB; 6LYX; X-ray; 1.70 A; A/B=74-205.
DR PDBsum; 6LYW; -.
DR PDBsum; 6LYX; -.
DR AlphaFoldDB; Q8LEK4; -.
DR SMR; Q8LEK4; -.
DR STRING; 3702.AT4G26160.1; -.
DR iPTMnet; Q8LEK4; -.
DR PaxDb; Q8LEK4; -.
DR PRIDE; Q8LEK4; -.
DR ProteomicsDB; 245235; -.
DR EnsemblPlants; AT4G26160.1; AT4G26160.1; AT4G26160.
DR GeneID; 828722; -.
DR Gramene; AT4G26160.1; AT4G26160.1; AT4G26160.
DR KEGG; ath:AT4G26160; -.
DR Araport; AT4G26160; -.
DR TAIR; locus:2120860; AT4G26160.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_055041_1_0_1; -.
DR InParanoid; Q8LEK4; -.
DR OMA; HATITEM; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q8LEK4; -.
DR PRO; PR:Q8LEK4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LEK4; baseline and differential.
DR Genevisible; Q8LEK4; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; 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 GO; GO:0051776; P:detection of redox state; IMP:TAIR.
DR GO; GO:0010109; P:regulation of photosynthesis; IMP:TAIR.
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 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Disulfide bond; Electron transport; Plastid;
KW Redox-active center; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..73
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 74..221
FT /note="Thioredoxin-like 2-1, chloroplastic"
FT /id="PRO_0000034167"
FT DOMAIN 74..202
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 125
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT ACT_SITE 128
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT DISULFID 125..128
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 12
FT /note="S -> R (in Ref. 4; AAD35006)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="N -> S (in Ref. 3; AAM62605)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="N -> D (in Ref. 3; AAM62605)"
FT /evidence="ECO:0000305"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6LYX"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:6LYX"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:6LYX"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:6LYX"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:6LYX"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:6LYX"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6LYX"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:6LYX"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:6LYX"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:6LYX"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:6LYX"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:6LYX"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:6LYX"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:6LYX"
SQ SEQUENCE 221 AA; 24353 MW; CA1EBC58401D7403 CRC64;
MSPTTTSLRS LSFSLYASSN STPISTPIEA RQLLSSCNRF YGLSSSSSSS SLTTSSLIGN
LVFSSRNQSL SVKVQALAAE TEQPKWWERK AGPNMIDITS AEQFLNALKD AGDRLVIVDF
YGTWCGSCRA MFPKLCKTAK EHPNILFLKV NFDENKSLCK SLNVKVLPYF HFYRGADGQV
ESFSCSLAKF QKLREAIERH NVGSISNISS SASEKVEDSS E
