TRXM2_ARATH
ID TRXM2_ARATH Reviewed; 186 AA.
AC Q9SEU8; Q56YG4; Q8LG26; Q9ZT79;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=Thioredoxin M2, chloroplastic {ECO:0000305};
DE Short=AtTrxm2 {ECO:0000303|PubMed:19825616};
DE Flags: Precursor;
GN Name=TRXM2 {ECO:0000303|PubMed:19825616};
GN OrderedLocusNames=At4g03520 {ECO:0000312|Araport:AT4G03520};
GN ORFNames=F9H3.15 {ECO:0000312|EMBL:AAD11594.1},
GN T5L23.1 {ECO:0000312|EMBL:AAD15308.1};
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 [MRNA].
RX PubMed=10580150; DOI=10.1016/s0378-1119(99)00448-5;
RA Mestres-Ortega D., Meyer Y.;
RT "The Arabidopsis thaliana genome encodes at least four thioredoxins m and a
RT new prokaryotic-like thioredoxin.";
RL Gene 240:307-316(1999).
RN [2]
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 [3]
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 [4]
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., 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 [5]
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., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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 [9]
RP INTERACTION WITH G6PD1 AND G6PD4.
RX PubMed=21309870; DOI=10.1111/j.1365-313x.2011.04535.x;
RA Meyer T., Hoelscher C., Schwoeppe C., von Schaewen A.;
RT "Alternative targeting of Arabidopsis plastidic glucose-6-phosphate
RT dehydrogenase G6PD1 involves cysteine-dependent interaction with G6PD4 in
RT the cytosol.";
RL Plant J. 66:745-758(2011).
RN [10]
RP INTERACTION WITH PGL3.
RX PubMed=24008768; DOI=10.1093/mp/sst126;
RA Hoelscher C., Meyer T., von Schaewen A.;
RT "Dual-targeting of Arabidopsis 6-phosphogluconolactonase 3 (PGL3) to
RT chloroplasts and peroxisomes involves interaction with Trx m2 in the
RT cytosol.";
RL Mol. Plant 7:252-255(2014).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase that may participate in
CC various redox reactions. May activate NADP-malate dehydrogenase.
CC -!- SUBUNIT: Interacts with G6PD1 and G6PD4 (PubMed:21309870). Interacts
CC with PGL3 (PubMed:24008768). {ECO:0000269|PubMed:21309870,
CC ECO:0000269|PubMed:24008768}.
CC -!- INTERACTION:
CC Q9SEU8; Q9SMX3: VDAC3; NbExp=4; IntAct=EBI-4475330, EBI-4457873;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19259774}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SEU8-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily.
CC {ECO:0000305}.
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DR EMBL; AF095750; AAF15949.1; -; mRNA.
DR EMBL; AC005142; AAD15308.1; -; Genomic_DNA.
DR EMBL; AF071527; AAD11594.1; -; Genomic_DNA.
DR EMBL; AL161497; CAB77837.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82333.1; -; Genomic_DNA.
DR EMBL; AY046001; AAK76675.1; -; mRNA.
DR EMBL; AY079362; AAL85093.1; -; mRNA.
DR EMBL; AK221358; BAD94225.1; -; mRNA.
DR EMBL; AY084496; AAM67285.1; -; mRNA.
DR PIR; F85044; F85044.
DR RefSeq; NP_192261.1; NM_116590.4. [Q9SEU8-1]
DR PDB; 7C3F; X-ray; 2.40 A; C/F/I/L/O/R/U/W=73-186.
DR PDBsum; 7C3F; -.
DR AlphaFoldDB; Q9SEU8; -.
DR SMR; Q9SEU8; -.
DR BioGRID; 10967; 4.
DR IntAct; Q9SEU8; 2.
DR MINT; Q9SEU8; -.
DR STRING; 3702.AT4G03520.1; -.
DR iPTMnet; Q9SEU8; -.
DR MetOSite; Q9SEU8; -.
DR PaxDb; Q9SEU8; -.
DR PRIDE; Q9SEU8; -.
DR ProteomicsDB; 232423; -. [Q9SEU8-1]
DR EnsemblPlants; AT4G03520.1; AT4G03520.1; AT4G03520. [Q9SEU8-1]
DR GeneID; 825653; -.
DR Gramene; AT4G03520.1; AT4G03520.1; AT4G03520. [Q9SEU8-1]
DR KEGG; ath:AT4G03520; -.
DR Araport; AT4G03520; -.
DR TAIR; locus:2128756; AT4G03520.
DR eggNOG; KOG0910; Eukaryota.
DR HOGENOM; CLU_090389_0_2_1; -.
DR InParanoid; Q9SEU8; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q9SEU8; -.
DR PRO; PR:Q9SEU8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SEU8; baseline and differential.
DR Genevisible; Q9SEU8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0008047; F:enzyme activator activity; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:TAIR.
DR InterPro; IPR005746; Thioredoxin.
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 TIGRFAMs; TIGR01068; thioredoxin; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Disulfide bond;
KW Electron transport; Plastid; Redox-active center; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 73..186
FT /note="Thioredoxin M2, chloroplastic"
FT /id="PRO_0000034163"
FT DOMAIN 73..186
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 104
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 111
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 112
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 110..113
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 92
FT /note="S -> F (in Ref. 1; AAF15949)"
FT /evidence="ECO:0000305"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:7C3F"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:7C3F"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:7C3F"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:7C3F"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:7C3F"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:7C3F"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:7C3F"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:7C3F"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:7C3F"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:7C3F"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:7C3F"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:7C3F"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:7C3F"
SQ SEQUENCE 186 AA; 20312 MW; 08EE6C4344BBCFD5 CRC64;
MAAFTCTSRP PISLRSETRI VSSSPSASSL SSRRMFAVLP ESSGLRIRLS LSPASLTSIH
QPRVSRLRRA VVCEAQETTT DIQVVNDSTW DSLVLKATGP VVVDFWAPWC GPCKMIDPLV
NDLAQHYTGK IKFYKLNTDE SPNTPGQYGV RSIPTIMIFV GGEKKDTIIG AVPKTTLTSS
LDKFLP
