TRXM4_ARATH
ID TRXM4_ARATH Reviewed; 193 AA.
AC Q9SEU6; Q0WUS9; Q9LDP6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 25-MAY-2022, entry version 160.
DE RecName: Full=Thioredoxin M4, chloroplastic;
DE Short=AtTrxm4;
DE Flags: Precursor;
GN OrderedLocusNames=At3g15360; ORFNames=MJK13.2;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
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 [5]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-193.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=19631646; DOI=10.1016/j.febslet.2009.07.035;
RA Nee G., Zaffagnini M., Trost P., Issakidis-Bourguet E.;
RT "Redox regulation of chloroplastic glucose-6-phosphate dehydrogenase: a new
RT role for f-type thioredoxin.";
RL FEBS Lett. 583:2827-2832(2009).
RN [9]
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 [10]
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).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase involved in the redox
CC regulation of enzyme of the oxidative pentose phosphate pathway. Under
CC reducing conditions, inhibits the glucose-6-phosphate dehydrogenase.
CC {ECO:0000269|PubMed:19631646}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19259774}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily.
CC {ECO:0000305}.
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DR EMBL; AF095752; AAF15951.1; -; mRNA.
DR EMBL; AB022218; BAB02365.1; -; Genomic_DNA.
DR EMBL; AC024081; AAF35402.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75659.1; -; Genomic_DNA.
DR EMBL; AF375443; AAK53027.1; -; mRNA.
DR EMBL; AY060538; AAL31169.1; -; mRNA.
DR EMBL; AY088157; AAM65701.1; -; mRNA.
DR EMBL; AK227059; BAE99119.1; -; mRNA.
DR RefSeq; NP_188155.1; NM_112404.5.
DR AlphaFoldDB; Q9SEU6; -.
DR SMR; Q9SEU6; -.
DR BioGRID; 6109; 7.
DR IntAct; Q9SEU6; 6.
DR STRING; 3702.AT3G15360.1; -.
DR iPTMnet; Q9SEU6; -.
DR PaxDb; Q9SEU6; -.
DR PRIDE; Q9SEU6; -.
DR ProteomicsDB; 234648; -.
DR EnsemblPlants; AT3G15360.1; AT3G15360.1; AT3G15360.
DR GeneID; 820775; -.
DR Gramene; AT3G15360.1; AT3G15360.1; AT3G15360.
DR KEGG; ath:AT3G15360; -.
DR Araport; AT3G15360; -.
DR TAIR; locus:2090126; AT3G15360.
DR eggNOG; KOG0910; Eukaryota.
DR HOGENOM; CLU_090389_0_0_1; -.
DR InParanoid; Q9SEU6; -.
DR OMA; ANSFTSH; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q9SEU6; -.
DR PRO; PR:Q9SEU6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SEU6; baseline and differential.
DR Genevisible; Q9SEU6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; 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; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0008047; F:enzyme activator activity; IDA:TAIR.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
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:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:TAIR.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IDA:UniProtKB.
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 2: Evidence at transcript level;
KW Chloroplast; Disulfide bond; Electron transport; Plastid;
KW Redox-active center; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..82
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 83..193
FT /note="Thioredoxin M4, chloroplastic"
FT /id="PRO_0000034165"
FT DOMAIN 83..192
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 117
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 118
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 116..119
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 151
FT /note="A -> P (in Ref. 1; AAF15951)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 193 AA; 21172 MW; 7189545252C60D9D CRC64;
MASLLDSVTV TRVFSLPIAA SVSSSSAAPS VSRRRISPAR FLEFRGLKSS RSLVTQSASL
GANRRTRIAR GGRIACEAQD TTAAAVEVPN LSDSEWQTKV LESDVPVLVE FWAPWCGPCR
MIHPIVDQLA KDFAGKFKFY KINTDESPNT ANRYGIRSVP TVIIFKGGEK KDSIIGAVPR
ETLEKTIERF LVE
