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Database: UniProt
Entry: Q9SEU7
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Original site: Q9SEU7 
ID   TRXM3_ARATH             Reviewed;         173 AA.
AC   Q9SEU7; Q42072; Q67XN4; Q67ZH7; Q681Y9; Q9SKS6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Thioredoxin M3, chloroplastic;
DE            Short=AtTrxm3;
DE   AltName: Full=Protein GFP ARRESTED TRAFFICKING 1;
DE   Flags: Precursor;
GN   Name=GAT1; OrderedLocusNames=At2g15570; ORFNames=F9O13.12;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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;
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-173.
RC   STRAIN=cv. Columbia; TISSUE=Seedling;
RX   PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA   Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA   Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA   Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA   Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA   Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA   Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT   "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT   a set of 5000 non-redundant ESTs.";
RL   Plant J. 9:101-124(1996).
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   FUNCTION.
RX   PubMed=19820302;
RA   Benitez-Alfonso Y., Jackson D.;
RT   "Redox homeostasis regulates plasmodesmal communication in Arabidopsis
RT   meristems.";
RL   Plant Signal. Behav. 4:655-659(2009).
RN   [10]
RP   FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=19218459; DOI=10.1073/pnas.0808717106;
RA   Benitez-Alfonso Y., Cilia M., San Roman A., Thomas C., Maule A., Hearn S.,
RA   Jackson D.;
RT   "Control of Arabidopsis meristem development by thioredoxin-dependent
RT   regulation of intercellular transport.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:3615-3620(2009).
CC   -!- FUNCTION: Thiol-disulfide oxidoreductase required for maintaining
CC       symplastic permeability in the meristem. Involved in redox regulation
CC       of callose deposition, plasmodesmata cell-to-cell communication and
CC       meristem maintenance. {ECO:0000269|PubMed:19218459,
CC       ECO:0000269|PubMed:19820302}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:19218459, 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=Q9SEU7-1; Sequence=Displayed;
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis in the root
CC       meristem at the transition from heart to torpedo stage. At the
CC       cotyledon stage, expressed in root and shoot meristems, with weak
CC       expression in provascular tissues. Expressed later in the seedling root
CC       meristem, shoot apex, and vasculature. During flowering, expressed in
CC       inflorescence and floral meristems, and in petal, stamen, and carpel
CC       primordia. {ECO:0000269|PubMed:19218459}.
CC   -!- DISRUPTION PHENOTYPE: Seedling lethality when homozygous. Increased
CC       callose deposition and accumulation of reactive oxygen species in
CC       roots. {ECO:0000269|PubMed:19218459}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF095751; AAF15950.1; -; mRNA.
DR   EMBL; AC006248; AAD17401.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06417.1; -; Genomic_DNA.
DR   EMBL; AK175478; BAD43241.1; -; mRNA.
DR   EMBL; AK176140; BAD43903.1; -; mRNA.
DR   EMBL; AK176784; BAD44547.1; -; mRNA.
DR   EMBL; BT025735; ABF83625.1; -; mRNA.
DR   EMBL; Z26209; CAA81191.1; -; mRNA.
DR   PIR; F84530; F84530.
DR   RefSeq; NP_179159.1; NM_127118.4. [Q9SEU7-1]
DR   AlphaFoldDB; Q9SEU7; -.
DR   SMR; Q9SEU7; -.
DR   STRING; 3702.Q9SEU7; -.
DR   PaxDb; 3702-AT2G15570-2; -.
DR   ProteomicsDB; 232396; -. [Q9SEU7-1]
DR   EnsemblPlants; AT2G15570.1; AT2G15570.1; AT2G15570. [Q9SEU7-1]
DR   GeneID; 816050; -.
DR   Gramene; AT2G15570.1; AT2G15570.1; AT2G15570. [Q9SEU7-1]
DR   KEGG; ath:AT2G15570; -.
DR   Araport; AT2G15570; -.
DR   TAIR; AT2G15570; ATHM3.
DR   eggNOG; KOG0910; Eukaryota.
DR   HOGENOM; CLU_090389_0_2_1; -.
DR   InParanoid; Q9SEU7; -.
DR   OMA; AASTFHC; -.
DR   PhylomeDB; Q9SEU7; -.
DR   PRO; PR:Q9SEU7; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SEU7; baseline and differential.
DR   Genevisible; Q9SEU7; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0009570; C:chloroplast stroma; TAS:UniProtKB.
DR   GO; GO:0045454; P:cell redox homeostasis; IMP:UniProtKB.
DR   GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; IMP:UniProtKB.
DR   GO; GO:0010647; P:positive regulation of cell communication; IMP:UniProtKB.
DR   GO; GO:0048509; P:regulation of meristem development; IMP:UniProtKB.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF21; THIOREDOXIN M3, CHLOROPLASTIC; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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..67
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           68..173
FT                   /note="Thioredoxin M3, chloroplastic"
FT                   /id="PRO_0000034164"
FT   DOMAIN          68..173
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        96
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        99
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            97
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            98
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        96..99
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        110
FT                   /note="A -> T (in Ref. 4; BAD43241)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        124
FT                   /note="A -> E (in Ref. 1; AAF15950)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136
FT                   /note="I -> V (in Ref. 4; BAD44547)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   173 AA;  19500 MW;  F103CA26FCB87613 CRC64;
     MAISSSSSSI CFNPTRFHTA RHISSPSRLF PVTSFSPRSL RFSDRRSLLS SSASRLRLSP
     LCVRDSRAAE VTQRSWEDSV LKSETPVLVE FYTSWCGPCR MVHRIIDEIA GDYAGKLNCY
     LLNADNDLPV AEEYEIKAVP VVLLFKNGEK RESIMGTMPK EFYISAIERV LNS
//
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