TRXH9_ARATH
ID TRXH9_ARATH Reviewed; 140 AA.
AC Q9C9Y6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Thioredoxin H9;
DE Short=AtTrxh9;
DE AltName: Full=Thioredoxin 9;
DE Short=AtTRX9;
GN Name=TRX9; Synonyms=ATH9; OrderedLocusNames=At3g08710; ORFNames=F17O14.18;
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=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 [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 Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15619004; DOI=10.1007/s00018-004-4296-4;
RA Gelhaye E., Rouhier N., Navrot N., Jacquot J.P.;
RT "The plant thioredoxin system.";
RL Cell. Mol. Life Sci. 62:24-35(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-136, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-2
RP AND CYS-4, MYRISTOYLATION AT GLY-2, AND PALMITOYLATION AT CYS-4.
RX PubMed=20133584; DOI=10.1073/pnas.0913759107;
RA Meng L., Wong J.H., Feldman L.J., Lemaux P.G., Buchanan B.B.;
RT "A membrane-associated thioredoxin required for plant growth moves from
RT cell to cell, suggestive of a role in intercellular communication.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3900-3905(2010).
CC -!- FUNCTION: Probable thiol-disulfide oxidoreductase that may play a role
CC in intercellular communication due to its ability to move from cell to
CC cell. {ECO:0000269|PubMed:20133584}.
CC -!- INTERACTION:
CC Q9C9Y6; Q3E9D5: SAMDC4; NbExp=3; IntAct=EBI-4466064, EBI-25512418;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20133584}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants with short roots and small yellowish
CC leaves. {ECO:0000269|PubMed:20133584}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC012562; AAG51342.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74667.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74668.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63932.1; -; Genomic_DNA.
DR EMBL; AK226711; BAE98817.1; -; mRNA.
DR EMBL; BT011728; AAS49091.1; -; mRNA.
DR RefSeq; NP_001078124.1; NM_001084655.2.
DR RefSeq; NP_001325992.1; NM_001337765.1.
DR RefSeq; NP_187483.1; NM_111705.4.
DR AlphaFoldDB; Q9C9Y6; -.
DR SMR; Q9C9Y6; -.
DR BioGRID; 5353; 6.
DR IntAct; Q9C9Y6; 6.
DR STRING; 3702.AT3G08710.1; -.
DR iPTMnet; Q9C9Y6; -.
DR SwissPalm; Q9C9Y6; -.
DR PaxDb; Q9C9Y6; -.
DR PRIDE; Q9C9Y6; -.
DR ProteomicsDB; 232394; -.
DR EnsemblPlants; AT3G08710.1; AT3G08710.1; AT3G08710.
DR EnsemblPlants; AT3G08710.2; AT3G08710.2; AT3G08710.
DR EnsemblPlants; AT3G08710.3; AT3G08710.3; AT3G08710.
DR GeneID; 820018; -.
DR Gramene; AT3G08710.1; AT3G08710.1; AT3G08710.
DR Gramene; AT3G08710.2; AT3G08710.2; AT3G08710.
DR Gramene; AT3G08710.3; AT3G08710.3; AT3G08710.
DR KEGG; ath:AT3G08710; -.
DR Araport; AT3G08710; -.
DR TAIR; locus:2077833; AT3G08710.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_1_1; -.
DR InParanoid; Q9C9Y6; -.
DR OMA; CIAKQHA; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q9C9Y6; -.
DR PRO; PR:Q9C9Y6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C9Y6; baseline and differential.
DR Genevisible; Q9C9Y6; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:TAIR.
DR GO; GO:0007154; P:cell communication; IDA: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 Cell membrane; Disulfide bond; Electron transport; Lipoprotein; Membrane;
KW Myristate; Palmitate; Phosphoprotein; Redox-active center;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:20133584"
FT CHAIN 2..140
FT /note="Thioredoxin H9"
FT /id="PRO_0000326466"
FT DOMAIN 25..129
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 57
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 58
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17586839,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:20133584"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:20133584"
FT DISULFID 57..60
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MUTAGEN 2
FT /note="G->A: Loss of membrane localization. Loss of cell to
FT cell movement."
FT /evidence="ECO:0000269|PubMed:20133584"
FT MUTAGEN 4
FT /note="C->W: No effect on membrane localization. Loss of
FT cell to cell movement."
FT /evidence="ECO:0000269|PubMed:20133584"
SQ SEQUENCE 140 AA; 15334 MW; 2FC1DA8E7579C38A CRC64;
MGSCVSKGKG DDDSVHNVEF SGGNVHLITT KESWDDKLAE ADRDGKIVVA NFSATWCGPC
KIVAPFFIEL SEKHSSLMFL LVDVDELSDF SSSWDIKATP TFFFLKNGQQ IGKLVGANKP
ELQKKVTSII DSVPESPQRP
