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Thioredoxin H5 (AtTrxh5) (Protein LOCUS OF INSENSITIVITY TO VICTORIN 1) (Thioredoxin 5) (AtTRX5)

 TRXH5_ARATH             Reviewed;         118 AA.
Q39241; Q38881; Q56X92; Q9MAJ6;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 142.
RecName: Full=Thioredoxin H5;
Short=AtTrxh5;
AltName: Full=Protein LOCUS OF INSENSITIVITY TO VICTORIN 1;
AltName: Full=Thioredoxin 5;
Short=AtTRX5;
Name=TRX5; Synonyms=LIV1; OrderedLocusNames=At1g45145;
ORFNames=F27F5.21;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Callus;
PubMed=7777559; DOI=10.1073/pnas.92.12.5620;
Rivera-Madrid R., Mestres D., Marinho P., Jacquot J.-P.,
Decottignies P., Miginiac-Maslow M., Meyer Y.;
"Evidence for five divergent thioredoxin h sequences in Arabidopsis
thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 92:5620-5624(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
PubMed=8642611; DOI=10.1007/BF02498636;
Sahrawy M., Hecht V., Lopez Jaramillo J., Chueca A., Chartier Y.,
Meyer Y.;
"Intron position as an evolutionary marker of thioredoxins and
thioredoxin domains.";
J. Mol. Evol. 42:422-431(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION.
PubMed=14749482; DOI=10.1093/pcp/pch019;
Yamazaki D., Motohashi K., Kasama T., Hara Y., Hisabori T.;
"Target proteins of the cytosolic thioredoxins in Arabidopsis
thaliana.";
Plant Cell Physiol. 45:18-27(2004).
[10]
INDUCTION.
PubMed=14976236; DOI=10.1104/pp.103.035782;
Laloi C., Mestres-Ortega D., Marco Y., Meyer Y., Reichheld J.P.;
"The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative
stress and its W-box-mediated response to pathogen elicitor.";
Plant Physiol. 134:1006-1016(2004).
[11]
FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-39
AND CYS-42.
PubMed=17322408; DOI=10.1105/tpc.106.047563;
Sweat T.A., Wolpert T.J.;
"Thioredoxin h5 is required for victorin sensitivity mediated by a CC-
NBS-LRR gene in Arabidopsis.";
Plant Cell 19:673-687(2007).
[12]
GENE FAMILY, AND NOMENCLATURE.
PubMed=19825616; DOI=10.1093/mp/ssn076;
Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N.;
"Comparative genomic study of the thioredoxin family in photosynthetic
organisms with emphasis on Populus trichocarpa.";
Mol. Plant 2:308-322(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Thiol-disulfide oxidoreductase involved in response to
pathogens and oxidative stresses. Required for the response to
victorin, a phytotoxin which induces programmed cell death in
sensitive plants. Possesses insulin disulfide bonds reducing
activity. {ECO:0000269|PubMed:14749482,
ECO:0000269|PubMed:17322408}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- INDUCTION: By treatment with salicylic acid (SA), abscisic acid
(ABA), iron, copper and UV-C. Induced by wounding, oxidative
stress, infection with incompatible P.syringae and treatment with
the fungal phytotoxin victorin. {ECO:0000269|PubMed:14976236,
ECO:0000269|PubMed:17322408}.
-!- DISRUPTION PHENOTYPE: Insensitivity to victorin phytotoxin.
{ECO:0000269|PubMed:17322408}.
-!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type
subfamily. {ECO:0000305}.
-!- CAUTION: The active site contains a CPPC motif wich differs from
the conserved CGPC motif. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF69169.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Z35476; CAA84613.1; -; mRNA.
EMBL; U35829; AAC49356.1; -; Genomic_DNA.
EMBL; AC007915; AAF69169.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE32083.1; -; Genomic_DNA.
EMBL; AK118035; BAC42666.1; -; mRNA.
EMBL; AF360227; AAK25937.1; -; mRNA.
EMBL; AY040028; AAK64086.1; -; mRNA.
EMBL; AK221784; BAD93909.1; -; mRNA.
EMBL; AY087159; AAM64717.1; -; mRNA.
PIR; G96509; G96509.
PIR; S58120; S58120.
RefSeq; NP_175128.1; NM_103588.5.
UniGene; At.22939; -.
ProteinModelPortal; Q39241; -.
SMR; Q39241; -.
BioGrid; 26307; 76.
DIP; DIP-61886N; -.
IntAct; Q39241; 4.
STRING; 3702.AT1G45145.1; -.
iPTMnet; Q39241; -.
SwissPalm; Q39241; -.
PaxDb; Q39241; -.
PRIDE; Q39241; -.
EnsemblPlants; AT1G45145.1; AT1G45145.1; AT1G45145.
GeneID; 841082; -.
Gramene; AT1G45145.1; AT1G45145.1; AT1G45145.
KEGG; ath:AT1G45145; -.
Araport; AT1G45145; -.
TAIR; locus:2825451; AT1G45145.
eggNOG; KOG0907; Eukaryota.
eggNOG; COG0526; LUCA.
HOGENOM; HOG000292977; -.
InParanoid; Q39241; -.
KO; K03671; -.
OMA; LMKHGGL; -.
OrthoDB; EOG09360XJ5; -.
PhylomeDB; Q39241; -.
PRO; PR:Q39241; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q39241; baseline and differential.
Genevisible; Q39241; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0005829; C:cytosol; TAS:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:TAIR.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IBA:GO_Central.
GO; GO:0047134; F:protein-disulfide reductase activity; IBA:GO_Central.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0010188; P:response to microbial phytotoxin; IMP:TAIR.
GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
InterPro; IPR005746; Thioredoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR10438; PTHR10438; 1.
Pfam; PF00085; Thioredoxin; 1.
PIRSF; PIRSF000077; Thioredoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS00194; THIOREDOXIN_1; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Disulfide bond;
Electron transport; Redox-active center; Reference proteome;
Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 118 Thioredoxin H5.
/FTId=PRO_0000120050.
DOMAIN 2 113 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 39 39 Nucleophile. {ECO:0000255}.
ACT_SITE 42 42 Nucleophile. {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
DISULFID 39 42 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MUTAGEN 39 39 C->S: Loss of sensitivity to victorin
phytotoxin.
{ECO:0000269|PubMed:17322408}.
MUTAGEN 42 42 C->S: No effect on sensitivity to
victorin phytotoxin.
{ECO:0000269|PubMed:17322408}.
CONFLICT 118 118 A -> AL (in Ref. 2; AAC49356).
{ECO:0000305}.
SEQUENCE 118 AA; 13122 MW; 164FA8CDA98FC862 CRC64;
MAGEGEVIAC HTLEVWNEKV KDANESKKLI VIDFTASWCP PCRFIAPVFA EMAKKFTNVV
FFKIDVDELQ AVAQEFKVEA MPTFVFMKEG NIIDRVVGAA KDEINEKLMK HGGLVASA


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