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TRXH5_ARATH
ID   TRXH5_ARATH             Reviewed;         118 AA.
AC   Q39241; Q38881; Q56X92; Q9MAJ6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 163.
DE   RecName: Full=Thioredoxin H5;
DE            Short=AtTrxh5;
DE   AltName: Full=Protein LOCUS OF INSENSITIVITY TO VICTORIN 1;
DE   AltName: Full=Thioredoxin 5;
DE            Short=AtTRX5;
GN   Name=TRX5; Synonyms=LIV1; OrderedLocusNames=At1g45145; ORFNames=F27F5.21;
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].
RC   STRAIN=cv. Columbia; TISSUE=Callus;
RX   PubMed=7777559; DOI=10.1073/pnas.92.12.5620;
RA   Rivera-Madrid R., Mestres D., Marinho P., Jacquot J.-P., Decottignies P.,
RA   Miginiac-Maslow M., Meyer Y.;
RT   "Evidence for five divergent thioredoxin h sequences in Arabidopsis
RT   thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:5620-5624(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=8642611; DOI=10.1007/bf02498636;
RA   Sahrawy M., Hecht V., Lopez Jaramillo J., Chueca A., Chartier Y., Meyer Y.;
RT   "Intron position as an evolutionary marker of thioredoxins and thioredoxin
RT   domains.";
RL   J. Mol. Evol. 42:422-431(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [6]
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   [7]
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   [8]
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   [9]
RP   FUNCTION.
RX   PubMed=14749482; DOI=10.1093/pcp/pch019;
RA   Yamazaki D., Motohashi K., Kasama T., Hara Y., Hisabori T.;
RT   "Target proteins of the cytosolic thioredoxins in Arabidopsis thaliana.";
RL   Plant Cell Physiol. 45:18-27(2004).
RN   [10]
RP   INDUCTION.
RX   PubMed=14976236; DOI=10.1104/pp.103.035782;
RA   Laloi C., Mestres-Ortega D., Marco Y., Meyer Y., Reichheld J.P.;
RT   "The Arabidopsis cytosolic thioredoxin h5 gene induction by oxidative
RT   stress and its W-box-mediated response to pathogen elicitor.";
RL   Plant Physiol. 134:1006-1016(2004).
RN   [11]
RP   FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-39 AND
RP   CYS-42.
RX   PubMed=17322408; DOI=10.1105/tpc.106.047563;
RA   Sweat T.A., Wolpert T.J.;
RT   "Thioredoxin h5 is required for victorin sensitivity mediated by a CC-NBS-
RT   LRR gene in Arabidopsis.";
RL   Plant Cell 19:673-687(2007).
RN   [12]
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   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [14]
RP   INTERACTION WITH MDH1.
RX   PubMed=29194485; DOI=10.1093/jxb/erx396;
RA   Huang J., Niazi A.K., Young D., Rosado L.A., Vertommen D., Bodra N.,
RA   Abdelgawwad M.R., Vignols F., Wei B., Wahni K., Bashandy T., Bariat L.,
RA   Van Breusegem F., Messens J., Reichheld J.P.;
RT   "Self-protection of cytosolic malate dehydrogenase against oxidative stress
RT   in Arabidopsis.";
RL   J. Exp. Bot. 69:3491-3505(2018).
CC   -!- FUNCTION: Thiol-disulfide oxidoreductase involved in response to
CC       pathogens and oxidative stresses. Required for the response to
CC       victorin, a phytotoxin which induces programmed cell death in sensitive
CC       plants. Possesses insulin disulfide bonds reducing activity.
CC       {ECO:0000269|PubMed:14749482, ECO:0000269|PubMed:17322408}.
CC   -!- SUBUNIT: Interacts with MDH1. {ECO:0000269|PubMed:29194485}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: By treatment with salicylic acid (SA), abscisic acid (ABA),
CC       iron, copper and UV-C. Induced by wounding, oxidative stress, infection
CC       with incompatible P.syringae and treatment with the fungal phytotoxin
CC       victorin. {ECO:0000269|PubMed:14976236, ECO:0000269|PubMed:17322408}.
CC   -!- DISRUPTION PHENOTYPE: Insensitivity to victorin phytotoxin.
CC       {ECO:0000269|PubMed:17322408}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: The active site contains a CPPC motif wich differs from the
CC       conserved CGPC motif. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF69169.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; Z35476; CAA84613.1; -; mRNA.
DR   EMBL; U35829; AAC49356.1; -; Genomic_DNA.
DR   EMBL; AC007915; AAF69169.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE32083.1; -; Genomic_DNA.
DR   EMBL; AK118035; BAC42666.1; -; mRNA.
DR   EMBL; AF360227; AAK25937.1; -; mRNA.
DR   EMBL; AY040028; AAK64086.1; -; mRNA.
DR   EMBL; AK221784; BAD93909.1; -; mRNA.
DR   EMBL; AY087159; AAM64717.1; -; mRNA.
DR   PIR; G96509; G96509.
DR   PIR; S58120; S58120.
DR   RefSeq; NP_175128.1; NM_103588.5.
DR   AlphaFoldDB; Q39241; -.
DR   SMR; Q39241; -.
DR   BioGRID; 26307; 76.
DR   DIP; DIP-61886N; -.
DR   IntAct; Q39241; 75.
DR   STRING; 3702.AT1G45145.1; -.
DR   iPTMnet; Q39241; -.
DR   SwissPalm; Q39241; -.
DR   PaxDb; Q39241; -.
DR   PRIDE; Q39241; -.
DR   ProteomicsDB; 228706; -.
DR   EnsemblPlants; AT1G45145.1; AT1G45145.1; AT1G45145.
DR   GeneID; 841082; -.
DR   Gramene; AT1G45145.1; AT1G45145.1; AT1G45145.
DR   KEGG; ath:AT1G45145; -.
DR   Araport; AT1G45145; -.
DR   TAIR; locus:2825451; AT1G45145.
DR   eggNOG; KOG0907; Eukaryota.
DR   HOGENOM; CLU_090389_14_1_1; -.
DR   InParanoid; Q39241; -.
DR   OMA; CAPCKDI; -.
DR   OrthoDB; 1482186at2759; -.
DR   PhylomeDB; Q39241; -.
DR   PRO; PR:Q39241; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q39241; baseline and differential.
DR   Genevisible; Q39241; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0010188; P:response to microbial phytotoxin; IMP:TAIR.
DR   GO; GO:0006979; P:response to oxidative stress; IEP: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   Acetylation; Cytoplasm; Disulfide bond; Electron transport;
KW   Redox-active center; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..118
FT                   /note="Thioredoxin H5"
FT                   /id="PRO_0000120050"
FT   DOMAIN          2..113
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        39
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        42
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   DISULFID        39..42
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MUTAGEN         39
FT                   /note="C->S: Loss of sensitivity to victorin phytotoxin."
FT                   /evidence="ECO:0000269|PubMed:17322408"
FT   MUTAGEN         42
FT                   /note="C->S: No effect on sensitivity to victorin
FT                   phytotoxin."
FT                   /evidence="ECO:0000269|PubMed:17322408"
FT   CONFLICT        118
FT                   /note="A -> AL (in Ref. 2; AAC49356)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   118 AA;  13122 MW;  164FA8CDA98FC862 CRC64;
     MAGEGEVIAC HTLEVWNEKV KDANESKKLI VIDFTASWCP PCRFIAPVFA EMAKKFTNVV
     FFKIDVDELQ AVAQEFKVEA MPTFVFMKEG NIIDRVVGAA KDEINEKLMK HGGLVASA
 
 
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