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CITRX_ARATH
ID   CITRX_ARATH             Reviewed;         183 AA.
AC   Q9M7X9; C0Z2V5; Q8LFA3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Thioredoxin-like protein CITRX, chloroplastic {ECO:0000305};
DE            EC=1.8.-.- {ECO:0000269|PubMed:20511297};
DE   AltName: Full=Cf-9-interacting thioredoxin {ECO:0000303|PubMed:15131698};
DE            Short=AtCiTrx {ECO:0000303|PubMed:15131698};
DE   AltName: Full=PEP-associated protein 10 {ECO:0000303|PubMed:21949211};
DE   AltName: Full=Thioredoxin Trx p {ECO:0000303|PubMed:20133584};
DE   AltName: Full=Thioredoxin Z {ECO:0000303|PubMed:20511297};
DE   Flags: Precursor;
GN   Name=CITRX {ECO:0000303|PubMed:19825616};
GN   Synonyms=PAP10 {ECO:0000303|PubMed:21949211},
GN   TRX P {ECO:0000303|PubMed:20133584}, TRX Z {ECO:0000303|PubMed:20511297};
GN   OrderedLocusNames=At3g06730 {ECO:0000312|Araport:AT3G06730};
GN   ORFNames=F3E22.13 {ECO:0000312|EMBL:AAF63825.1};
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] (ISOFORM 1).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   RETRACTED PAPER.
RX   PubMed=15131698; DOI=10.1038/sj.emboj.7600224;
RA   Rivas S., Rougon-Cardoso A., Smoker M., Schauser L., Yoshioka H.,
RA   Jones J.D.;
RT   "CITRX thioredoxin interacts with the tomato Cf-9 resistance protein and
RT   negatively regulates defence.";
RL   EMBO J. 23:2156-2165(2004).
RN   [7]
RP   RETRACTION NOTICE OF PUBMED:15131698.
RX   PubMed=31310343; DOI=10.15252/embj.2019102435;
RA   Rivas S., Rougon-Cardoso A., Smoker M., Schauser L., Yoshioka H.,
RA   Jones J.D.;
RL   EMBO J. 38:e102435-e102435(2019).
RN   [8]
RP   FUNCTION.
RX   PubMed=16326926; DOI=10.1105/tpc.105.036392;
RA   Pfalz J., Liere K., Kandlbinder A., Dietz K.-J., Oelmueller R.;
RT   "pTAC2, -6, and -12 are components of the transcriptionally active plastid
RT   chromosome that are required for plastid gene expression.";
RL   Plant Cell 18:176-197(2006).
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   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH FLN1
RP   AND FLN2, AND MUTAGENESIS OF CYS-106 AND CYS-109.
RX   PubMed=20511297; DOI=10.1105/tpc.109.071001;
RA   Arsova B., Hoja U., Wimmelbacher M., Greiner E., Ustun S., Melzer M.,
RA   Petersen K., Lein W., Bornke F.;
RT   "Plastidial thioredoxin z interacts with two fructokinase-like proteins in
RT   a thiol-dependent manner: evidence for an essential role in chloroplast
RT   development in Arabidopsis and Nicotiana benthamiana.";
RL   Plant Cell 22:1498-1515(2010).
RN   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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).
RN   [12]
RP   FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=21949211; DOI=10.1104/pp.111.184515;
RA   Steiner S., Schroeter Y., Pfalz J., Pfannschmidt T.;
RT   "Identification of essential subunits in the plastid-encoded RNA polymerase
RT   complex reveals building blocks for proper plastid development.";
RL   Plant Physiol. 157:1043-1055(2011).
RN   [13]
RP   INTERACTION WITH MRL7.
RX   PubMed=23956074; DOI=10.1093/mp/sst092;
RA   Yua Q.B., Ma Q., Kong M.M., Zhao T.T., Zhang X.L., Zhou Q., Huang C.,
RA   Chong K., Yang Z.N.;
RT   "AtECB1/MRL7, a thioredoxin-like fold protein with disulfide reductase
RT   activity, regulates chloroplast gene expression and chloroplast biogenesis
RT   in Arabidopsis thaliana.";
RL   Mol. Plant 7:206-217(2014).
CC   -!- FUNCTION: Thiol-disulfide oxidoreductase that plays a role in proper
CC       chloroplast development, most likely through regulating plastid-encoded
CC       polymerase (PEP) dependent chloroplast transcription. Acts as a
CC       component of the transcriptionally active plastid chromosome that is
CC       required for plastid gene expression. {ECO:0000269|PubMed:16326926,
CC       ECO:0000269|PubMed:20133584, ECO:0000269|PubMed:20511297,
CC       ECO:0000269|PubMed:21949211}.
CC   -!- SUBUNIT: Interacts with FLN1 and FLN2 (PubMed:20511297). Interacts with
CC       MRL7 (PubMed:23956074). {ECO:0000269|PubMed:20511297,
CC       ECO:0000269|PubMed:23956074}.
CC   -!- INTERACTION:
CC       Q9M7X9; Q9M394: FLN1; NbExp=3; IntAct=EBI-9823626, EBI-9823647;
CC       Q9M7X9; F4I0K2: FLN2; NbExp=3; IntAct=EBI-9823626, EBI-9823671;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:20133584, ECO:0000269|PubMed:20511297}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9M7X9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9M7X9-2; Sequence=VSP_039287, VSP_039288;
CC   -!- DISRUPTION PHENOTYPE: Albino seedlings leading to lethality. Abnormal
CC       plastids lacking internal membrane structures.
CC       {ECO:0000269|PubMed:20133584, ECO:0000269|PubMed:20511297}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant CITRX-type
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: The article has been retracted, because it has become clear
CC       that the thioredoxin that interacts in yeast 2-hybrid with the Cf-9 C-
CC       terminus is in fact localized in the chloroplast, rendering a role in
CC       Cf-9 signaling unlikely. All the authors agree that this paper should
CC       be withdrawn from the scientific literature.
CC       {ECO:0000305|PubMed:31310343}.
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DR   EMBL; AC023912; AAF63825.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74449.1; -; Genomic_DNA.
DR   EMBL; AF370315; AAK44130.1; -; mRNA.
DR   EMBL; AY063100; AAL34274.1; -; mRNA.
DR   EMBL; AK318919; BAH57034.1; -; mRNA.
DR   EMBL; AY084959; AAM61520.1; -; mRNA.
DR   RefSeq; NP_187329.1; NM_111553.4. [Q9M7X9-1]
DR   AlphaFoldDB; Q9M7X9; -.
DR   SMR; Q9M7X9; -.
DR   BioGRID; 5193; 10.
DR   IntAct; Q9M7X9; 2.
DR   STRING; 3702.AT3G06730.1; -.
DR   PaxDb; Q9M7X9; -.
DR   PRIDE; Q9M7X9; -.
DR   ProteomicsDB; 246867; -. [Q9M7X9-1]
DR   EnsemblPlants; AT3G06730.1; AT3G06730.1; AT3G06730. [Q9M7X9-1]
DR   GeneID; 819858; -.
DR   Gramene; AT3G06730.1; AT3G06730.1; AT3G06730. [Q9M7X9-1]
DR   KEGG; ath:AT3G06730; -.
DR   Araport; AT3G06730; -.
DR   TAIR; locus:2083398; AT3G06730.
DR   eggNOG; KOG0907; Eukaryota.
DR   HOGENOM; CLU_110012_1_0_1; -.
DR   InParanoid; Q9M7X9; -.
DR   OMA; PLQMMRD; -.
DR   OrthoDB; 1482186at2759; -.
DR   PhylomeDB; Q9M7X9; -.
DR   PRO; PR:Q9M7X9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M7X9; baseline and differential.
DR   Genevisible; Q9M7X9; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0042644; C:chloroplast nucleoid; HDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IDA:TAIR.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IDA:TAIR.
DR   GO; GO:0045454; P:cell redox homeostasis; IMP:TAIR.
DR   GO; GO:0009657; P:plastid organization; IMP:TAIR.
DR   InterPro; IPR044182; CITRX.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR47834; PTHR47834; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chloroplast; Disulfide bond; Electron transport;
KW   Oxidoreductase; Plastid; Redox-active center; Reference proteome;
KW   Transit peptide; Transport.
FT   TRANSIT         1..81
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           82..183
FT                   /note="Thioredoxin-like protein CITRX, chloroplastic"
FT                   /id="PRO_0000394545"
FT   DOMAIN          82..183
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   SITE            100
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   SITE            107
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   SITE            108
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   DISULFID        106..109
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   VAR_SEQ         147..170
FT                   /note="RGLPTLFFISPDPSKDAIRTEGLI -> YCNLQLMFLNFMNLLSAYQCKFLH
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_039287"
FT   VAR_SEQ         171..183
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_039288"
FT   MUTAGEN         106
FT                   /note="C->S: Strongly reduces the interaction with FLN1 or
FT                   FLN2."
FT                   /evidence="ECO:0000269|PubMed:20511297"
FT   MUTAGEN         109
FT                   /note="C->S: Does not affect the interaction with FLN1 or
FT                   FLN2."
FT                   /evidence="ECO:0000269|PubMed:20511297"
FT   CONFLICT        9
FT                   /note="F -> L (in Ref. 5; AAM61520)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   183 AA;  20670 MW;  1A1152A76B5DE8D7 CRC64;
     MALVQSRTFP HLNTPLSPIL SSLHAPSSLF IRREIRPVAA PFSSSTAGNL PFSPLTRPRK
     LLCPPPRGKF VREDYLVKKL SAQELQELVK GDRKVPLIVD FYATWCGPCI LMAQELEMLA
     VEYESNAIIV KVDTDDEYEF ARDMQVRGLP TLFFISPDPS KDAIRTEGLI PLQMMHDIID
     NEM
 
 
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