位置:首页 > 蛋白库 > DJ1A_ARATH
DJ1A_ARATH
ID   DJ1A_ARATH              Reviewed;         392 AA.
AC   Q9FPF0; Q9LKA6;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Protein DJ-1 homolog A;
DE            Short=AtDJ1A;
GN   Name=DJ1A; OrderedLocusNames=At3g14990; ORFNames=K15M2.13;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia; TISSUE=Rosette leaf;
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 1).
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   INDUCTION BY CIS-JASMONE.
RX   PubMed=18356298; DOI=10.1073/pnas.0710305105;
RA   Bruce T.J., Matthes M.C., Chamberlain K., Woodcock C.M., Mohib A.,
RA   Webster B., Smart L.E., Birkett M.A., Pickett J.A., Napier J.A.;
RT   "cis-Jasmone induces Arabidopsis genes that affect the chemical ecology of
RT   multitrophic interactions with aphids and their parasitoids.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:4553-4558(2008).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CSD1 AND GPX2, INDUCTION,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=20406884; DOI=10.1242/jcs.063222;
RA   Xu X.M., Lin H., Maple J., Bjoerkblom B., Alves G., Larsen J.P.,
RA   Moeller S.G.;
RT   "The Arabidopsis DJ-1a protein confers stress protection through cytosolic
RT   SOD activation.";
RL   J. Cell Sci. 123:1644-1651(2010).
RN   [7]
RP   SUBUNIT.
RX   PubMed=23651081; DOI=10.1111/febs.12321;
RA   Kwon K., Choi D., Hyun J.K., Jung H.S., Baek K., Park C.;
RT   "Novel glyoxalases from Arabidopsis thaliana.";
RL   FEBS J. 280:3328-3339(2013).
CC   -!- FUNCTION: Involved in oxidative stress response. Confers protection
CC       against diverse stresses by binding both CSD1 and GPX2 and mediating
CC       the cytosolic activation of the Cu-Zn-dependent superoxide dismutase
CC       activity of CSD1. {ECO:0000269|PubMed:20406884}.
CC   -!- SUBUNIT: Homodimer (Probable). Interacts with CSD1 and GPX2.
CC       {ECO:0000269|PubMed:20406884, ECO:0000269|PubMed:23651081,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20406884}.
CC       Nucleus {ECO:0000269|PubMed:20406884}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FPF0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FPF0-2; Sequence=VSP_046013;
CC   -!- INDUCTION: By high light, copper, hydrogen peroxide, methyl viologen
CC       and cis-jasmone, but not methyl jasmonate.
CC       {ECO:0000269|PubMed:18356298, ECO:0000269|PubMed:20406884}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants have increased susceptibility to
CC       oxidative stress-induced cell death and accelerated cell death in aging
CC       plants. {ECO:0000269|PubMed:20406884}.
CC   -!- SIMILARITY: Belongs to the peptidase C56 family. {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; AP000370; BAA97062.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75598.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75599.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75600.1; -; Genomic_DNA.
DR   EMBL; AF326856; AAG41438.1; -; mRNA.
DR   EMBL; AF349515; AAK15562.1; -; mRNA.
DR   EMBL; AY039574; AAK62629.1; -; mRNA.
DR   EMBL; AY129490; AAM91076.1; -; mRNA.
DR   EMBL; AK317457; BAH20124.1; -; mRNA.
DR   RefSeq; NP_001030698.1; NM_001035621.1. [Q9FPF0-2]
DR   RefSeq; NP_188117.1; NM_112361.5. [Q9FPF0-1]
DR   RefSeq; NP_850588.1; NM_180257.1. [Q9FPF0-2]
DR   AlphaFoldDB; Q9FPF0; -.
DR   SMR; Q9FPF0; -.
DR   BioGRID; 6062; 7.
DR   IntAct; Q9FPF0; 2.
DR   STRING; 3702.AT3G14990.1; -.
DR   iPTMnet; Q9FPF0; -.
DR   MetOSite; Q9FPF0; -.
DR   PaxDb; Q9FPF0; -.
DR   PRIDE; Q9FPF0; -.
DR   ProteomicsDB; 222206; -. [Q9FPF0-1]
DR   EnsemblPlants; AT3G14990.1; AT3G14990.1; AT3G14990. [Q9FPF0-1]
DR   EnsemblPlants; AT3G14990.2; AT3G14990.2; AT3G14990. [Q9FPF0-2]
DR   EnsemblPlants; AT3G14990.3; AT3G14990.3; AT3G14990. [Q9FPF0-2]
DR   GeneID; 820728; -.
DR   Gramene; AT3G14990.1; AT3G14990.1; AT3G14990. [Q9FPF0-1]
DR   Gramene; AT3G14990.2; AT3G14990.2; AT3G14990. [Q9FPF0-2]
DR   Gramene; AT3G14990.3; AT3G14990.3; AT3G14990. [Q9FPF0-2]
DR   KEGG; ath:AT3G14990; -.
DR   Araport; AT3G14990; -.
DR   TAIR; locus:2086295; AT3G14990.
DR   eggNOG; KOG2764; Eukaryota.
DR   HOGENOM; CLU_000445_44_0_1; -.
DR   InParanoid; Q9FPF0; -.
DR   OMA; ISDCANT; -.
DR   PhylomeDB; Q9FPF0; -.
DR   BRENDA; 4.2.1.130; 399.
DR   PRO; PR:Q9FPF0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9FPF0; baseline and differential.
DR   Genevisible; Q9FPF0; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0019172; F:glyoxalase III activity; IDA:TAIR.
DR   GO; GO:1903189; P:glyoxal metabolic process; IBA:GO_Central.
DR   GO; GO:1900409; P:positive regulation of cellular response to oxidative stress; IDA:UniProtKB.
DR   Gene3D; 3.40.50.880; -; 2.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR006287; DJ-1.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   Pfam; PF01965; DJ-1_PfpI; 2.
DR   SUPFAM; SSF52317; SSF52317; 2.
DR   TIGRFAMs; TIGR01383; not_thiJ; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW   Stress response.
FT   CHAIN           1..392
FT                   /note="Protein DJ-1 homolog A"
FT                   /id="PRO_0000421813"
FT   DOMAIN          6..174
FT                   /note="PfpI endopeptidase 1"
FT   DOMAIN          212..378
FT                   /note="PfpI endopeptidase 2"
FT   VAR_SEQ         1..23
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046013"
SQ   SEQUENCE   392 AA;  41857 MW;  A29CE52C5E3D090A CRC64;
     MASFTKTVLI PIAHGTEPLE AVAMITVLRR GGADVTVASV ETQVGVDACH GIKMVADTLL
     SDITDSVFDL IVLPGGLPGG ETLKNCKSLE NMVKKQDSDG RLNAAICCAP ALALGTWGLL
     EGKKATGYPV FMEKLAATCA TAVESRVQID GRIVTSRGPG TTIEFSITLI EQLFGKEKAD
     EVSSILLLRP NPGEEFTFTE LNQTNWSFED TPQILVPIAE ESEEIEAIAL VDILRRAKAN
     VVIAAVGNSL EVEGSRKAKL VAEVLLDEVA EKSFDLIVLP GGLNGAQRFA SCEKLVNMLR
     KQAEANKPYG GICASPAYVF EPNGLLKGKK ATTHPVVSDK LSDKSHIEHR VVVDGNVITS
     RAPGTAMEFS LAIVEKFYGR EKALQLGKAT LV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024