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O3L4_ARATH
ID   O3L4_ARATH              Reviewed;         240 AA.
AC   Q8L9W8; Q84WC9;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Protein OXIDATIVE STRESS 3 LIKE 4 {ECO:0000303|PubMed:18980652};
DE            Short=AtO3L4 {ECO:0000303|PubMed:18980652};
DE   AltName: Full=KID-containing protein {ECO:0000303|PubMed:12631331};
DE            Short=AtKCP {ECO:0000303|PubMed:12631331};
GN   Name=O3L4 {ECO:0000303|PubMed:18980652};
GN   Synonyms=KCP {ECO:0000303|PubMed:12631331};
GN   OrderedLocusNames=At5g24890 {ECO:0000312|Araport:AT5G24890};
GN   ORFNames=F6A4.100 {ECO:0000312|EMBL:AED93375.1};
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   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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY.
RX   PubMed=12631331; DOI=10.1046/j.1365-313x.2003.01694.x;
RA   Gao M.-J., Schaefer U.A., Parkin I.A.P., Hegedus D.D., Lydiate D.J.,
RA   Hannoufa A.;
RT   "A novel protein from Brassica napus has a putative KID domain and responds
RT   to low temperature.";
RL   Plant J. 33:1073-1086(2003).
RN   [6]
RP   FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Landsberg erecta, and cv. Wassilewskija;
RX   PubMed=18980652; DOI=10.1111/j.1365-313x.2008.03717.x;
RA   Blanvillain R., Kim J.H., Wu S., Lima A., Ow D.W.;
RT   "OXIDATIVE STRESS 3 is a chromatin-associated factor involved in tolerance
RT   to heavy metals and oxidative stress.";
RL   Plant J. 57:654-665(2009).
RN   [7]
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).
CC   -!- FUNCTION: Transcription activator which may regulates gene expression
CC       through interaction with the histone deacetylase HDA19 (By similarity).
CC       Promotes slightly the tolerance to cadmium (Cd) and to oxidizing
CC       chemicals (e.g. diamide and tert-butyl hydroperoxide (t-BOOH))
CC       (PubMed:18980652). {ECO:0000250|UniProtKB:Q84U09,
CC       ECO:0000269|PubMed:18980652}.
CC   -!- SUBUNIT: Interacts with HDA19; Ser-213 is critical for this
CC       interaction. {ECO:0000250|UniProtKB:Q84U09}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9LVB9}.
CC   -!- DOMAIN: The kinase-inducible domain (KID, 202-229) is required for
CC       interaction with HDA19. {ECO:0000250|UniProtKB:Q84U09}.
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DR   EMBL; CP002688; AED93375.1; -; Genomic_DNA.
DR   EMBL; AY088175; AAM65718.1; -; mRNA.
DR   EMBL; BT003969; AAO42013.1; -; mRNA.
DR   EMBL; BT020475; AAW38976.1; -; mRNA.
DR   EMBL; BT023742; AAZ23934.1; -; mRNA.
DR   RefSeq; NP_197871.1; NM_122398.4.
DR   AlphaFoldDB; Q8L9W8; -.
DR   STRING; 3702.AT5G24890.1; -.
DR   PaxDb; Q8L9W8; -.
DR   PRIDE; Q8L9W8; -.
DR   ProteomicsDB; 182990; -.
DR   EnsemblPlants; AT5G24890.1; AT5G24890.1; AT5G24890.
DR   GeneID; 832558; -.
DR   Gramene; AT5G24890.1; AT5G24890.1; AT5G24890.
DR   KEGG; ath:AT5G24890; -.
DR   Araport; AT5G24890; -.
DR   TAIR; locus:2149413; AT5G24890.
DR   eggNOG; KOG4210; Eukaryota.
DR   HOGENOM; CLU_066544_2_0_1; -.
DR   InParanoid; Q8L9W8; -.
DR   OMA; DTDNNSY; -.
DR   OrthoDB; 1263702at2759; -.
DR   PhylomeDB; Q8L9W8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8L9W8; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0046686; P:response to cadmium ion; IMP:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Phosphoprotein; Reference proteome; Stress response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..240
FT                   /note="Protein OXIDATIVE STRESS 3 LIKE 4"
FT                   /id="PRO_0000455035"
FT   REGION          1..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..229
FT                   /note="Kinase-inducible domain (KID)"
FT                   /evidence="ECO:0000250|UniProtKB:Q84U09"
FT   MOTIF           142..150
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        11..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..83
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..189
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            213
FT                   /note="Critical for interaction with HDA19"
FT                   /evidence="ECO:0000250|UniProtKB:Q84U09"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q84U09"
FT   CONFLICT        182
FT                   /note="D -> E (in Ref. 3; AAO42013)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   240 AA;  26577 MW;  5A4143571BF732A3 CRC64;
     MELMAKPTFS IEVSQYGTTD LPATEKASSS SSSFETTNEE GVEESGLSRI WSGQTADYSS
     DSSSIGTPGD SEEDEEESEN ENDDVSSKEL GLRGLASMSS LEDSLPSKRG LSNHYKGKSK
     SFGNLGEIGS VKEVAKQENP LNKRRRLQIC NKLARKSFYS WQNPKSMPLL PVNEDEDDDD
     EDDDEEDLKS GFDENKSSSD EEGVKKVVVR KGSFKNRAYK SRSCFALSDL IEEEDDDDDQ
 
 
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