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ABR1_ARATH
ID   ABR1_ARATH              Reviewed;         391 AA.
AC   Q9FGF8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Ethylene-responsive transcription factor ABR1;
DE   AltName: Full=Protein ABA REPRESSOR 1;
GN   Name=ABR1; Synonyms=ERF111; OrderedLocusNames=At5g64750; ORFNames=MVP7.8;
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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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].
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   FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16227468; DOI=10.1104/pp.105.066324;
RA   Pandey G.K., Grant J.J., Cheong Y.H., Kim B.G., Li L., Luan S.;
RT   "ABR1, an APETALA2-domain transcription factor that functions as a
RT   repressor of ABA response in Arabidopsis.";
RL   Plant Physiol. 139:1185-1193(2005).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16407444; DOI=10.1104/pp.105.073783;
RA   Nakano T., Suzuki K., Fujimura T., Shinshi H.;
RT   "Genome-wide analysis of the ERF gene family in Arabidopsis and rice.";
RL   Plant Physiol. 140:411-432(2006).
RN   [6]
RP   INDUCTION BY ABSCISIC ACID; SALT AND YY1.
RC   STRAIN=cv. Columbia;
RX   PubMed=26961720; DOI=10.1016/j.molp.2016.02.010;
RA   Li T., Wu X.-Y., Li H., Song J.-H., Liu J.-Y.;
RT   "A dual-function transcription factor, AtYY1, is a novel negative regulator
RT   of the Arabidopsis ABA response network.";
RL   Mol. Plant 9:650-661(2016).
CC   -!- FUNCTION: Negative regulator of the abscisic acid (ABA) signaling
CC       pathway involved in seed germination and in responses to stress
CC       conditions. Probably acts as a transcriptional activator. Binds to the
CC       GCC-box pathogenesis-related promoter element. May be involved in the
CC       regulation of gene expression by stress factors and by components of
CC       stress signal transduction pathways (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:16227468}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous with lower levels in seeds and siliques.
CC       {ECO:0000269|PubMed:16227468}.
CC   -!- INDUCTION: By abscisic acid (ABA) and stresses, including cold, drought
CC       and salt (PubMed:16227468, PubMed:26961720). Triggered by YY1
CC       (PubMed:26961720). {ECO:0000269|PubMed:16227468,
CC       ECO:0000269|PubMed:26961720}.
CC   -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB025637; BAB10308.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97946.1; -; Genomic_DNA.
DR   EMBL; AY140092; AAM98233.1; -; mRNA.
DR   EMBL; BT008480; AAP37839.1; -; mRNA.
DR   RefSeq; NP_201280.1; NM_125871.5.
DR   AlphaFoldDB; Q9FGF8; -.
DR   SMR; Q9FGF8; -.
DR   BioGRID; 21838; 28.
DR   IntAct; Q9FGF8; 27.
DR   STRING; 3702.AT5G64750.1; -.
DR   PaxDb; Q9FGF8; -.
DR   PRIDE; Q9FGF8; -.
DR   ProteomicsDB; 244629; -.
DR   EnsemblPlants; AT5G64750.1; AT5G64750.1; AT5G64750.
DR   GeneID; 836596; -.
DR   Gramene; AT5G64750.1; AT5G64750.1; AT5G64750.
DR   KEGG; ath:AT5G64750; -.
DR   Araport; AT5G64750; -.
DR   TAIR; locus:2176095; AT5G64750.
DR   eggNOG; ENOG502S34Q; Eukaryota.
DR   HOGENOM; CLU_042594_2_5_1; -.
DR   InParanoid; Q9FGF8; -.
DR   OMA; EMGNAVY; -.
DR   OrthoDB; 1085802at2759; -.
DR   PhylomeDB; Q9FGF8; -.
DR   PRO; PR:Q9FGF8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FGF8; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEP:TAIR.
DR   GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR   GO; GO:0009749; P:response to glucose; IEP:TAIR.
DR   GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR   GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR   GO; GO:0062211; P:root regeneration; IMP:TAIR.
DR   CDD; cd00018; AP2; 1.
DR   Gene3D; 3.30.730.10; -; 1.
DR   InterPro; IPR001471; AP2/ERF_dom.
DR   InterPro; IPR036955; AP2/ERF_dom_sf.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR044808; ERF_plant.
DR   PANTHER; PTHR31190; PTHR31190; 1.
DR   Pfam; PF00847; AP2; 1.
DR   PRINTS; PR00367; ETHRSPELEMNT.
DR   SMART; SM00380; AP2; 1.
DR   SUPFAM; SSF54171; SSF54171; 1.
DR   PROSITE; PS51032; AP2_ERF; 1.
PE   2: Evidence at transcript level;
KW   Abscisic acid signaling pathway; Activator; DNA-binding;
KW   Ethylene signaling pathway; Nucleus; Reference proteome; Stress response;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..391
FT                   /note="Ethylene-responsive transcription factor ABR1"
FT                   /id="PRO_0000297915"
FT   DNA_BIND        184..241
FT                   /note="AP2/ERF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT   REGION          45..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  42814 MW;  0755E9BE5F2046FB CRC64;
     MCVLKVANQE DNVGKKAESI RDDDHRTLSE IDQWLYLFAA EDDHHRHSFP TQQPPPSSSS
     SSLISGFSRE MEMSAIVSAL THVVAGNVPQ HQQGGGEGSG EGTSNSSSSS GQKRRREVEE
     GGAKAVKAAN TLTVDQYFSG GSSTSKVREA SSNMSGPGPT YEYTTTATAS SETSSFSGDQ
     PRRRYRGVRQ RPWGKWAAEI RDPFKAARVW LGTFDNAESA ARAYDEAALR FRGNKAKLNF
     PENVKLVRPA STEAQPVHQT AAQRPTQSRN SGSTTTLLPI RPASNQSVHS QPLMQSYNLS
     YSEMARQQQQ FQQHHQQSLD LYDQMSFPLR FGHTGGSMMQ STSSSSSHSR PLFSPAAVQP
     PPESASETGY LQDIQWPSDK TSNNYNNSPS S
 
 
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