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ERD15_ARATH
ID   ERD15_ARATH             Reviewed;         163 AA.
AC   Q39096; Q3E6W2; Q8LBP5;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Protein EARLY RESPONSIVE TO DEHYDRATION 15;
DE   AltName: Full=PAM2-containing protein CID1;
DE   AltName: Full=Polyadenylate-binding protein-interacting protein 1;
DE            Short=PABP-interacting protein 1;
DE            Short=Poly(A)-binding protein-interacting protein 1;
DE   AltName: Full=Protein CTC-INTERACTING DOMAIN 1;
DE   AltName: Full=Protein LIGHT STRESS-REGULATED 1;
GN   Name=ERD15; Synonyms=CID1, LSR1; OrderedLocusNames=At2g41430;
GN   ORFNames=F13H10.2, T26J13.2;
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] (ISOFORM 1), AND INDUCTION BY DEHYDRATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=7846179; DOI=10.1104/pp.106.4.1707;
RA   Kiyosue T., Yamaguchi-Shinozaki K., Shinozaki K.;
RT   "ERD15, a cDNA for a dehydration-induced gene from Arabidopsis thaliana.";
RL   Plant Physiol. 106:1707-1707(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia; TISSUE=Rosette leaf;
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   [7]
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   [8]
RP   INDUCTION BY PAENIBACILLUS POLYMYXA.
RX   PubMed=10550893; DOI=10.1094/mpmi.1999.12.11.951;
RA   Timmusk S., Wagner E.G.;
RT   "The plant-growth-promoting rhizobacterium Paenibacillus polymyxa induces
RT   changes in Arabidopsis thaliana gene expression: a possible connection
RT   between biotic and abiotic stress responses.";
RL   Mol. Plant Microbe Interact. 12:951-959(1999).
RN   [9]
RP   INDUCTION BY LIGHT AND ABIOTIC STRESS, AND SUBCELLULAR LOCATION.
RX   PubMed=11683875; DOI=10.1046/j.1432-1033.2001.02471.x;
RA   Dunaeva M., Adamska I.;
RT   "Identification of genes expressed in response to light stress in leaves of
RT   Arabidopsis thaliana using RNA differential display.";
RL   Eur. J. Biochem. 268:5521-5529(2001).
RN   [10]
RP   INDUCTION BY HYPERGRAVITY.
RX   PubMed=14686431; DOI=10.1016/s0273-1177(03)00243-6;
RA   Yoshioka R., Soga K., Wakabayashi K., Takeba G., Hoson T.;
RT   "Hypergravity-induced changes in gene expression in Arabidopsis
RT   hypocotyls.";
RL   Adv. Space Res. 31:2187-2193(2003).
RN   [11]
RP   GENE FAMILY, PAM2 MOTIF, INTERACTION WITH PAB2, MUTAGENESIS OF
RP   9-SER--PRO-13, AND TISSUE SPECIFICITY.
RX   PubMed=15650869; DOI=10.1007/s00438-004-1090-9;
RA   Bravo J., Aguilar-Henonin L., Olmedo G., Guzman P.;
RT   "Four distinct classes of proteins as interaction partners of the PABC
RT   domain of Arabidopsis thaliana Poly(A)-binding proteins.";
RL   Mol. Genet. Genomics 272:651-665(2005).
RN   [12]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY BIOTIC AND ABIOTIC STRESS.
RX   PubMed=17056758; DOI=10.1104/pp.106.086223;
RA   Kariola T., Brader G., Helenius E., Li J., Heino P., Palva E.T.;
RT   "EARLY RESPONSIVE TO DEHYDRATION 15, a negative regulator of abscisic acid
RT   responses in Arabidopsis.";
RL   Plant Physiol. 142:1559-1573(2006).
RN   [13]
RP   INTERACTION WITH MPC.
RX   PubMed=18796636; DOI=10.1105/tpc.108.061929;
RA   Tiwari S., Schulz R., Ikeda Y., Dytham L., Bravo J., Mathers L.,
RA   Spielman M., Guzman P., Oakey R.J., Kinoshita T., Scott R.J.;
RT   "MATERNALLY EXPRESSED PAB C-TERMINAL, a novel imprinted gene in
RT   Arabidopsis, encodes the conserved C-terminal domain of polyadenylate
RT   binding proteins.";
RL   Plant Cell 20:2387-2398(2008).
RN   [14]
RP   PAM2 MOTIF, INTERACTION WITH PAB2; PAB4 AND PAB8, AND REVIEW.
RX   PubMed=22118612; DOI=10.1016/j.plantsci.2011.08.009;
RA   Aalto M.K., Helenius E., Kariola T., Pennanen V., Heino P., Horak H.,
RA   Puzorjova I., Kollist H., Palva E.T.;
RT   "ERD15--an attenuator of plant ABA responses and stomatal aperture.";
RL   Plant Sci. 182:19-28(2012).
CC   -!- FUNCTION: Central component of stress responses that interacts with
CC       poly(A)-binding proteins. Negative regulator of abscisic acid (ABA)
CC       responses, including resistance to drought and freezing as well as
CC       stomatal closure regulation. Mediates resistance to the bacterial
CC       necrotroph pathogen Erwinia carotovora subsp. carotovora and promotes
CC       the induction of marker genes for systemic acquired resistance (SAR).
CC       {ECO:0000269|PubMed:17056758}.
CC   -!- SUBUNIT: Interacts with PAB2, PAB4 and PAB8. Interacts with MPC.
CC       {ECO:0000269|PubMed:15650869, ECO:0000269|PubMed:18796636,
CC       ECO:0000269|PubMed:22118612}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:11683875}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q39096-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q39096-2; Sequence=VSP_044341, VSP_044342;
CC   -!- TISSUE SPECIFICITY: Expressed in cauline leaves, stems, rosette leaves,
CC       immature siliques and primary inflorescences.
CC       {ECO:0000269|PubMed:15650869}.
CC   -!- INDUCTION: Strongly induced by abiotic stresses such as abscisic acid
CC       (ABA), salicylic acid (SA), wounding, high light, cold stress,
CC       oxidative stress, hypergravity and dehydration. Accumulates upon root
CC       colonization by the plant-growth-promoting rhizobacterium (PGPR)
CC       Paenibacillus polymyxa. Slightly reduced levels in response to UV-A
CC       illumination, salt stress and heat shock treatment.
CC       {ECO:0000269|PubMed:10550893, ECO:0000269|PubMed:11683875,
CC       ECO:0000269|PubMed:14686431, ECO:0000269|PubMed:17056758,
CC       ECO:0000269|PubMed:7846179}.
CC   -!- DOMAIN: Contains a PAM2-like motif, which seems to be involved in the
CC       binding to the PABC/CTC domain of PAB proteins.
CC   -!- DISRUPTION PHENOTYPE: Hypersensitive to abscisic acid (ABA) leading to
CC       improved tolerance to both drought and freezing, as well as impaired
CC       seed germination in the presence of ABA. {ECO:0000269|PubMed:17056758}.
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DR   EMBL; D30719; BAA06384.1; -; mRNA.
DR   EMBL; AC004625; AAC23728.1; -; Genomic_DNA.
DR   EMBL; AC005662; AAM15070.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09973.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09974.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09975.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09976.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09977.1; -; Genomic_DNA.
DR   EMBL; AF372909; AAK49625.1; -; mRNA.
DR   EMBL; AY056399; AAL08255.1; -; mRNA.
DR   EMBL; AY065120; AAL38296.1; -; mRNA.
DR   EMBL; AY081636; AAM10198.1; -; mRNA.
DR   EMBL; BT002663; AAO11579.1; -; mRNA.
DR   EMBL; BX820705; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK317136; BAH19822.1; -; mRNA.
DR   EMBL; AY087077; AAM64638.1; -; mRNA.
DR   PIR; T02438; T02438.
DR   RefSeq; NP_001189727.1; NM_001202798.1. [Q39096-1]
DR   RefSeq; NP_181674.1; NM_129706.4. [Q39096-1]
DR   RefSeq; NP_850350.1; NM_180019.3. [Q39096-1]
DR   RefSeq; NP_973657.1; NM_201928.2. [Q39096-2]
DR   RefSeq; NP_973658.1; NM_201929.2. [Q39096-1]
DR   AlphaFoldDB; Q39096; -.
DR   BioGRID; 4078; 4.
DR   ELM; Q39096; -.
DR   IntAct; Q39096; 3.
DR   STRING; 3702.AT2G41430.4; -.
DR   iPTMnet; Q39096; -.
DR   PaxDb; Q39096; -.
DR   PRIDE; Q39096; -.
DR   ProteomicsDB; 221865; -. [Q39096-1]
DR   EnsemblPlants; AT2G41430.1; AT2G41430.1; AT2G41430. [Q39096-1]
DR   EnsemblPlants; AT2G41430.2; AT2G41430.2; AT2G41430. [Q39096-1]
DR   EnsemblPlants; AT2G41430.3; AT2G41430.3; AT2G41430. [Q39096-2]
DR   EnsemblPlants; AT2G41430.4; AT2G41430.4; AT2G41430. [Q39096-1]
DR   EnsemblPlants; AT2G41430.5; AT2G41430.5; AT2G41430. [Q39096-1]
DR   GeneID; 818741; -.
DR   Gramene; AT2G41430.1; AT2G41430.1; AT2G41430. [Q39096-1]
DR   Gramene; AT2G41430.2; AT2G41430.2; AT2G41430. [Q39096-1]
DR   Gramene; AT2G41430.3; AT2G41430.3; AT2G41430. [Q39096-2]
DR   Gramene; AT2G41430.4; AT2G41430.4; AT2G41430. [Q39096-1]
DR   Gramene; AT2G41430.5; AT2G41430.5; AT2G41430. [Q39096-1]
DR   KEGG; ath:AT2G41430; -.
DR   Araport; AT2G41430; -.
DR   TAIR; locus:2060529; AT2G41430.
DR   eggNOG; ENOG502S19Q; Eukaryota.
DR   HOGENOM; CLU_108773_0_0_1; -.
DR   InParanoid; Q39096; -.
DR   OMA; CSPRFIQ; -.
DR   PhylomeDB; Q39096; -.
DR   PRO; PR:Q39096; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q39096; baseline and differential.
DR   Genevisible; Q39096; AT.
DR   GO; GO:0005737; C:cytoplasm; ISS:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0042651; C:thylakoid membrane; TAS:TAIR.
DR   GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR   GO; GO:0010196; P:nonphotochemical quenching; IMP:TAIR.
DR   GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR   GO; GO:0009644; P:response to high light intensity; IMP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; NAS:TAIR.
DR   InterPro; IPR040414; CID1/CID2.
DR   PANTHER; PTHR33790; PTHR33790; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Reference proteome.
FT   CHAIN           1..163
FT                   /note="Protein EARLY RESPONSIVE TO DEHYDRATION 15"
FT                   /id="PRO_0000419743"
FT   REGION          118..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           10..20
FT                   /note="PAM2-like"
FT   VAR_SEQ         115..120
FT                   /note="FGKNGE -> KSVSFP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14993207"
FT                   /id="VSP_044341"
FT   VAR_SEQ         121..163
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14993207"
FT                   /id="VSP_044342"
FT   MUTAGEN         9..13
FT                   /note="Missing: Loss of PAB2-binding."
FT                   /evidence="ECO:0000269|PubMed:15650869"
FT   CONFLICT        82
FT                   /note="D -> Y (in Ref. 7; AAM64638)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   163 AA;  18411 MW;  F110A4F395417223 CRC64;
     MAMVSGRRST LNPDAPLFIP AAVRQVEDFS PEWWQLVTTS TWYPDYWISQ QQQGADGFYD
     NGENENGGGH IDVADLLPES FDFDDMEDFF DTDAAEFDQG FDGRMYYQAP SEFGFGKNGE
     MVKKSSGNRS PRSIVEPAKY AEKPAKWGNQ RVAAAPRNIH QPR
 
 
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