DOR_ARATH
ID DOR_ARATH Reviewed; 387 AA.
AC Q5BPS3; Q84RJ0; Q9SIC2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=F-box protein DOR;
DE AltName: Full=Protein DROUGHT TOLERANCE REPRESSOR;
GN Name=DOR; OrderedLocusNames=At2g31470; ORFNames=T28P16.4;
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=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 [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 GENOMIC DNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE, AND
RP INTERACTION WITH ASK14 AND CUL1.
RX PubMed=18835996; DOI=10.1104/pp.108.126912;
RA Zhang Y., Xu W., Li Z., Deng X.W., Wu W., Xue Y.;
RT "F-box protein DOR functions as a novel inhibitory factor for abscisic
RT acid-induced stomatal closure under drought stress in Arabidopsis.";
RL Plant Physiol. 148:2121-2133(2008).
CC -!- FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase
CC complexes, which may mediate the ubiquitination and subsequent
CC proteasomal degradation of target proteins (By similarity). Negative
CC regulator of guard cell abscisic acid (ABA) signaling, especially
CC during drought stress. {ECO:0000250, ECO:0000269|PubMed:18835996}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (ASK-cullin-F-box) protein ligase complex (By
CC similarity). Interacts with ASK14 and CUL1. {ECO:0000250,
CC ECO:0000269|PubMed:18835996}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5BPS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BPS3-2; Sequence=VSP_036630;
CC -!- TISSUE SPECIFICITY: Strongly expressed in guard cells. Mostly
CC represented in seedlings, leaves and flowers, and, to a lower extent,
CC in roots and siliques. {ECO:0000269|PubMed:18835996}.
CC -!- INDUCTION: Repressed by ABA. {ECO:0000269|PubMed:18835996}.
CC -!- DOMAIN: The F-box is necessary for the interaction with ASK proteins.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitive ABA response of stomatal closing
CC and substantial increase of drought tolerance.
CC {ECO:0000269|PubMed:18835996}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD26472.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BX821031; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC007169; AAD26472.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08552.1; -; Genomic_DNA.
DR EMBL; AY924755; AAX23830.1; -; Genomic_DNA.
DR EMBL; BX821031; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY231430; AAO86858.1; -; mRNA.
DR PIR; B84721; B84721.
DR RefSeq; NP_180705.1; NM_128704.2. [Q5BPS3-1]
DR AlphaFoldDB; Q5BPS3; -.
DR BioGRID; 3052; 1.
DR IntAct; Q5BPS3; 2.
DR STRING; 3702.AT2G31470.1; -.
DR PaxDb; Q5BPS3; -.
DR PRIDE; Q5BPS3; -.
DR EnsemblPlants; AT2G31470.1; AT2G31470.1; AT2G31470. [Q5BPS3-1]
DR GeneID; 817705; -.
DR Gramene; AT2G31470.1; AT2G31470.1; AT2G31470. [Q5BPS3-1]
DR KEGG; ath:AT2G31470; -.
DR Araport; AT2G31470; -.
DR TAIR; locus:2061325; AT2G31470.
DR eggNOG; ENOG502SNHU; Eukaryota.
DR HOGENOM; CLU_027176_8_1_1; -.
DR InParanoid; Q5BPS3; -.
DR OMA; SPRYNDV; -.
DR PhylomeDB; Q5BPS3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5BPS3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q5BPS3; baseline and differential.
DR Genevisible; Q5BPS3; AT.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0042631; P:cellular response to water deprivation; IMP:UniProtKB.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:UniProtKB.
DR InterPro; IPR013187; F-box-assoc_dom_typ3.
DR InterPro; IPR017451; F-box-assoc_interact_dom.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF08268; FBA_3; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR TIGRFAMs; TIGR01640; F_box_assoc_1; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..387
FT /note="F-box protein DOR"
FT /id="PRO_0000283391"
FT DOMAIN 19..64
FT /note="F-box"
FT VAR_SEQ 185..387
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16244158"
FT /id="VSP_036630"
SQ SEQUENCE 387 AA; 44770 MW; ABA57A2679C00184 CRC64;
MKSRRQNVSV ARQTILGRDE NFEPIPIDLV IEIFSRSPVK SIARCRCVSK LWASILRLPY
FTELYLTKSC ARPRLLFACQ KHRELFFFST PQPHNPNESS SPLAASFHMK IPFDGRFNII
SPIGGLVFVR YEQILKGRKT PEFVSAICNP STGQSLTLPK PKTRKRIWGT SHFGYDPIEK
QFKVLSMNIG DGVYKEHYVL TLGTENLSWR RIECSIPHVH GSKGICINGV LYYRAKADMF
SGTLMIVCFD VRFEKFSYIK ILKPTTTLIS YNGKLASLVW EGPSYICGKR FEMWVLGDPE
KHEWLKHTYE LRPRWQNVLG EDLLIFAGMT GTNEIVLSPK YPSHPFYVFY YNLERNTIRR
VEIQGMGAFK VNEDYIFLDH VEDVKLI
