OCP3_ARATH
ID OCP3_ARATH Reviewed; 354 AA.
AC Q8H0V5; Q9LFN0;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein OVEREXPRESSOR OF CATIONIC PEROXIDASE 3 {ECO:0000303|PubMed:15923348};
GN Name=OCP3 {ECO:0000303|PubMed:15923348};
GN OrderedLocusNames=At5g11270 {ECO:0000312|Araport:AT5G11270};
GN ORFNames=F2I11.160 {ECO:0000312|EMBL:CAB96662.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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, MUTAGENESIS OF ALA-211, INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15923348; DOI=10.1105/tpc.105.032375;
RA Coego A., Ramirez V., Gil M.J., Flors V., Mauch-Mani B., Vera P.;
RT "An Arabidopsis homeodomain transcription factor, OVEREXPRESSOR OF CATIONIC
RT PEROXIDASE 3, mediates resistance to infection by necrotrophic pathogens.";
RL Plant Cell 17:2123-2137(2005).
RN [5]
RP FUNCTION, MUTAGENESIS OF ALA-211, AND INDUCTION BY DROUGHT AND ABSCISIC
RP ACID.
RC STRAIN=cv. Columbia;
RX PubMed=19175769; DOI=10.1111/j.1365-313x.2009.03804.x;
RA Ramirez V., Coego A., Lopez A., Agorio A., Flors V., Vera P.;
RT "Drought tolerance in Arabidopsis is controlled by the OCP3 disease
RT resistance regulator.";
RL Plant J. 58:578-591(2009).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ALA-211.
RC STRAIN=cv. Columbia;
RX PubMed=20836879; DOI=10.1186/1471-2229-10-199;
RA Ramirez V., Van der Ent S., Garcia-Andrade J., Coego A., Pieterse C.M.,
RA Vera P.;
RT "OCP3 is an important modulator of NPR1-mediated jasmonic acid-dependent
RT induced defenses in Arabidopsis.";
RL BMC Plant Biol. 10:199-199(2010).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ALA-211.
RC STRAIN=cv. Columbia;
RX PubMed=21564353; DOI=10.1111/j.1365-313x.2011.04633.x;
RA Garcia-Andrade J., Ramirez V., Flors V., Vera P.;
RT "Arabidopsis ocp3 mutant reveals a mechanism linking ABA and JA to
RT pathogen-induced callose deposition.";
RL Plant J. 67:783-794(2011).
CC -!- FUNCTION: May modulate chromatin structure by regulation of nucleosome
CC assembly/disassembly (By similarity). Homeodomain transcription factor
CC that mediates jasmonic acid (JA)-mediated COI1-dependent and abscisic
CC acid (ABA)-mediated PMR4-dependent resistance to infection by
CC necrotrophic fungal pathogens (e.g. B.cinerea and P.cucumerina) and
CC bacterial pathogens (e.g. P.syringae DC3000); this resistance involves
CC at least callose deposition (PubMed:15923348, PubMed:20836879,
CC PubMed:21564353). Required for the P.fluorescens WCS417r-triggered JA-
CC dependent induced systemic resistance (ISR) against both P.syringae
CC DC3000 and H.arabidopsidis (PubMed:20836879). Negative regulator of the
CC ABA-dependent drought resistance (PubMed:19175769).
CC {ECO:0000250|UniProtKB:Q70Z19, ECO:0000269|PubMed:15923348,
CC ECO:0000269|PubMed:19175769, ECO:0000269|PubMed:20836879,
CC ECO:0000269|PubMed:21564353}.
CC -!- INTERACTION:
CC Q8H0V5; Q8GXL7: GATA24; NbExp=4; IntAct=EBI-4428411, EBI-4426127;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000269|PubMed:15923348}.
CC -!- INDUCTION: Constitutively expressed in healthy plants but repressed in
CC response to infection by necrotrophic fungi (PubMed:15923348).
CC Repressed by drought and abscisic acid (ABA) (PubMed:19175769).
CC {ECO:0000269|PubMed:15923348, ECO:0000269|PubMed:19175769}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB96662.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL360314; CAB96662.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED91654.1; -; Genomic_DNA.
DR EMBL; BT002017; AAN72028.1; -; mRNA.
DR EMBL; BT008743; AAP42756.1; -; mRNA.
DR RefSeq; NP_196688.2; NM_121165.4.
DR AlphaFoldDB; Q8H0V5; -.
DR SMR; Q8H0V5; -.
DR IntAct; Q8H0V5; 8.
DR STRING; 3702.AT5G11270.1; -.
DR iPTMnet; Q8H0V5; -.
DR PaxDb; Q8H0V5; -.
DR PRIDE; Q8H0V5; -.
DR ProteomicsDB; 238994; -.
DR EnsemblPlants; AT5G11270.1; AT5G11270.1; AT5G11270.
DR GeneID; 830997; -.
DR Gramene; AT5G11270.1; AT5G11270.1; AT5G11270.
DR KEGG; ath:AT5G11270; -.
DR Araport; AT5G11270; -.
DR TAIR; locus:2148012; AT5G11270.
DR eggNOG; ENOG502QV0N; Eukaryota.
DR HOGENOM; CLU_051943_0_0_1; -.
DR InParanoid; Q8H0V5; -.
DR OMA; KRIVKWF; -.
DR OrthoDB; 1361134at2759; -.
DR PhylomeDB; Q8H0V5; -.
DR PRO; PR:Q8H0V5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8H0V5; baseline and differential.
DR Genevisible; Q8H0V5; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0009682; P:induced systemic resistance; IMP:UniProtKB.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0031347; P:regulation of defense response; IMP:UniProtKB.
DR GO; GO:2000071; P:regulation of defense response by callose deposition; IMP:UniProtKB.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009620; P:response to fungus; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR Pfam; PF00046; Homeodomain; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; DNA-binding; Homeobox;
KW Jasmonic acid signaling pathway; Nucleus; Oxidoreductase; Peroxidase;
KW Plant defense; Reference proteome; Repeat.
FT CHAIN 1..354
FT /note="Protein OVEREXPRESSOR OF CATIONIC PEROXIDASE 3"
FT /id="PRO_0000432549"
FT DNA_BIND 286..345
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 65..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 63..70
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 191..198
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 293..300
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 155..179
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 211
FT /note="A->T: In ocp3; increased accumulation of H(2)O(2),
FT abscisic acid (ABA) and constitutive expression of
FT GSTF6/GST1 and PDF1.2A defense genes. Enhanced resistance
FT to the necrotrophic pathogens Botrytis cinerea and
FT Plectosphaerella cucumerina in a jasmonic acid-dependent
FT manner, due, at least, to ABA-dependent intensified callose
FT deposition. Higher drought resistance in an ABA-dependent
FT manner associated with better stomatal closure. Increased
FT sensitivity to plant growth inhibition by ABA. Impaired in
FT Pseudomonas fluorescens WCS417r-triggered induced systemic
FT resistance (ISR) against both Pseudomonas syringae DC3000
FT and Hyaloperonospora arabidopsidis."
FT /evidence="ECO:0000269|PubMed:15923348,
FT ECO:0000269|PubMed:19175769, ECO:0000269|PubMed:20836879,
FT ECO:0000269|PubMed:21564353"
SQ SEQUENCE 354 AA; 39112 MW; 671F1AF5E95A8AB5 CRC64;
MIKAMALSSA GVVSHLHPPS FSSSSGLSVN RVLFRNRNAS PCGLSLPILN PSRSVLVFAR
GKNRKGFVSS SSSSPKKNKK KSLDGADNGG GEEEEDPFEA LFNLLEEDLK NDNSDDEEIS
EEELEALADE LARALGVGDD VDDIDLFGSV TGDVDVDVDN DDDDNDDDDN DDDDDDSEED
ERPTKLKNWQ LKRLAYALKA GRRKTSIKNL AAEVCLDRAY VLELLRDPPP KLLMLSATLP
DEKPPVAAPE NSSPDPSPVE SLSAEDVVVE PKEKVKDEAV HVMQQRWSAQ KRVKKAHIET
LEKVYRRSKR PTNAVVSSIV QVTNLPRKRV LKWFEDKRAE DGVPDKRAPY QAPV
