CAR4_ARATH
ID CAR4_ARATH Reviewed; 177 AA.
AC Q9LVH4;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein C2-DOMAIN ABA-RELATED 4 {ECO:0000303|PubMed:25465408};
DE AltName: Full=C2 domain-containing protein;
DE Short=AtC2;
DE AltName: Full=GTPase activating protein 1 {ECO:0000303|PubMed:23550829};
DE Short=AtGAP1 {ECO:0000303|PubMed:23550829};
GN Name=CAR4 {ECO:0000303|PubMed:25465408};
GN Synonyms=C2, GAP1 {ECO:0000303|PubMed:23550829};
GN OrderedLocusNames=At3g17980 {ECO:0000312|Araport:AT3G17980};
GN ORFNames=MEB5.18 {ECO:0000312|EMBL:BAB02719.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH YCHF1.
RC STRAIN=cv. Col-2, and cv. Columbia;
RX PubMed=23550829; DOI=10.1111/pce.12108;
RA Cheung M.-Y., Li M.-W., Yung Y.-L., Wen C.-Q., Lam H.-M.;
RT "The unconventional P-loop NTPase OsYchF1 and its regulator OsGAP1 play
RT opposite roles in salinity stress tolerance.";
RL Plant Cell Environ. 36:2008-2020(2013).
RN [5]
RP FUNCTION, MUTAGENESIS OF LYS-50; LYS-52; ASP-85 AND ASP-87, SUBCELLULAR
RP LOCATION, SUBUNIT, AND INTERACTION WITH PYR1.
RC STRAIN=cv. Columbia;
RX PubMed=26719420; DOI=10.1073/pnas.1512779113;
RA Diaz M., Sanchez-Barrena M.J., Gonzalez-Rubio J.M., Rodriguez L.,
RA Fernandez D., Antoni R., Yunta C., Belda-Palazon B., Gonzalez-Guzman M.,
RA Peirats-Llobet M., Menendez M., Boskovic J., Marquez J.A., Rodriguez P.L.,
RA Albert A.;
RT "Calcium-dependent oligomerization of CAR proteins at cell membrane
RT modulates ABA signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E396-E405(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
RX PubMed=22139170; DOI=10.1107/s1744309111040541;
RA Diaz M., Rodriguez L., Gonzalez-Guzman M., Martinez-Ripoll M., Albert A.;
RT "Crystallization and preliminary crystallographic analysis of a C2 protein
RT from Arabidopsis thaliana.";
RL Acta Crystallogr. F 67:1575-1578(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH CALCIUM, FUNCTION,
RP DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-85 AND ASP-87, SUBCELLULAR
RP LOCATION, INTERACTION WITH PYR1; PYL1; PYL4; PYL6 AND PYL8, GENE FAMILY,
RP AND NOMENCLATURE.
RX PubMed=25465408; DOI=10.1105/tpc.114.129973;
RA Rodriguez L., Gonzalez-Guzman M., Diaz M., Rodrigues A.,
RA Izquierdo-Garcia A.C., Peirats-Llobet M., Fernandez M.A., Antoni R.,
RA Fernandez D., Marquez J.A., Mulet J.M., Albert A., Rodriguez P.L.;
RT "C2-domain abscisic acid-related proteins mediate the interaction of
RT PYR/PYL/RCAR abscisic acid receptors with the plasma membrane and regulate
RT abscisic acid sensitivity in Arabidopsis.";
RL Plant Cell 26:4802-4820(2014).
CC -!- FUNCTION: Mediates the transient calcium-dependent interaction of
CC PYR/PYL/RCAR abscisic acid (ABA) receptors with the plasma membrane and
CC thus regulates ABA sensitivity (PubMed:26719420, PubMed:25465408).
CC Stimulates the GTPase/ATPase activities of YchF1, and regulates its
CC subcellular localization. Promotes tolerance towards salinity stress by
CC limiting the accumulation of reactive oxygen species (ROS)
CC (PubMed:23550829). Promotes resistance to bacterial pathogens (e.g.
CC Xanthomonas oryzae pv. oryzae and P. syringae pv. tomato DC3000) (By
CC similarity). Binds liposomes in the absence of exogenous Ca(2+), but
CC this activity is enhanced in the presence of Ca(2+) and generates
CC membrane curvature (PubMed:26719420). {ECO:0000250|UniProtKB:Q6YWF1,
CC ECO:0000269|PubMed:23550829, ECO:0000269|PubMed:25465408,
CC ECO:0000269|PubMed:26719420}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Dimers and oligomers (PubMed:26719420). Binds to PYR/PYL/RCAR
CC abscisic acid intracellular receptors in an ABA-independent manner,
CC both at the plasma membrane and in the nucleus (PubMed:25465408,
CC PubMed:26719420). Interacts directly with PYR1, PYL1, PYL4, PYL6 and
CC PYL8 (PubMed:25465408, PubMed:26719420). Binds phospholipids in a
CC Ca(2+)-dependent manner (PubMed:25465408). Interacts with YchF1
CC (PubMed:23550829). {ECO:0000269|PubMed:23550829,
CC ECO:0000269|PubMed:25465408, ECO:0000269|PubMed:26719420}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25465408,
CC ECO:0000269|PubMed:26719420}. Nucleus {ECO:0000269|PubMed:25465408}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:23550829,
CC ECO:0000269|PubMed:26719420}. Note=Localized mainly in the cytosol
CC under NaCl treatment, but translocates to the plasma membrane upon
CC wounding. {ECO:0000269|PubMed:23550829}.
CC -!- DISRUPTION PHENOTYPE: When associated with disruption in CAR1, CAR5 and
CC CAR9 genes, reduced sensitivity to abscisic acid (ABA) during seedling
CC establishment and root growth regulation.
CC {ECO:0000269|PubMed:25465408}.
CC -!- SIMILARITY: Belongs to the plant CAR protein family.
CC {ECO:0000305|PubMed:25465408}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB019230; BAB02719.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76031.1; -; Genomic_DNA.
DR EMBL; BT021979; AAY17416.1; -; mRNA.
DR EMBL; BT030626; ABR46206.1; -; mRNA.
DR RefSeq; NP_188425.2; NM_112679.4.
DR PDB; 4V29; X-ray; 1.60 A; A/B=1-177.
DR PDB; 5A4X; X-ray; 2.20 A; A/B=1-177.
DR PDB; 5A50; X-ray; 2.40 A; A/B=1-177.
DR PDB; 5A51; X-ray; 1.60 A; A/B=1-177.
DR PDBsum; 4V29; -.
DR PDBsum; 5A4X; -.
DR PDBsum; 5A50; -.
DR PDBsum; 5A51; -.
DR AlphaFoldDB; Q9LVH4; -.
DR SMR; Q9LVH4; -.
DR STRING; 3702.AT3G17980.1; -.
DR PaxDb; Q9LVH4; -.
DR PRIDE; Q9LVH4; -.
DR ProteomicsDB; 240594; -.
DR EnsemblPlants; AT3G17980.1; AT3G17980.1; AT3G17980.
DR GeneID; 821323; -.
DR Gramene; AT3G17980.1; AT3G17980.1; AT3G17980.
DR KEGG; ath:AT3G17980; -.
DR Araport; AT3G17980; -.
DR TAIR; locus:2088505; AT3G17980.
DR eggNOG; KOG1030; Eukaryota.
DR HOGENOM; CLU_106037_0_0_1; -.
DR InParanoid; Q9LVH4; -.
DR OMA; VKMGRQK; -.
DR OrthoDB; 1371982at2759; -.
DR PhylomeDB; Q9LVH4; -.
DR PRO; PR:Q9LVH4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVH4; baseline and differential.
DR Genevisible; Q9LVH4; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IMP:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR044562; CAR1-11.
DR PANTHER; PTHR45933; PTHR45933; 1.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Calcium; Cell membrane;
KW Cytoplasm; GTPase activation; Lipid-binding; Membrane; Metal-binding;
KW Nucleus; Plant defense; Reference proteome.
FT CHAIN 1..177
FT /note="Protein C2-DOMAIN ABA-RELATED 4"
FT /id="PRO_0000433314"
FT DOMAIN 4..118
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0007744|PDB:4V29"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0007744|PDB:4V29"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0007744|PDB:4V29"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0007744|PDB:4V29"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0007744|PDB:4V29"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0007744|PDB:4V29"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0007744|PDB:4V29"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0007744|PDB:4V29"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0007744|PDB:4V29"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0007744|PDB:4V29"
FT MUTAGEN 50
FT /note="K->A: Small reduction in the ability to bind
FT liposomes in the absence of free Ca(2+); when associated
FT with A-52."
FT /evidence="ECO:0000269|PubMed:26719420"
FT MUTAGEN 52
FT /note="K->A: Small reduction in the ability to bind
FT liposomes in the absence of free Ca(2+); when associated
FT with A-50."
FT /evidence="ECO:0000269|PubMed:26719420"
FT MUTAGEN 85
FT /note="D->A: Impaired Ca(2+)-dependent phospholipids
FT binding and reduced abscisic acid (ABA) sensitivity, as
FT well as altered membrane localization and PYR1 binding;
FT when associated with A-87."
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0000269|PubMed:26719420"
FT MUTAGEN 87
FT /note="D->A: Impaired Ca(2+)-dependent phospholipids
FT binding and reduced abscisic acid (ABA) sensitivity, as
FT well as altered membrane localization and PYR1 binding;
FT when associated with A-85."
FT /evidence="ECO:0000269|PubMed:25465408,
FT ECO:0000269|PubMed:26719420"
FT STRAND 18..29
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5A4X"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:4V29"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:4V29"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5A4X"
SQ SEQUENCE 177 AA; 19900 MW; 8B9D5D1601868E1B CRC64;
MTTACPARTS SLMDDLLGLL RIRIKRGVNL AVRDISSSDP YVVVKMGKQK LKTRVINKDV
NPEWNEDLTL SVTDSNLTVL LTVYDHDMFS KDDKMGDAEF EIKPYIEALR MQLDGLPSGT
IVTTVKPSRR NCLAEESRVT WVDGKLVQDL VLRLRHVECG EVEAQLQWID LPGSKGL
