CAR10_ARATH
ID CAR10_ARATH Reviewed; 180 AA.
AC Q9ZVF1;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein C2-DOMAIN ABA-RELATED 10 {ECO:0000303|PubMed:25465408};
GN Name=CAR10 {ECO:0000303|PubMed:25465408};
GN OrderedLocusNames=At2g01540 {ECO:0000312|Araport:AT2G01540};
GN ORFNames=F2I9.16 {ECO:0000312|EMBL:AAC67330.1};
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 {ECO:0000312|Proteomes:UP000006548};
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 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 GENE FAMILY, 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: Stimulates the GTPase/ATPase activities of Obg-like ATPases
CC (By similarity). Mediates the transient calcium-dependent interaction
CC of PYR/PYL/RCAR abscisic acid (ABA) receptors with the plasma membrane
CC and thus regulates ABA sensitivity (By similarity).
CC {ECO:0000250|UniProtKB:Q9FHP6, ECO:0000250|UniProtKB:Q9LVH4}.
CC -!- SUBUNIT: Binds to PYR/PYL/RCAR abscisic acid intracellular receptors in
CC an ABA-independent manner, both at the plasma membrane and in the
CC nucleus. {ECO:0000250|UniProtKB:Q9FHP6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9FHP6}.
CC Nucleus {ECO:0000250|UniProtKB:Q9FHP6}.
CC -!- SIMILARITY: Belongs to the plant CAR protein family.
CC {ECO:0000305|PubMed:25465408}.
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DR EMBL; AC005560; AAC67330.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05466.1; -; Genomic_DNA.
DR EMBL; AY062604; AAL32682.1; -; mRNA.
DR EMBL; AY093363; AAM13362.1; -; mRNA.
DR PIR; A84426; A84426.
DR RefSeq; NP_178263.1; NM_126215.5.
DR AlphaFoldDB; Q9ZVF1; -.
DR SMR; Q9ZVF1; -.
DR IntAct; Q9ZVF1; 3.
DR STRING; 3702.AT2G01540.1; -.
DR PaxDb; Q9ZVF1; -.
DR PRIDE; Q9ZVF1; -.
DR ProteomicsDB; 239193; -.
DR EnsemblPlants; AT2G01540.1; AT2G01540.1; AT2G01540.
DR GeneID; 814683; -.
DR Gramene; AT2G01540.1; AT2G01540.1; AT2G01540.
DR KEGG; ath:AT2G01540; -.
DR Araport; AT2G01540; -.
DR TAIR; locus:2049602; AT2G01540.
DR eggNOG; KOG1030; Eukaryota.
DR HOGENOM; CLU_106037_0_0_1; -.
DR InParanoid; Q9ZVF1; -.
DR OMA; ENINPVW; -.
DR OrthoDB; 1345669at2759; -.
DR PhylomeDB; Q9ZVF1; -.
DR PRO; PR:Q9ZVF1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVF1; baseline and differential.
DR Genevisible; Q9ZVF1; AT.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS: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 2: Evidence at transcript level;
KW Abscisic acid signaling pathway; Calcium; Cell membrane; GTPase activation;
KW Lipid-binding; Membrane; Metal-binding; Nucleus; Reference proteome.
FT CHAIN 1..180
FT /note="Protein C2-DOMAIN ABA-RELATED 10"
FT /id="PRO_0000433320"
FT DOMAIN 1..105
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
SQ SEQUENCE 180 AA; 20085 MW; 159740D3A1E8190F CRC64;
MDQKPLGLLT IHVKRGINLA IRDHRSSDPY IVLNVADQTL KTRVVKKNCN PVWNEEMTVA
IKDPNVPIRL TVFDWDKFTG DDKMGDANID IQPYLEALKM GMELLRLPNG CAIKRVQPSR
HNCLSDESSI VWNNGKITQD LILRLNNVEC GEIEIMLEWH EGAGCRGITS SSKGGGSSST
