CAR9_ARATH
ID CAR9_ARATH Reviewed; 185 AA.
AC Q9S7J9;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein C2-DOMAIN ABA-RELATED 9 {ECO:0000303|PubMed:25465408};
GN Name=CAR9 {ECO:0000303|PubMed:25465408};
GN OrderedLocusNames=At1g70790 {ECO:0000312|Araport:AT1G70790};
GN ORFNames=F15H11.4 {ECO:0000312|EMBL:AAG52327.1},
GN F5A18.3 {ECO:0000312|EMBL:AAG52327.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, 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 (PubMed:25465408).
CC {ECO:0000250|UniProtKB:Q9LVH4, ECO:0000269|PubMed:25465408}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
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 -!- DISRUPTION PHENOTYPE: When associated with disruption in CAR1, CAR4 and
CC CAR5 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}.
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DR EMBL; AC008148; AAD55494.1; -; Genomic_DNA.
DR EMBL; AC011663; AAG52327.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35116.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35117.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60806.1; -; Genomic_DNA.
DR EMBL; BT026107; ABG48463.1; -; mRNA.
DR EMBL; AY085364; AAM62594.1; -; mRNA.
DR PIR; E96732; E96732.
DR RefSeq; NP_001319362.1; NM_001334479.1.
DR RefSeq; NP_565001.1; NM_105747.3.
DR RefSeq; NP_849874.1; NM_179543.3.
DR AlphaFoldDB; Q9S7J9; -.
DR SMR; Q9S7J9; -.
DR STRING; 3702.AT1G70790.1; -.
DR PaxDb; Q9S7J9; -.
DR PRIDE; Q9S7J9; -.
DR ProteomicsDB; 240250; -.
DR EnsemblPlants; AT1G70790.1; AT1G70790.1; AT1G70790.
DR EnsemblPlants; AT1G70790.2; AT1G70790.2; AT1G70790.
DR EnsemblPlants; AT1G70790.3; AT1G70790.3; AT1G70790.
DR GeneID; 843416; -.
DR Gramene; AT1G70790.1; AT1G70790.1; AT1G70790.
DR Gramene; AT1G70790.2; AT1G70790.2; AT1G70790.
DR Gramene; AT1G70790.3; AT1G70790.3; AT1G70790.
DR KEGG; ath:AT1G70790; -.
DR Araport; AT1G70790; -.
DR TAIR; locus:2013905; AT1G70790.
DR eggNOG; KOG1030; Eukaryota.
DR HOGENOM; CLU_106037_0_0_1; -.
DR InParanoid; Q9S7J9; -.
DR OMA; DESSIIW; -.
DR OrthoDB; 1345669at2759; -.
DR PhylomeDB; Q9S7J9; -.
DR PRO; PR:Q9S7J9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S7J9; baseline and differential.
DR Genevisible; Q9S7J9; AT.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; IMP: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..185
FT /note="Protein C2-DOMAIN ABA-RELATED 9"
FT /id="PRO_0000433319"
FT DOMAIN 1..104
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 185 AA; 21054 MW; 7E2AC0D42F6D207F CRC64;
MEDKPLGILR VHVKRGINLA IRDATTSDPY VVITLANQKL KTRVINNNCN PVWNEQLTLS
IKDVNDPIRL TVFDKDRFSG DDKMGDAEID FRPFLEAHQM ELDFQKLPNG CAIKRIRPGR
TNCLAEESSI TWSNGKIMQE MILRLKNVEC GEVELMLEWT DGPGCKGLGR EGSKKTPWMP
TKRLD
