CAR8_ARATH
ID CAR8_ARATH Reviewed; 165 AA.
AC O49303;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein C2-DOMAIN ABA-RELATED 8 {ECO:0000303|PubMed:25465408};
GN Name=CAR8 {ECO:0000303|PubMed:25465408};
GN OrderedLocusNames=At1g23140 {ECO:0000312|Araport:AT1G23140};
GN ORFNames=T26J12.9 {ECO:0000312|EMBL:AAC00606.1};
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 de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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; AC002311; AAC00606.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30344.1; -; Genomic_DNA.
DR EMBL; BT043489; ACF88494.1; -; mRNA.
DR PIR; F86365; F86365.
DR RefSeq; NP_173727.1; NM_102162.3.
DR AlphaFoldDB; O49303; -.
DR SMR; O49303; -.
DR STRING; 3702.AT1G23140.1; -.
DR PaxDb; O49303; -.
DR PRIDE; O49303; -.
DR ProteomicsDB; 240280; -.
DR EnsemblPlants; AT1G23140.1; AT1G23140.1; AT1G23140.
DR GeneID; 838922; -.
DR Gramene; AT1G23140.1; AT1G23140.1; AT1G23140.
DR KEGG; ath:AT1G23140; -.
DR Araport; AT1G23140; -.
DR TAIR; locus:2201190; AT1G23140.
DR eggNOG; KOG1030; Eukaryota.
DR HOGENOM; CLU_106037_0_0_1; -.
DR InParanoid; O49303; -.
DR OMA; ITVEIGW; -.
DR OrthoDB; 1345669at2759; -.
DR PhylomeDB; O49303; -.
DR PRO; PR:O49303; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O49303; baseline and differential.
DR Genevisible; O49303; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; Acetylation; Calcium; Cell membrane;
KW GTPase activation; Lipid-binding; Membrane; Metal-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..165
FT /note="Protein C2-DOMAIN ABA-RELATED 8"
FT /id="PRO_0000433318"
FT DOMAIN 1..106
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
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 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 73
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="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9SSL1"
SQ SEQUENCE 165 AA; 18569 MW; 5B6F0678DA10962F CRC64;
MENLVGLLRI RVKRGINLVS RDSNTSDPFV VVTMGSQKLK TRGVENSCNP EWDDELTLGI
NDPNQHVTLE VYDKDTFTSH DPMGDAEIDI KPFFEVQGTD IQELTNGTEI RRVKPSGDNC
LAEESRIIFS NGKILQDMIL QLRNVESGEV EIQIEWINVT GSSDF
