CAR5_ARATH
ID CAR5_ARATH Reviewed; 200 AA.
AC Q9LP65; B4G290; F4HYI3;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein C2-DOMAIN ABA-RELATED 5 {ECO:0000303|PubMed:25465408};
GN Name=CAR5 {ECO:0000303|PubMed:25465408};
GN OrderedLocusNames=At1g48590 {ECO:0000312|Araport:AT1G48590};
GN ORFNames=T1N15.21 {ECO:0000312|EMBL:AAF79703.1};
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] (ISOFORM 2).
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 FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, GENE FAMILY, AND
RP 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 -!- 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:0000269|PubMed:25465408}.
CC Nucleus {ECO:0000269|PubMed:25465408}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LP65-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LP65-2; Sequence=VSP_057721;
CC Name=3;
CC IsoId=Q9LP65-3; Sequence=VSP_057722;
CC -!- DISRUPTION PHENOTYPE: When associated with disruption in CAR1, CAR4 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}.
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DR EMBL; AC020889; AAF79703.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32319.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32320.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32321.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60097.1; -; Genomic_DNA.
DR EMBL; BT043478; ACF88483.1; -; mRNA.
DR PIR; E96525; E96525.
DR RefSeq; NP_001185174.1; NM_001198245.1. [Q9LP65-1]
DR RefSeq; NP_001185175.1; NM_001198246.1. [Q9LP65-3]
DR RefSeq; NP_001322406.1; NM_001333345.1. [Q9LP65-2]
DR RefSeq; NP_175292.2; NM_103755.3. [Q9LP65-2]
DR AlphaFoldDB; Q9LP65; -.
DR SMR; Q9LP65; -.
DR STRING; 3702.AT1G48590.2; -.
DR PaxDb; Q9LP65; -.
DR PRIDE; Q9LP65; -.
DR ProteomicsDB; 222800; -. [Q9LP65-1]
DR EnsemblPlants; AT1G48590.1; AT1G48590.1; AT1G48590. [Q9LP65-2]
DR EnsemblPlants; AT1G48590.2; AT1G48590.2; AT1G48590. [Q9LP65-1]
DR EnsemblPlants; AT1G48590.3; AT1G48590.3; AT1G48590. [Q9LP65-3]
DR EnsemblPlants; AT1G48590.4; AT1G48590.4; AT1G48590. [Q9LP65-2]
DR GeneID; 841280; -.
DR Gramene; AT1G48590.1; AT1G48590.1; AT1G48590. [Q9LP65-2]
DR Gramene; AT1G48590.2; AT1G48590.2; AT1G48590. [Q9LP65-1]
DR Gramene; AT1G48590.3; AT1G48590.3; AT1G48590. [Q9LP65-3]
DR Gramene; AT1G48590.4; AT1G48590.4; AT1G48590. [Q9LP65-2]
DR KEGG; ath:AT1G48590; -.
DR Araport; AT1G48590; -.
DR TAIR; locus:2198024; AT1G48590.
DR eggNOG; KOG1030; Eukaryota.
DR InParanoid; Q9LP65; -.
DR OrthoDB; 1371982at2759; -.
DR PhylomeDB; Q9LP65; -.
DR PRO; PR:Q9LP65; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LP65; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA: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 PRINTS; PR00360; C2DOMAIN.
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; Alternative splicing; Calcium;
KW Cell membrane; GTPase activation; Lipid-binding; Membrane; Metal-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..200
FT /note="Protein C2-DOMAIN ABA-RELATED 5"
FT /id="PRO_0000433315"
FT DOMAIN 22..142
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /id="VSP_057721"
FT VAR_SEQ 74..105
FT /note="Missing (in isoform 3)"
FT /id="VSP_057722"
SQ SEQUENCE 200 AA; 22755 MW; 572F77699202D07B CRC64;
MIVSFLYFSS LFPTSLRKIN LVAGEKHKDR RMKPSLMDSL LGLLRIRIKR GVNLAVRDLN
SSDPYVVVKM AKQKLKTRVI YKNVNPEWNE DLTLSVSDPN LTVLLTVYDY DTFTKDDKMG
DAEFGIKPFV NALKMHLHDL PSGTIVTTVQ PSRDNCLAEE SRVIWSDGKL VQDIVLRLRH
VECGEVEAQL QWIDLPGKGL
