CAR6_ARATH
ID CAR6_ARATH Reviewed; 174 AA.
AC Q9S764;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein C2-DOMAIN ABA-RELATED 6 {ECO:0000303|PubMed:25465408};
DE AltName: Full=Protein ENHANCED BENDING 1 {ECO:0000303|PubMed:21367967};
GN Name=CAR6 {ECO:0000303|PubMed:25465408};
GN Synonyms=EHB1 {ECO:0000303|PubMed:21367967};
GN OrderedLocusNames=At1g70800 {ECO:0000312|Araport:AT1G70800};
GN ORFNames=F15H11.5 {ECO:0000312|EMBL:AAD55495.1},
GN F5A18.2 {ECO:0000312|EMBL:AAG52328.1};
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 Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RPT3/NPH3 AND PHOT1.
RX PubMed=21367967; DOI=10.1104/pp.110.167411;
RA Knauer T., Duemmer M., Landgraf F., Forreiter C.;
RT "A negative effector of blue light-induced and gravitropic bending in
RT Arabidopsis.";
RL Plant Physiol. 156:439-447(2011).
RN [5]
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). Prevents hypocotyl
CC bending as well as gravitropic response under blue light conditions
CC (PubMed:21367967). {ECO:0000250|UniProtKB:Q9FHP6,
CC ECO:0000250|UniProtKB:Q9LVH4, ECO:0000269|PubMed:21367967}.
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 (By similarity). Subunit of a complex made of CAR6, PHOT1 and
CC RPT3/NPH3. Interacts directly with RPT3/NPH3 (PubMed:21367967).
CC {ECO:0000250|UniProtKB:Q9FHP6, ECO:0000269|PubMed:21367967}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9FHP6}.
CC Nucleus {ECO:0000250|UniProtKB:Q9FHP6}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to blue light leading to an
CC enhanced phototropic bending and a faster response to gravitropic
CC stimulus. {ECO:0000269|PubMed:21367967}.
CC -!- SIMILARITY: Belongs to the plant CAR protein family.
CC {ECO:0000305|PubMed:25465408}.
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DR EMBL; AC008148; AAD55495.1; -; Genomic_DNA.
DR EMBL; AC011663; AAG52328.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35118.1; -; Genomic_DNA.
DR EMBL; BT010681; AAR20738.1; -; mRNA.
DR EMBL; BT010960; AAR24738.1; -; mRNA.
DR PIR; F96732; F96732.
DR RefSeq; NP_177237.1; NM_105748.3.
DR AlphaFoldDB; Q9S764; -.
DR SMR; Q9S764; -.
DR STRING; 3702.AT1G70800.1; -.
DR PaxDb; Q9S764; -.
DR PRIDE; Q9S764; -.
DR ProteomicsDB; 239182; -.
DR EnsemblPlants; AT1G70800.1; AT1G70800.1; AT1G70800.
DR GeneID; 843417; -.
DR Gramene; AT1G70800.1; AT1G70800.1; AT1G70800.
DR KEGG; ath:AT1G70800; -.
DR Araport; AT1G70800; -.
DR TAIR; locus:2014015; AT1G70800.
DR eggNOG; KOG1030; Eukaryota.
DR HOGENOM; CLU_106037_0_0_1; -.
DR InParanoid; Q9S764; -.
DR OMA; ESSCVWR; -.
DR OrthoDB; 1345669at2759; -.
DR PhylomeDB; Q9S764; -.
DR PRO; PR:Q9S764; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S764; baseline and differential.
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:0009630; P:gravitropism; IMP:UniProtKB.
DR GO; GO:0009638; P:phototropism; IMP:TAIR.
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 GO; GO:0009637; P:response to blue light; IMP:TAIR.
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 Abscisic acid signaling pathway; Calcium; Cell membrane;
KW Developmental protein; GTPase activation; Lipid-binding; Membrane;
KW Metal-binding; Nucleus; Reference proteome.
FT CHAIN 1..174
FT /note="Protein C2-DOMAIN ABA-RELATED 6"
FT /id="PRO_0000433316"
FT DOMAIN 1..115
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 36
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"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
SQ SEQUENCE 174 AA; 19632 MW; CCE7E9618D0666DF CRC64;
MEKTEEEVEM KELVGLVRIL VKRGIDLARR DALSSDPFVV ITMGPQKLKS FTVKNNCNPE
WNEELTLAIE DPNEPVKLMV YDKDTFTADD KMGDAQIDMK PFLDVHKLGL KELPHGKELK
RIVPTRDNCL SEDSIIVSDN GKIVQDMILL LKNVECGKVE IQLEWLKNPG GSGL
