CAR1_ARATH
ID CAR1_ARATH Reviewed; 168 AA.
AC Q9FHP6; C0Z2Y5;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein C2-DOMAIN ABA-RELATED 1 {ECO:0000303|PubMed:25465408};
GN Name=CAR1 {ECO:0000303|PubMed:25465408};
GN OrderedLocusNames=At5g37740 {ECO:0000312|Araport:AT5G37740};
GN ORFNames=K12B20.22 {ECO:0000312|EMBL:BAB08320.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RC TISSUE=Flower {ECO:0000312|EMBL:BAH57064.1}, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, MUTAGENESIS OF ASP-22 AND ASP-27, DISRUPTION PHENOTYPE,
RP INTERACTION WITH PYR1; PYL1; PYL4; PYL6 AND PYL8, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, 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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RC STRAIN=cv. Columbia;
RX PubMed=26719420; DOI=10.1073/pnas.1512779113;
RA Diaz M., Sanchez-Barrena M.J., Gonzalez-Rubio J.M., Rodriguez L.,
RA Fernandez D., Antoni R., Yunta C., Belda-Palazon B., Gonzalez-Guzman M.,
RA Peirats-Llobet M., Menendez M., Boskovic J., Marquez J.A., Rodriguez P.L.,
RA Albert A.;
RT "Calcium-dependent oligomerization of CAR proteins at cell membrane
RT modulates ABA signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E396-E405(2016).
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). Binds liposomes
CC in the absence of exogenous Ca(2+), but this activity is enhanced in
CC the presence of Ca(2+) and generates membrane curvature (By
CC similarity). {ECO:0000250|UniProtKB:Q9LVH4,
CC ECO:0000269|PubMed:25465408}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Dimers and oligomers (By similarity). Binds to PYR/PYL/RCAR
CC abscisic acid intracellular receptors in an ABA-independent manner,
CC both at the plasma membrane and in the nucleus. Interacts directly with
CC PYR1, PYL1, PYL4, PYL6 and PYL8. Binds phospholipids in a Ca(2+)-
CC dependent manner. {ECO:0000250|UniProtKB:Q9LVH4,
CC ECO:0000269|PubMed:25465408}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25465408}.
CC Nucleus {ECO:0000269|PubMed:25465408}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist. {ECO:0000305};
CC Name=1;
CC IsoId=Q9FHP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FHP6-2; Sequence=VSP_057720;
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:25465408}.
CC -!- DEVELOPMENTAL STAGE: Predominantly expressed in the vascular bundle of
CC the primary root and in the cortex of the root upper part. In lateral
CC roots, detected in epidermis and root tips.
CC {ECO:0000269|PubMed:25465408}.
CC -!- DISRUPTION PHENOTYPE: When associated with disruption in CAR4, CAR5 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; AB018107; BAB08320.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94225.1; -; Genomic_DNA.
DR EMBL; AY074354; AAL67050.1; -; mRNA.
DR EMBL; AY113975; AAM45023.1; -; mRNA.
DR EMBL; BT000677; AAN31823.1; -; mRNA.
DR EMBL; AK318949; BAH57064.1; -; mRNA.
DR RefSeq; NP_198590.1; NM_123133.4. [Q9FHP6-1]
DR PDB; 5A52; X-ray; 1.65 A; A=1-168.
DR PDBsum; 5A52; -.
DR AlphaFoldDB; Q9FHP6; -.
DR SMR; Q9FHP6; -.
DR IntAct; Q9FHP6; 1.
DR STRING; 3702.AT5G37740.2; -.
DR EnsemblPlants; AT5G37740.1; AT5G37740.1; AT5G37740. [Q9FHP6-1]
DR GeneID; 833752; -.
DR Gramene; AT5G37740.1; AT5G37740.1; AT5G37740. [Q9FHP6-1]
DR KEGG; ath:AT5G37740; -.
DR Araport; AT5G37740; -.
DR eggNOG; KOG1030; Eukaryota.
DR PhylomeDB; Q9FHP6; -.
DR PRO; PR:Q9FHP6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHP6; baseline and differential.
DR Genevisible; Q9FHP6; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IMP:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; 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 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Acetylation;
KW Alternative splicing; Calcium; Cell membrane; GTPase activation;
KW Lipid-binding; Membrane; Metal-binding; Nucleus; Reference proteome.
FT CHAIN 1..168
FT /note="Protein C2-DOMAIN ABA-RELATED 1"
FT /id="PRO_0000433311"
FT DOMAIN 1..104
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:0000269|PubMed:26719420,
FT ECO:0007744|PDB:5A52"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26719420,
FT ECO:0007744|PDB:5A52"
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:0000269|PubMed:26719420,
FT ECO:0007744|PDB:5A52"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26719420,
FT ECO:0007744|PDB:5A52"
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"
FT VAR_SEQ 1..69
FT /note="MENLVGLLRIHVKRGVNLAIRDISSSDPYIVVHCGKQKLKTRVVKHSVNPEW
FT NDDLTLSVTDPNLPIKL -> MMQ (in isoform 2)"
FT /id="VSP_057720"
FT MUTAGEN 22
FT /note="D->A: Impaired Ca(2+)-dependent phospholipids
FT binding; when associated with A-27."
FT /evidence="ECO:0000269|PubMed:25465408"
FT MUTAGEN 27
FT /note="D->A: Impaired Ca(2+)-dependent phospholipids
FT binding; when associated with A-22."
FT /evidence="ECO:0000269|PubMed:25465408"
FT STRAND 6..17
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:5A52"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:5A52"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:5A52"
SQ SEQUENCE 168 AA; 18842 MW; 488EF142D8CA80D8 CRC64;
MENLVGLLRI HVKRGVNLAI RDISSSDPYI VVHCGKQKLK TRVVKHSVNP EWNDDLTLSV
TDPNLPIKLT VYDYDLLSAD DKMGEAEFHI GPFIEAIKFA HQLGPGLPNG TIIKKIEPSR
KNCLSESSHI VLNQGKIVQN MFLRLQHVEC GEVELQLEWI DVPGSRGI
