GAP1_ORYSI
ID GAP1_ORYSI Reviewed; 165 AA.
AC A2X479;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=GTPase activating protein 1 {ECO:0000305};
DE Short=OsGAP1 {ECO:0000305};
DE AltName: Full=G-protein binding protein 1 {ECO:0000305};
DE Short=OsGPBP1 {ECO:0000305};
GN ORFNames=OsI_07012 {ECO:0000312|EMBL:EAY85639.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000312|Proteomes:UP000007015};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Mediates the transient calcium-dependent interaction of
CC PYR/PYL/RCAR abscisic acid (ABA) receptors with the plasma membrane and
CC thus regulates ABA sensitivity (By similarity). Stimulates the
CC GTPase/ATPase activities of YchF1, and regulates its subcellular
CC localization. Promotes tolerance towards salinity stress by limiting
CC the accumulation of reactive oxygen species (ROS). Promotes resistance
CC to bacterial pathogens (By similarity). {ECO:0000250|UniProtKB:Q6YWF1,
CC 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. Binds phospholipids in a Ca(2+)-dependent manner (By
CC similarity). Interacts with YchF1 (By similarity).
CC {ECO:0000250|UniProtKB:Q6YWF1, ECO:0000250|UniProtKB:Q9LVH4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9LVH4}.
CC Nucleus {ECO:0000250|UniProtKB:Q9LVH4}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6YWF1}. Note=Localized mainly in the cytosol
CC under NaCl treatment, but translocates to the plasma membrane upon
CC wounding. {ECO:0000250|UniProtKB:Q6YWF1}.
CC -!- SIMILARITY: Belongs to the plant CAR protein family. {ECO:0000305}.
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DR EMBL; CM000127; EAY85639.1; -; Genomic_DNA.
DR AlphaFoldDB; A2X479; -.
DR SMR; A2X479; -.
DR STRING; 39946.A2X479; -.
DR EnsemblPlants; BGIOSGA008103-TA; BGIOSGA008103-PA; BGIOSGA008103.
DR Gramene; BGIOSGA008103-TA; BGIOSGA008103-PA; BGIOSGA008103.
DR HOGENOM; CLU_106037_0_0_1; -.
DR OMA; KPNRENC; -.
DR Proteomes; UP000007015; Chromosome 2.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IEA:EnsemblPlants.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:1901002; P:positive regulation of response to salt stress; ISS:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; ISS:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEA:EnsemblPlants.
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 3: Inferred from homology;
KW Abscisic acid signaling pathway; Calcium; Cell membrane; Cytoplasm;
KW GTPase activation; Lipid-binding; Membrane; Metal-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..165
FT /note="GTPase activating protein 1"
FT /id="PRO_0000433310"
FT DOMAIN 1..105
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 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9LVH4"
SQ SEQUENCE 165 AA; 18548 MW; 1FC73789C7A67D74 CRC64;
MLGHLVGLVK VRVVRGVNLA VRDLRSSDPY VIVRMGKQKL KTRVIKKTTN PEWNDELTLS
IEDPAVPVRL EVYDKDTFID DAMGNAELDI RPLVEVVKMK IEGVADNTVV KKVVPNRQNC
LAEESTIYIS EGKVKQDVVL RLRDVECGEI ELQLQWVDIP GSKGV
