GAP1_ORYSJ
ID GAP1_ORYSJ Reviewed; 165 AA.
AC Q6YWF1; A0A0N7KF73;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=GTPase activating protein 1 {ECO:0000303|PubMed:19086295};
DE Short=OsGAP1 {ECO:0000303|PubMed:19086295};
DE AltName: Full=G-protein binding protein 1 {ECO:0000303|PubMed:18182423};
DE Short=OsGPBP1 {ECO:0000303|PubMed:18182423};
GN Name=GAP1 {ECO:0000303|PubMed:19086295};
GN Synonyms=GPBP1 {ECO:0000303|PubMed:18182423};
GN OrderedLocusNames=Os02g0327000 {ECO:0000312|EMBL:BAF08623.1},
GN LOC_Os02g22130 {ECO:0000305};
GN ORFNames=OsJ_06508 {ECO:0000312|EMBL:EAZ22831.1},
GN OSJNBb0042G06.10 {ECO:0000312|EMBL:BAD16390.1},
GN P0476C12.36 {ECO:0000312|EMBL:BAD15699.1};
OS Oryza sativa subsp. japonica (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=39947 {ECO:0000312|Proteomes:UP000059680};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=18182423; DOI=10.1093/jxb/erm272;
RA Cheung M.-Y., Zeng N.-Y., Tong S.-W., Li F.W.-Y., Zhao K.-J., Zhang Q.,
RA Sun S.S.-M., Lam H.-M.;
RT "Expression of a RING-HC protein from rice improves resistance to
RT Pseudomonas syringae pv. tomato DC3000 in transgenic Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 58:4147-4159(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, INDUCTION BY WOUNDING, AND INTERACTION WITH YCHF1.
RC STRAIN=cv. Aichi asahi;
RX PubMed=19086295; DOI=10.1111/j.1469-8137.2008.02473.x;
RA Cheung M.-Y., Zeng N.-Y., Tong S.-W., Li W.-Y., Xue Y., Zhao K.-J.,
RA Wang C., Zhang Q., Fu Y., Sun Z., Sun S.-S., Lam H.-M.;
RT "Constitutive expression of a rice GTPase-activating protein induces
RT defense responses.";
RL New Phytol. 179:530-545(2008).
RN [8]
RP FUNCTION, INTERACTION WITH YCHF1, AND SUBCELLULAR LOCATION.
RX PubMed=20876569; DOI=10.1074/jbc.m110.172080;
RA Cheung M.Y., Xue Y., Zhou L., Li M.W., Sun S.S., Lam H.M.;
RT "An ancient P-loop GTPase in rice is regulated by a higher plant-specific
RT regulatory protein.";
RL J. Biol. Chem. 285:37359-37369(2010).
RN [9]
RP FUNCTION, INTERACTION WITH YCHF1, AND SUBCELLULAR LOCATION.
RX PubMed=23550829; DOI=10.1111/pce.12108;
RA Cheung M.-Y., Li M.-W., Yung Y.-L., Wen C.-Q., Lam H.-M.;
RT "The unconventional P-loop NTPase OsYchF1 and its regulator OsGAP1 play
RT opposite roles in salinity stress tolerance.";
RL Plant Cell Environ. 36:2008-2020(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), FUNCTION, AND MUTAGENESIS OF LEU-5;
RP LEU-8; ASP-23; ASP-28; LYS-37; LYS-39; LYS-41; ARG-43; THR-58; SER-60;
RP ARG-117; ASN-119; GLU-123; GLU-124; ARG-141; ARG-143; GLU-146 AND GLU-149.
RX PubMed=26286751; DOI=10.1074/jbc.m115.655639;
RA Yung Y.L., Cheung M.Y., Miao R., Fong Y.H., Li K.P., Yu M.H., Chye M.L.,
RA Wong K.B., Lam H.M.;
RT "Site-directed mutagenesis shows the significance of interactions with
RT phospholipids and the G-protein OsYchF1 for the physiological functions of
RT the rice GTPase-activating protein 1 (OsGAP1).";
RL J. Biol. Chem. 290:23984-23996(2015).
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 (PubMed:19086295, PubMed:20876569, PubMed:23550829). Binds
CC phospholipids in a Ca(2+)-independent manner (PubMed:20876569).
CC Promotes tolerance towards salinity stress by limiting the accumulation
CC of reactive oxygen species (ROS) (PubMed:19086295, PubMed:23550829).
CC Promotes resistance to bacterial pathogens, such as Xanthomonas oryzae
CC pv. oryzae and Pseudomonas syringae pv. tomato strain DC3000
CC (PubMed:19086295). Binding to YCHF1 is required for its role in
CC stimulating defense responses and the ability to alleviate salt stress
CC (PubMed:26286751). {ECO:0000250|UniProtKB:Q9LVH4,
CC ECO:0000269|PubMed:19086295, ECO:0000269|PubMed:20876569,
CC ECO:0000269|PubMed:23550829, ECO:0000269|PubMed:26286751}.
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). Interacts with YchF1 (PubMed:19086295,
CC PubMed:23550829, PubMed:20876569). {ECO:0000250|UniProtKB:Q9LVH4,
CC ECO:0000269|PubMed:19086295, ECO:0000269|PubMed:20876569,
CC ECO:0000269|PubMed:23550829}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20876569,
CC ECO:0000269|PubMed:23550829}. Nucleus {ECO:0000250|UniProtKB:Q9LVH4}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:20876569,
CC ECO:0000269|PubMed:23550829}. Note=Localized mainly in the cytosol
CC under NaCl treatment, but translocates to the plasma membrane upon
CC wounding. {ECO:0000269|PubMed:20876569, ECO:0000269|PubMed:23550829}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:19086295}.
CC -!- SIMILARITY: Belongs to the plant CAR protein family. {ECO:0000305}.
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DR EMBL; EF584506; ABU62827.1; -; mRNA.
DR EMBL; AP004789; BAD15699.1; -; Genomic_DNA.
DR EMBL; AP005778; BAD16390.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08623.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS78417.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ22831.1; -; Genomic_DNA.
DR EMBL; AK073631; BAG93560.1; -; mRNA.
DR EMBL; AK104165; BAG96469.1; -; mRNA.
DR RefSeq; XP_015627601.1; XM_015772115.1.
DR PDB; 4RJ9; X-ray; 1.63 A; A=1-165.
DR PDBsum; 4RJ9; -.
DR AlphaFoldDB; Q6YWF1; -.
DR SMR; Q6YWF1; -.
DR STRING; 4530.OS02T0327000-01; -.
DR PaxDb; Q6YWF1; -.
DR PRIDE; Q6YWF1; -.
DR EnsemblPlants; Os02t0327000-01; Os02t0327000-01; Os02g0327000.
DR EnsemblPlants; Os02t0327000-02; Os02t0327000-02; Os02g0327000.
DR GeneID; 4329192; -.
DR Gramene; Os02t0327000-01; Os02t0327000-01; Os02g0327000.
DR Gramene; Os02t0327000-02; Os02t0327000-02; Os02g0327000.
DR KEGG; osa:4329192; -.
DR eggNOG; KOG1030; Eukaryota.
DR HOGENOM; CLU_106037_0_0_1; -.
DR InParanoid; Q6YWF1; -.
DR OMA; KPNRENC; -.
DR OrthoDB; 1360428at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6YWF1; OS.
DR GO; GO:0005829; C:cytosol; IDA: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; IDA: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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP: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; Calcium; Cell membrane;
KW Cytoplasm; GTPase activation; Lipid-binding; Membrane; Metal-binding;
KW Nucleus; Plant defense; Reference proteome.
FT CHAIN 1..165
FT /note="GTPase activating protein 1"
FT /id="PRO_0000433309"
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"
FT MUTAGEN 5
FT /note="L->A: Abolishes binding to YCHF1, but no effect on
FT phospholipid binding; when associated with A-8; A-58 and A-
FT 60."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 8
FT /note="L->A: Abolishes binding to YCHF1, but no effect on
FT phospholipid binding; when associated with A-5; A-58 and A-
FT 60."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 23
FT /note="D->A: Abolishes phospholipid binding, but no effect
FT on binding to YCHF1; when associated with A-28."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 28
FT /note="D->A: Abolishes phospholipid binding, but no effect
FT on binding to YCHF1; when associated with A-23."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 37
FT /note="K->A: Abolishes binding to YCHF1, and partial loss
FT of phospholipid binding; when associated with A-39; A-41
FT and A-43."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 39
FT /note="K->A: Abolishes binding to YCHF1, and partial loss
FT of phospholipid binding; when associated with A-37; A-41
FT and A-43."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 41
FT /note="K->A: Abolishes binding to YCHF1, and partial loss
FT of phospholipid binding; when associated with A-37; A-39
FT and A-43."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 43
FT /note="R->A: Abolishes binding to YCHF1, and partial loss
FT of phospholipid binding; when associated with A-37; A-39
FT and A-41."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 58
FT /note="T->A: Abolishes binding to YCHF1, but no effect on
FT phospholipid binding; when associated with A-5; A-8 and A-
FT 60."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 60
FT /note="S->A: Abolishes binding to YCHF1, but no effect on
FT phospholipid binding; when associated with A-8; A-8 and A-
FT 58."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 117
FT /note="R->A: Abolishes phospholipid binding, but no effect
FT on binding to YCHF1; when associated with A-119; A-123 and
FT A-124."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 119
FT /note="N->A: Abolishes phospholipid binding, but no effect
FT on binding to YCHF1; when associated with A-117; A-123 and
FT A-124."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 123
FT /note="E->A: Abolishes phospholipid binding, but no effect
FT on binding to YCHF1; when associated with A-117; A-119 and
FT A-124."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 124
FT /note="E->A: Abolishes phospholipid binding, but no effect
FT on binding to YCHF1; when associated with A-117; A-119 and
FT A-123."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 141
FT /note="R->A: Abolishes phospholipid binding, but no effect
FT on binding to YCHF1; when associated with A-143; A-146 and
FT A-149."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 143
FT /note="R->A: Abolishes phospholipid binding, but no effect
FT on binding to YCHF1; when associated with A-141; A-146 and
FT A-149."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 146
FT /note="E->A: Abolishes phospholipid binding, but no effect
FT on binding to YCHF1; when associated with A-141; A-143 and
FT A-149."
FT /evidence="ECO:0000269|PubMed:26286751"
FT MUTAGEN 149
FT /note="E->A: Abolishes phospholipid binding, but no effect
FT on binding to YCHF1; when associated with A-141; A-143 and
FT A-146."
FT /evidence="ECO:0000269|PubMed:26286751"
FT STRAND 7..18
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4RJ9"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:4RJ9"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:4RJ9"
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
