ID   RGAP1_ARATH             Reviewed;         466 AA.
AC   Q9FMR1;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Rho GTPase-activating protein 1;
DE   AltName: Full=Rho-type GTPase-activating protein 1;
GN   Name=ROPGAP1; OrderedLocusNames=At5g22400; ORFNames=MWD9.20;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
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   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a GTPase activator for the Rac-type GTPase by
CC       converting it to an inactive GDP-bound state. {ECO:0000250}.
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DR   EMBL; AB007651; BAB08339.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93022.1; -; Genomic_DNA.
DR   EMBL; AK229223; BAF01090.1; -; mRNA.
DR   EMBL; BT026360; ABH04467.1; -; mRNA.
DR   RefSeq; NP_197632.1; NM_122145.5.
DR   AlphaFoldDB; Q9FMR1; -.
DR   SMR; Q9FMR1; -.
DR   BioGRID; 17576; 1.
DR   STRING; 3702.AT5G22400.1; -.
DR   PaxDb; Q9FMR1; -.
DR   PRIDE; Q9FMR1; -.
DR   ProteomicsDB; 236962; -.
DR   EnsemblPlants; AT5G22400.1; AT5G22400.1; AT5G22400.
DR   GeneID; 832301; -.
DR   Gramene; AT5G22400.1; AT5G22400.1; AT5G22400.
DR   KEGG; ath:AT5G22400; -.
DR   Araport; AT5G22400; -.
DR   TAIR; locus:2176392; AT5G22400.
DR   eggNOG; KOG4270; Eukaryota.
DR   HOGENOM; CLU_031591_1_0_1; -.
DR   InParanoid; Q9FMR1; -.
DR   OMA; DFHASIE; -.
DR   OrthoDB; 747695at2759; -.
DR   PhylomeDB; Q9FMR1; -.
DR   PRO; PR:Q9FMR1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FMR1; baseline and differential.
DR   Genevisible; Q9FMR1; AT.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 3.90.810.10; -; 1.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR036936; CRIB_dom_sf.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR044785; RopGAP1-5.
DR   PANTHER; PTHR23177; PTHR23177; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   2: Evidence at transcript level;
KW   GTPase activation; Reference proteome.
FT   CHAIN           1..466
FT                   /note="Rho GTPase-activating protein 1"
FT                   /id="PRO_0000422716"
FT   DOMAIN          117..130
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          162..342
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          354..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   466 AA;  51991 MW;  5A727A2E64C0C308 CRC64;
     MTEVLHFPSS PSASHSSSSS SSSPSPSSLS YASRSNATLL ISSDHNRRNP VARFDQDVDF
     HASIEEQDLR RRSSTDGGEE DDGGEDQISL LALLVAIFRR SLISCKSNRR ELCSMEIGWP
     TNVRHVAHVT FDRFNGFLGL PVEFEPEVPR RAPSASATVF GVSTESMQLS YDSRGNCVPT
     ILLLMQNCLY SQGGLQAEGI FRLTAENSEE EAVREQLNRG FIPERIDVHC LAGLIKAWFR
     ELPTSVLDSL SPEQVMQCQT EEENVELVRL LPPTEAALLD WAINLMADVV QYEHLNKMNS
     RNIAMVFAPN MTQMDDPLTA LMYAVQVMNF LKTLIEKTLR ERQDSVVEQA HAFPLEPSDE
     SGHQSPSQSL AFNTSEQSEE TQSDNIENAE NQSSSSEISD ELTLENNACE QRETDFGKYR
     TGRLSDSSQQ VVLNLDPPAQ WPVGRTKGLT NLSRVGSRVE RTEAWR