ID RGAP5_ARATH Reviewed; 331 AA.
AC Q6NKT5; Q9SGC6; Q9SJF6;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Rho GTPase-activating protein 5;
DE AltName: Full=Rho-type GTPase-activating protein 5;
GN Name=ROPGAP5; OrderedLocusNames=At1g08340; ORFNames=T27G7.4;
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=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 Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22984069; DOI=10.1126/science.1222597;
RA Oda Y., Fukuda H.;
RT "Initiation of cell wall pattern by a Rho- and microtubule-driven symmetry
RT breaking.";
RL Science 337:1333-1336(2012).
CC -!- FUNCTION: Acts as a GTPase activator for the Rac-type GTPase by
CC converting it to an inactive GDP-bound state. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22984069};
CC Peripheral membrane protein {ECO:0000305|PubMed:22984069}.
CC -!- TISSUE SPECIFICITY: Expressed in differentiating xylem cells.
CC {ECO:0000269|PubMed:22984069}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF18245.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF22885.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006932; AAF22885.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011438; AAF18245.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28278.1; -; Genomic_DNA.
DR EMBL; BT012608; AAT06427.1; -; mRNA.
DR EMBL; BT014961; AAT47812.1; -; mRNA.
DR EMBL; AK228173; BAF00129.1; -; mRNA.
DR PIR; B86217; B86217.
DR RefSeq; NP_172310.1; NM_100707.4.
DR AlphaFoldDB; Q6NKT5; -.
DR SMR; Q6NKT5; -.
DR STRING; 3702.Q6NKT5; -.
DR PaxDb; 3702-AT1G08340-1; -.
DR ProteomicsDB; 236999; -.
DR EnsemblPlants; AT1G08340.1; AT1G08340.1; AT1G08340.
DR GeneID; 837354; -.
DR Gramene; AT1G08340.1; AT1G08340.1; AT1G08340.
DR KEGG; ath:AT1G08340; -.
DR Araport; AT1G08340; -.
DR TAIR; AT1G08340; -.
DR eggNOG; KOG4270; Eukaryota.
DR HOGENOM; CLU_031591_2_0_1; -.
DR InParanoid; Q6NKT5; -.
DR OMA; VARCETE; -.
DR OrthoDB; 5480623at2759; -.
DR PhylomeDB; Q6NKT5; -.
DR PRO; PR:Q6NKT5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NKT5; baseline and differential.
DR Genevisible; Q6NKT5; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 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; MKIAA1688 PROTEIN; 1.
DR PANTHER; PTHR23177:SF57; RHO GTPASE-ACTIVATING PROTEIN 5; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; GTPase activation; Membrane; Reference proteome.
FT CHAIN 1..331
FT /note="Rho GTPase-activating protein 5"
FT /id="PRO_0000422720"
FT DOMAIN 3..16
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 48..225
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 227..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..280
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 331 AA; 36830 MW; 6A2D10122F3EF858 CRC64;
MDIGGPTNIR HVAHVTFDRF DGFLGLPSEF EPDVPRKAPS ASATVFGVST ESMQLSYDSR
GNCVPVILLL LQSRLYDQGG LQAEGVFRIT GENSEEEFVR EQLNKGIIPD GIDVHCLAGL
IKAWFRELPR GVLDPLPSEQ VMQCESDEDF VKVVRLLPQT EASLLNWAIN LMADVIQFEH
VNKMNSRNLA LVFAPNMSQM ADPLTALMYA VQVMKLLKSL TEKTVREREA SSSVVDRRCS
KEAEDGEKEK DNEEEEEDEE EEEEEEDEDE DEEEEGDGVY IIKEEEASEI IKVVADEHKS
GSIKSEFEGS SATDSKGDNG VVQPPICSSN P
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