RGD2_YEAST
ID RGD2_YEAST Reviewed; 714 AA.
AC P43556; D6VTI3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Rho-GTPase-activating protein RGD2;
GN Name=RGD2; OrderedLocusNames=YFL047W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND INTERACTION WITH CDC42 AND RHO5.
RX PubMed=11591390; DOI=10.1016/s0014-5793(01)02906-4;
RA Roumanie O., Weinachter C., Larrieu I., Crouzet M., Doignon F.;
RT "Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins
RT from Saccharomyces cerevisiae.";
RL FEBS Lett. 506:149-156(2001).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Acts in signal transduction. Activates CDC42 and RHO5.
CC {ECO:0000269|PubMed:11591390}.
CC -!- SUBUNIT: Interacts with CDC42 and RHO5. {ECO:0000269|PubMed:11591390}.
CC -!- MISCELLANEOUS: Present with 1750 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; D50617; BAA09194.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12393.1; -; Genomic_DNA.
DR PIR; S56208; S56208.
DR RefSeq; NP_428268.1; NM_001179920.1.
DR AlphaFoldDB; P43556; -.
DR SMR; P43556; -.
DR BioGRID; 31100; 72.
DR DIP; DIP-4958N; -.
DR IntAct; P43556; 23.
DR MINT; P43556; -.
DR STRING; 4932.YFL047W; -.
DR iPTMnet; P43556; -.
DR MaxQB; P43556; -.
DR PaxDb; P43556; -.
DR PRIDE; P43556; -.
DR EnsemblFungi; YFL047W_mRNA; YFL047W; YFL047W.
DR GeneID; 850497; -.
DR KEGG; sce:YFL047W; -.
DR SGD; S000001847; RGD2.
DR VEuPathDB; FungiDB:YFL047W; -.
DR eggNOG; ENOG502QQWB; Eukaryota.
DR HOGENOM; CLU_008201_1_0_1; -.
DR InParanoid; P43556; -.
DR OMA; KRKTWIY; -.
DR BioCyc; YEAST:G3O-30418-MON; -.
DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P43556; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43556; protein.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000935; C:division septum; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:SGD.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 2.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 2.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; GTPase activation; Reference proteome.
FT CHAIN 1..714
FT /note="Rho-GTPase-activating protein RGD2"
FT /id="PRO_0000097318"
FT DOMAIN 2..441
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 218..298
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 475..704
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
SQ SEQUENCE 714 AA; 82209 MW; 52CF174C5F650157 CRC64;
MLSFCDYFWS EDLVSGLDVL FDRLYHGCEQ CDLFIQLFAS RMQFEVSHGR QLFGIEAGMD
NLKAVQEDED EGVTVSRALR GILQEMSQEG THHLTIASNI ESLVLQPFSK WCIEHRERIQ
YSEKTLLTNV NNFRKSKKYV GKLEKEYFNK CRQLEEFKRT HFNEDELANA MKSLKIQNKY
EEDVAREKDH RFFNRIAGID FDYKTMKETL QLLLTKLPKT DYKLPLISYS LSNTNNGGEI
TKFLLDHMSL KDIDQAETFG QDLLNLGFLK YCNGVGNTFV NSKKFQYQWK NTAYMFANVP
MPGSEEPTTG ESLISRFNNW DGSSAKEIIQ SKIGNDQGAA KIQAPHISDN ERTLFRMMDA
LAASDKKYYQ ECFKMDALRC SVEELLIDHL SFMEKCESDR LNAIKKATLD FCSTLGNKIS
SLRLCIDKML TLENDIDPTA DLLQLLVKYK TGSFKPQAIV YNNYYNPGSF QNFGVDLETR
CRLDKKVVPL IISSIFSYMD KIYPDLPNDK VRTSIWTDSV KLSLTHQLRN LLNKQQFHNE
GEIFDILSTS KLEPSTIASV VKIYLLELPD PLIPNDVSDI LRVLYLDYPP LVETALQNST
SSPENQQDDD NEEGFDTKRI RGLYTTLSSL SKPHIATLDA ITTHFYRLIK ILKMGENGNE
VADEFTVSIS QEFANCIIQS KITDDNEIGF KIFYDLLTHK KQIFHELKRQ NSKN
