RGF3_SCHPO
ID RGF3_SCHPO Reviewed; 1275 AA.
AC Q9Y7U5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Rho1 guanine nucleotide exchange factor 3;
DE AltName: Full=Lethal at division protein 1;
GN Name=rgf3; Synonyms=lad1; ORFNames=SPCC645.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15546915; DOI=10.1242/jcs.01530;
RA Tajadura V., Garcia B., Garcia I., Garcia P., Sanchez Y.;
RT "Schizosaccharomyces pombe Rgf3p is a specific Rho1 GEF that regulates cell
RT wall beta-glucan biosynthesis through the GTPase Rho1p.";
RL J. Cell Sci. 117:6163-6174(2004).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16324155; DOI=10.1111/j.1365-2443.2005.00908.x;
RA Mutoh T., Nakano K., Mabuchi I.;
RT "Rho1-GEFs Rgf1 and Rgf2 are involved in formation of cell wall and septum,
RT while Rgf3 is involved in cytokinesis in fission yeast.";
RL Genes Cells 10:1189-1202(2005).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16291723; DOI=10.1242/jcs.02664;
RA Morrell-Falvey J.L., Ren L., Feoktistova A., Haese G.D., Gould K.L.;
RT "Cell wall remodeling at the fission yeast cell division site requires the
RT Rho-GEF Rgf3p.";
RL J. Cell Sci. 118:5563-5573(2005).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Stimulates the exchange of Rho1 GDP-bound form into GTP-bound
CC form. Regulates, via interaction and activation of Rho1, beta-1,3-
CC glucan biosynthesis and cell wall integrity during septation. Involved
CC in the regulation of contractile ring assembly.
CC {ECO:0000269|PubMed:15546915, ECO:0000269|PubMed:16291723,
CC ECO:0000269|PubMed:16324155}.
CC -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000269|PubMed:15546915,
CC ECO:0000269|PubMed:16291723, ECO:0000269|PubMed:16324155,
CC ECO:0000269|PubMed:16823372}. Note=Localizes to the outer area (150 nm)
CC of the contractile ring.
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DR EMBL; CU329672; CAB39902.1; -; Genomic_DNA.
DR PIR; T41523; T41523.
DR RefSeq; NP_588115.1; NM_001023105.2.
DR AlphaFoldDB; Q9Y7U5; -.
DR SMR; Q9Y7U5; -.
DR BioGRID; 276000; 20.
DR STRING; 4896.SPCC645.06c.1; -.
DR iPTMnet; Q9Y7U5; -.
DR MaxQB; Q9Y7U5; -.
DR PaxDb; Q9Y7U5; -.
DR PRIDE; Q9Y7U5; -.
DR EnsemblFungi; SPCC645.06c.1; SPCC645.06c.1:pep; SPCC645.06c.
DR GeneID; 2539437; -.
DR KEGG; spo:SPCC645.06c; -.
DR PomBase; SPCC645.06c; rgf3.
DR VEuPathDB; FungiDB:SPCC645.06c; -.
DR eggNOG; KOG4305; Eukaryota.
DR HOGENOM; CLU_001083_1_0_1; -.
DR InParanoid; Q9Y7U5; -.
DR OMA; LLPCYSF; -.
DR PhylomeDB; Q9Y7U5; -.
DR PRO; PR:Q9Y7U5; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:PomBase.
DR GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0090334; P:regulation of cell wall (1->3)-beta-D-glucan biosynthetic process; IMP:PomBase.
DR GO; GO:0140279; P:regulation of mitotic division septum assembly; IMP:PomBase.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041675; PH_5.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF15405; PH_5; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Guanine-nucleotide releasing factor;
KW Phosphoprotein; Reference proteome; Septation.
FT CHAIN 1..1275
FT /note="Rho1 guanine nucleotide exchange factor 3"
FT /id="PRO_0000080972"
FT DOMAIN 465..657
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 692..855
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 930..1239
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1275 AA; 144431 MW; E5B6CFA7780FD2FF CRC64;
MKLSNELFHR SSKDHGGKSR ICLDSSEDTY PPHSSSPPSF QKRLSFSDFS TTRLFSPPFL
SKRSNNSPHR FSYSPPQHPA SINSRRVASY TVQSSPSRTT YRQLPNEPQN SAAYTTYSSF
PNALFDDFSP NNPLDTDPFL TSPGNKQNTV DSFRPLPETP VSPGGSLVHP LPRPPLPSSV
SSHSSPYSTT SSTSLYSLYN DISLSCSPEP YLPLSPTRSP ARTPSPIRLY SSDALRPQSP
LSPSVEYLTP PNPYSLKSDI SSTRQLPKIP VQDYASGKIS SPLITRTHRR AQSETLFSSC
REPWLVGKLY KWCKEEVFTA LGGLVHEGVS RREVAQVMAT LFTIHIASME FLIAEIIAKN
ILGDWINYGL VEVINLEKLQ IAFTSNEPPS GSGVLPFLTN GGCYSYICRS RSCPSKYQCY
SCRCARNSSL EFTSLPGQSS DTWSIFWNIS SLNSLPSSLS KREIARQNNI HELICKESDY
VADLNTLAEL FRDGIVQQQD AIVPSNRVAD FIQSVFGNVE SIRQLHSRLF LPQLIMRERL
QGPVVSIIGD ILLEWIHAAK SSYINYAKQF PLADETYKLE CQRNTYFARW LAACRSDPRC
RRLDFQHFLQ RPTQRLQRYT LELDTILKHT EQSSWDFQLI TQAVKELRAT CEECDAVIAT
VLEANRIRDL SYQLLFKNHE SVNLELRDPE REFFFEGIVQ RRSDSRLDWL DIHLFLLDNY
LIMAKARKDK RTNASRYVVS KRPIPLDLLV LSPKMDDFQL KSNTNKFLGS LAGNLPQESL
TTKSKRKSKV NLELMFDATA EKNNENSMNS AVFEKSQLYP FTIRHLGAYT ASYTLYVESL
QLRKLWVEKI NVAKKRHSQK INIKNPFALK VVSDVAFQYP PSDLVNGNEP LNSFNEITLV
EGSSIDRALN EVAWKHPIVS EELLPEPIAY GDISCIAQFN DYEGHVSVLI ATSTGIFLGA
FGDSSDIRDW KKISSQRRVT QLGVVEEFDI LLELRDKTLY AHKLSRIIEM GLIESKIAVV
IGTPHAVSFF KIGKLSEGAS VKRERTLVFY KEGLGNTTTI ICCEPVIGLG HNYQKTYAFK
RKDVTSFRTL DDFHVTANCH SIDCFKYSIA LCHNKGIDVL RLDPKLAVGF PSPSVLNDTL
FRNRINNSKP LGVFRIHDPS LFACCYQFGA VFVNGEGSMV NKECWFDWIG KPNSVTSCHG
YLIAFNDEFV EIWNTRTRKL NQIIQGNDIK YYPSNSDWLA NGKYIMFGMV HPQYHDRHLI
LALNKAKTNS FIIED
