RGF1_SCHPO
ID RGF1_SCHPO Reviewed; 1334 AA.
AC Q9Y7U6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Rho1 guanine nucleotide exchange factor 1;
GN Name=rgf1; ORFNames=SPCC645.07;
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=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 [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16421249; DOI=10.1091/mbc.e05-10-0933;
RA Garcia P., Tajadura V., Garcia I., Sanchez Y.;
RT "Rgf1p is a specific Rho1-GEF that coordinates cell polarization with cell
RT wall biogenesis in fission yeast.";
RL Mol. Biol. Cell 17:1620-1631(2006).
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-381, 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 and Rho5 GDP-bound form into
CC GTP-bound form. Controls septum formation, cell wall synthesis and
CC localization of F-actin patches. Coordinates actin deposition with cell
CC wall biosynthesis during bipolar growth. {ECO:0000269|PubMed:16291723,
CC ECO:0000269|PubMed:16324155, ECO:0000269|PubMed:16421249}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16291723,
CC ECO:0000269|PubMed:16324155, ECO:0000269|PubMed:16421249,
CC ECO:0000269|PubMed:16823372}. Note=Septum. Localizes to cell tips
CC during interphase and the septum in mitotic cells.
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DR EMBL; CU329672; CAB39903.1; -; Genomic_DNA.
DR PIR; T41524; T41524.
DR RefSeq; NP_588116.1; NM_001023106.2.
DR AlphaFoldDB; Q9Y7U6; -.
DR SMR; Q9Y7U6; -.
DR BioGRID; 276139; 21.
DR STRING; 4896.SPCC645.07.1; -.
DR iPTMnet; Q9Y7U6; -.
DR MaxQB; Q9Y7U6; -.
DR PaxDb; Q9Y7U6; -.
DR PRIDE; Q9Y7U6; -.
DR EnsemblFungi; SPCC645.07.1; SPCC645.07.1:pep; SPCC645.07.
DR GeneID; 2539580; -.
DR KEGG; spo:SPCC645.07; -.
DR PomBase; SPCC645.07; rgf1.
DR VEuPathDB; FungiDB:SPCC645.07; -.
DR eggNOG; KOG4305; Eukaryota.
DR HOGENOM; CLU_001251_2_1_1; -.
DR InParanoid; Q9Y7U6; -.
DR OMA; PYFARFD; -.
DR PhylomeDB; Q9Y7U6; -.
DR PRO; PR:Q9Y7U6; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; 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:0009272; P:fungal-type cell wall biogenesis; IGI:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IC:GOC-OWL.
DR GO; GO:1903338; P:regulation of cell wall organization or biogenesis; EXP:PomBase.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.10.10; -; 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; IPR000591; DEP_dom.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041675; PH_5.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF15405; PH_5; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF46785; SSF46785; 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; Cytoplasm; Guanine-nucleotide releasing factor;
KW Phosphoprotein; Reference proteome; Septation.
FT CHAIN 1..1334
FT /note="Rho1 guanine nucleotide exchange factor 1"
FT /id="PRO_0000080970"
FT DOMAIN 621..808
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 843..973
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 995..1293
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1334 AA; 150114 MW; 637BAF224817FF66 CRC64;
MDYRHPNALG VNESSRAYEE IFGAPRKREP ARTVSTPAFM EPAPVSKKPL PPPTRRLPRK
PLPFRSTSLQ PPSSQPPAPP THQREASPVK NIEHSESFPS VFGTSNNHQI VPLTLKDGND
FGALYASLNT TPHFPQVSNH APNNSNSPSL TWHTSSGDDS NQNPFFVRRQ SQSSTSPVSD
SVDENLLSAV SSVTESVETN LHLDQNYPYG SPVRSSKNPF LSSNSRLPTD DSSHTVGSHS
FTSGTHPPIV SSNSAFTLPN AVTPAAQAPL IRSVSEYPAN VSPPAQSLQL PKSTSNPADL
HLSIASASSH KNIFSGLDVF SNVFHGPSTT LRDREHDMRN RSFDHSTLAH YEAVKQQRLG
VEPTARSFTL SSYKSRASGN SLINDRSSTT TPTFVNSEAS SPVHKNKRRR RIYAALLSRV
ASELLDRLQL GDITKDGLIY SNAFTGDHAV TVLMGIIHTS DRNLALLVGR SLDAQKFIHD
VTYDHRLRDS HREIYQLQGT GYRPFLRAND NASINNKNHH KELEDNESGT RISPSTLGDT
SFPNGIFTLL THCYSPTCAK DHPCYSISCP RRLEQQHRLF AKMRANTEQS SSLAFDDKEQ
KLWIHSVPQE IAYSVSDRER KRQEVICEVI YTERDFVKDL EYLRDYWIKP LWASSCIPER
KKEKFIRTVF LNALEVQAVN SKLAEALTKR QNYKPIVDNI ADIFLEHVPK FEPFIRYGAG
QLYGKYEFEK EKSSNPAFAK FVSDVERLKE SRKLELNGYL TKPTTRLARY PLLLEAVLKY
TDEGNPDKQD IPKVINIVRG FLSRLNVESG KAENKFNLFH LNQQLVFKPG EHYDLHLLDA
NRQLIFKGPL KKRSAGSTSS ESASDVTLFL FDHALLIVKP KTINKRELLK VFQRPIPLLL
LQLFLVDDNG LRIPYSSKQQ LAAVSKAANG KPPSRFYPFS LQLLGRRGYE ITLYATTEVS
RDKWLEHIDN QQTLLQHRNQ WFESVTICSN FFVGDNKVNA IGVYDSGRRL LYGTDTGVYV
SLRKANSPLQ FKPVRALNIP NISQLEVIEE YSLLLLLSDK VLYSYPLEMI DADTTQAPKK
ARKVSGHTTF FRVGICLGKV LVCAVKSSVL SATIKVFEPV TNYSKTRNMP SLKKFLTVNQ
DPLRIVKELY IPTESTSVHF LKNKLCVGCT RGFEVVSLDN LETQSLLDPA DTSLEFVEKK
ENVKPIAIYR MNGGEFLLCY SQFAFYVNRD GWRSRPTWFV VWEGSPQNFA LSYPYILAFE
PTFIEIRHVE TSELIHVISG RNIRLLADGR GKLGDGGEIF YACDQRGENC ETSVVCSLRL
TSAAAHAKEQ HVDK
