RGF2_SCHPO
ID RGF2_SCHPO Reviewed; 1158 AA.
AC Q9UTR5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Rho1 guanine nucleotide exchange factor 2;
GN Name=rgf2; ORFNames=SPAC1006.06;
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746 AND SER-747, AND
RP IDENTIFICATION BY 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. {ECO:0000269|PubMed:16291723,
CC ECO:0000269|PubMed:16324155}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16291723,
CC ECO:0000269|PubMed:16324155, ECO:0000269|PubMed:16823372}. Note=Septum.
CC Localizes to cell tips during interphase and the septum in mitotic
CC cells.
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DR EMBL; CU329670; CAB60236.1; -; Genomic_DNA.
DR PIR; T50454; T50454.
DR RefSeq; NP_594853.1; NM_001020282.2.
DR AlphaFoldDB; Q9UTR5; -.
DR SMR; Q9UTR5; -.
DR BioGRID; 279393; 12.
DR STRING; 4896.SPAC1006.06.1; -.
DR iPTMnet; Q9UTR5; -.
DR MaxQB; Q9UTR5; -.
DR PaxDb; Q9UTR5; -.
DR PRIDE; Q9UTR5; -.
DR EnsemblFungi; SPAC1006.06.1; SPAC1006.06.1:pep; SPAC1006.06.
DR GeneID; 2542953; -.
DR KEGG; spo:SPAC1006.06; -.
DR PomBase; SPAC1006.06; rgf2.
DR VEuPathDB; FungiDB:SPAC1006.06; -.
DR eggNOG; KOG4305; Eukaryota.
DR HOGENOM; CLU_001251_2_1_1; -.
DR InParanoid; Q9UTR5; -.
DR OMA; GEGWPIT; -.
DR PhylomeDB; Q9UTR5; -.
DR PRO; PR:Q9UTR5; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0030428; C:cell septum; IDA:BHF-UCL.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:PomBase.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:PomBase.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:BHF-UCL.
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:0060622; P:regulation of ascospore wall beta-glucan biosynthetic process; IMP:BHF-UCL.
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; 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; SM00325; RhoGEF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50010; DH_2; 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..1158
FT /note="Rho1 guanine nucleotide exchange factor 2"
FT /id="PRO_0000080971"
FT DOMAIN 447..634
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 670..805
FT /note="PH"
FT DOMAIN 825..1120
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 42..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1158 AA; 130879 MW; 6FFE8244710D33B1 CRC64;
MLRNGAQNGN INSESHESFG KAAKGFRIFS SFSSSQKLFQ RRSSGSITHS PTALSSTTSL
NENDGNHFRP ASSLSFSPSS LSRKDSGPGD GLEVNKKNNF YRRSSSTDDF GISHARSRKE
IQSLGRPHTR QSFSVSDVSN GSSYPNIRKN SVHVNAPMPS FPEGSTAVLL KHHSGSKSAS
AISNIAPSHS NSTSSRRPYI HPAFLSQVAV EFRKRLNIGD RVKDGLLYKD AFLGSEAVDV
LMHIVRTTDR NLALLLGRAL DSQKMFHDVT YSHRLRDSLK EVYQYRRIIS PPPGLSSMDS
NGSSIENNFL YTKRRANTSD SFDSVLSDSS TTPTISSSVQ VNSLAFITSS LSAITKEPEA
PETEYNPHGV FTLLTECYSS TCSRNRLCYS ISCPRRLEQQ ARLHLKVQPV LSGGSTSITD
KQEEDHRLWS ENVPKQVVDQ IDVREWKRQE IIFEVIYTER DFVRDLEYIR DFWIKPLSTS
NVIPENNRQQ FIRCVFHNIM QIHAVNSRLS NALNRTQTLQ PVVNTIGDLF LDYVPKFEPF
IKYGANQAIA KFEFEREKST NRNFANYVHE VERLRESRKL ELNGYLTKPT TRLARYPLLL
SGVLKYTDKD NPDTENIPRV IEMIREFLTK LNYETGKTEN RLSLLQLNEQ LSCSPADRAK
LTLFDPSRLL IFKGVVKLKA SSYSNGDTEN DIHMFLLDNF LLLCKIKIQM KRRVHKLHLR
PLPLELLSIS YIEDSPSRGS LPRRPSSALL TNPISITKSN PPPVKAYGLQ LVFIGARGFS
ISLYLNTLIA RDQWKQHIEK QQDIIRKRHL VFESRGICCQ SWFTGNKLLC AVAYDAGRKL
LFGTYKGLYI SSRKSNNGSC LEPIFKLQLP NISQLDVIEE HNVLLLLAEK ILYELPLDAL
DSVEQINSKS LRRVTGHVSF VKTGFCMQRI LVCAVKSTVL NTTLRIYEAD RALKNKKTQS
LKKPFGNQAT LKIFTEVQMP MEALSVHFLK TKLCVGSFKG FDIISLENAV FQSLLNPADT
SFRFLEKRED IRPIAMFRLR GEFLLCYSDF AFFVNTNGWK SRQSWMINWE GQPQGCALCY
PYILAFEPDF IEIRNAETAE LVQIIMGQNI KLLTDGRGLI SEGGEILYST EPIPFSSGEN
PIVHSLILPP ANAAGPAL
