GEF2_SCHPO
ID GEF2_SCHPO Reviewed; 1101 AA.
AC Q09733;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Rho guanine nucleotide exchange factor gef2;
GN Name=gef2; ORFNames=SPAC31A2.16;
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.
RX PubMed=14637153; DOI=10.1016/j.bbrc.2003.10.140;
RA Iwaki N., Karatsu K., Miyamoto M.;
RT "Role of guanine nucleotide exchange factors for Rho family GTPases in the
RT regulation of cell morphology and actin cytoskeleton in fission yeast.";
RL Biochem. Biophys. Res. Commun. 312:414-420(2003).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736 AND SER-977, 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: Has a role in the control of cell polarity and cytokinesis.
CC Involved in bipolar growth and septum formation.
CC {ECO:0000269|PubMed:14637153}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:16823372}. Note=Septum.
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DR EMBL; CU329670; CAA90474.1; -; Genomic_DNA.
DR PIR; T38614; S58108.
DR RefSeq; NP_592928.1; NM_001018329.2.
DR AlphaFoldDB; Q09733; -.
DR SMR; Q09733; -.
DR BioGRID; 279599; 17.
DR DIP; DIP-59762N; -.
DR IntAct; Q09733; 1.
DR STRING; 4896.SPAC31A2.16.1; -.
DR iPTMnet; Q09733; -.
DR MaxQB; Q09733; -.
DR PaxDb; Q09733; -.
DR PRIDE; Q09733; -.
DR EnsemblFungi; SPAC31A2.16.1; SPAC31A2.16.1:pep; SPAC31A2.16.
DR GeneID; 2543168; -.
DR KEGG; spo:SPAC31A2.16; -.
DR PomBase; SPAC31A2.16; gef2.
DR VEuPathDB; FungiDB:SPAC31A2.16; -.
DR eggNOG; ENOG502QVFV; Eukaryota.
DR HOGENOM; CLU_283307_0_0_1; -.
DR InParanoid; Q09733; -.
DR OMA; MRTESTY; -.
DR PRO; PR:Q09733; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0071341; C:medial cortical node; 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:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IGI:PomBase.
DR GO; GO:1902408; P:mitotic cytokinesis, site selection; IGI:PomBase.
DR Gene3D; 1.20.900.10; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR032634; Gef2/Nod1_dom.
DR Pfam; PF17114; Nod1; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW Septation.
FT CHAIN 1..1101
FT /note="Rho guanine nucleotide exchange factor gef2"
FT /id="PRO_0000080989"
FT DOMAIN 230..428
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT REGION 203..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1101 AA; 126538 MW; B26C47589F76F50B CRC64;
MDVGTMGSRA ELLAISIQFG GLWVFRDLLQ MNPLFEQDHV FCTFNHPNMG LVLISFAKVD
GHILAAYALS KLGPDTFSIC YPFSSKLDAF AQTLDLEWQI ASMHKEAAAC VYEFLCVESV
CLHTGENWRE SVIEPEYASY IFDTINVFQS SSLTRELYSL GEPNGVREFV VDAIFDIKVD
NSWWEDPSNS YWKTVIGSRE MFEDSRKKTS SPSPSFASSK DAGTIPAIQK KKSLLIEMME
TESTYVERLR HLVNDYALPL RDLAKSSKKL LGLYELNTLF PPCLNKLIQL NSAFLDEFEA
IMSDLNFEDI DEKKFEEIDL RLACCFESHF FAFSQHYPRY LEQSNDFGNV LKMASKIPKF
VEFHDQVKLN ANMNVGLSQL IMEPVQRIPR YSLFLDQIIL LTQEGECQHT YVRSVEIIKN
IAEMPTVDAE ERSRIFAGLQ HIIPDLAPNM ISNSRNFIDC IDVTREFLKN GQLHLIPYTL
ILFNDRICLV QRRSKSSIAS TILDLRKQNP RNSYSKEKRA QYIGSNMNEA VELTRSMVEE
NTIFLISKYA SSPSFFNEYP ILKFRCDFEN VRTMDRFYQS FQKALSMNKS QPSCLSFSKL
NDFVVFFNNY SRFEYEKESK RSDIVCICTN DANVDKHKFL QDGNIVITFF QQDEDFHLSF
DSWLGVSLPT EAVIAKEDLR EACLNYLINI KRLLLCPFSN RNFSSLDLYS NLIQHLLSAN
SSPRKSRLSF GGRPGSPSKI SLSLNRFYNQ GGLSKSCATL PSQMYNLDHN NISQKSLKFN
THNTSKASAE KTVEHLEAFK GGFKYHTDLK NLLYPLSEKE KIEGDELYDN ILKETFNEEL
LSHYPPNIIY ATFQKYLSSF INRKFGVLLS SSFIQQLNTV ENLNLSFNST DAVYHLKKIL
QDLPESSLKI LENIFSIASD LLLRLPLKDQ CDFVTKQLAI ALAPSMFGSN AVELVYYLAY
HSDRIFGTVE ELPTPVSPAN SNNDKQLDES KFQAIAMKEM PERHPKEILP GQIEREAYED
LRRKYHLTLA RLAQMTRLNE DSKKSIPLLY DRFNHDLKLI KQSVQASLIR KQCELDTAKW
TLEEYESKLN AKEGCQTNIF I
