ID   FUS1_SCHPO              Reviewed;        1372 AA.
AC   Q10719;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 145.
DE   RecName: Full=Cell fusion protein fus1;
GN   Name=fus1; ORFNames=SPAC20G4.02c;
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 [GENOMIC DNA].
RC   STRAIN=EG355;
RX   PubMed=7791776; DOI=10.1128/mcb.15.7.3697;
RA   Petersen J., Weilguny D., Egel R., Nielsen O.;
RT   "Characterization of fus1 of Schizosaccharomyces pombe: a developmentally
RT   controlled function needed for conjugation.";
RL   Mol. Cell. Biol. 15:3697-3707(1995).
RN   [2]
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).
CC   -!- FUNCTION: Required for cell fusion. It associates with the pre-zygotic
CC       projection tips in conjugating cells.
CC   -!- SUBUNIT: Interacts with actin at the FH2 domain. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By nitrogen starvation and by a pheromone signal in both P
CC       and M cell types. Essentially unexpressed in vegetative cells.
CC   -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L37838; AAA99003.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB11252.1; -; Genomic_DNA.
DR   PIR; T43296; T43296.
DR   RefSeq; NP_594737.1; NM_001020165.2.
DR   AlphaFoldDB; Q10719; -.
DR   SMR; Q10719; -.
DR   BioGRID; 278235; 42.
DR   STRING; 4896.SPAC20G4.02c.1; -.
DR   PaxDb; Q10719; -.
DR   EnsemblFungi; SPAC20G4.02c.1; SPAC20G4.02c.1:pep; SPAC20G4.02c.
DR   GeneID; 2541741; -.
DR   KEGG; spo:SPAC20G4.02c; -.
DR   PomBase; SPAC20G4.02c; fus1.
DR   VEuPathDB; FungiDB:SPAC20G4.02c; -.
DR   eggNOG; KOG1922; Eukaryota.
DR   HOGENOM; CLU_001313_1_0_1; -.
DR   InParanoid; Q10719; -.
DR   OMA; KENHKER; -.
DR   PhylomeDB; Q10719; -.
DR   PRO; PR:Q10719; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005937; C:mating projection; IDA:PomBase.
DR   GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR   GO; GO:0003779; F:actin binding; ISM:PomBase.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:1904600; P:actin fusion focus assembly; IMP:PomBase.
DR   GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR   GO; GO:0000755; P:cytogamy; IMP:PomBase.
DR   Gene3D; 1.20.58.2220; -; 1.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   InterPro; IPR010473; GTPase-bd.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM01140; Drf_GBD; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome; SH3-binding; Stress response.
FT   CHAIN           1..1372
FT                   /note="Cell fusion protein fus1"
FT                   /id="PRO_0000194902"
FT   DOMAIN          104..522
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT   DOMAIN          868..1278
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   MOTIF           802..817
FT                   /note="SH3-binding"
SQ   SEQUENCE   1372 AA;  157074 MW;  52349B4E1B9D6B98 CRC64;
     MMTASFKGIR ISKPIVKEIS SFGSLTNIDL HTDPYEKVEA KALSRSRLKN QSVKKTDLRI
     TNDYSSLFVS IENKKNTIPD IHCNNLSKRP VGFTDSYVPG EALLCPDDPN LVNELFDDVL
     KRLREEKSDS GEQFHWDANV TLSQENKWSF ITGYLSRNDK FLKISSNDSE LNVKASVISY
     IEKLSCTPLK LKYVESLAVA LRTESVTWVR YFLLMGGHIV LAKILQAIHE KKHLKSPDIT
     LEIAILKSMR CIIGQKIGTD FYLSNKYPID SVVHCLLSTK LLVRKLAAEL LTFLCYSEKP
     NGINAIMKCM KNFANLKVES MNVFDLWLSQ WKRTLLEKVV TEEKKVLEEA ALHDKITIEY
     IISQMLLINA FLENIPSKTA LLQFKESLRI GNFKSILLIL KKINDEGVLK QLEKCVKLVS
     LDTANEKHFL KHTPNSAAHQ SLLNTNMFND ANFEFMVKEH IKNFLKLLKE HNNPVRIIKL
     LDCLVLTLQA DKGNGNSNND IDCFYKELKI GNEQGNNAPG YSSVTSGYGT TNSKKVVASY
     DNTDDNEYSV SKSELYATGD TNNTTNQGYE NSERKYVESS KYETDLKNIF DCLCLLFPSE
     FDPQSSFSAE KIFSKLKHLL TRTRDSYISE DTKILRLLNR SSSKLQDRDQ EYLISKNNVN
     GNGNRDWVQP VNTTSSVSAF ASPRIKPKLL FQPNQDEKLK LCKLDLAKAN SITLKSEPSS
     AVSTHSFEVH LSMPGTQIKS ANLAEKMETS KHKVFNPKRI DVVSDLPLDY RKSYYGRFSI
     TDTKRFSKIE NMRIKEVIDG NPFKAPPPAP LPPPAPPLPT AMSSLQKFEK NDSQIFRKTI
     IIPENISIDD IFKFCSGSES EVYASKIPGE LCNPSKRLKQ LHWKRLEVPF EKTLWNIVVA
     DPYLLTLKLT AEGIFKQLED CYPLREVTVS NKKVKEYTGF MPVDLQQMVS IRLHRFNSLT
     PIEIAKKFFH CDHDIMELVD FFNDRKFFRQ EGLKKQLKPY MSSRNEEVME VSEKLLELSR
     FDQIYTLIVV DIDTYYEKRM AALKIKSFLA NNFRDFRRQI RKLHCASLEL KSSLHFKYFL
     NLVLHIGNFM NDAPRRAKGY RLESLLRASM IKNDKTGLTL LHTIEKIVRT HFPQLEAFLV
     DLKAIPEISR FNLEQLEQDC NDICERMKNV EKDFSNEGIF SNHKALHPDD HICEVMVPWI
     PSGKSMVDEL NSDITELKTT LKTTLLMYGE NPDEPTSSAR FFNNLNEIIL EYKKASTVNQ
     KMEKEEELAF LRLQALKASV KSNNAENSGS SKNEEVSATM ENLISQLQKG LCDDSLSNKT
     DCTESSKQTI ETLMNYENDK QTLEGSNKKR QTVVLKAECM LKQLENNNEL KR