ID FUS1_YEAST Reviewed; 512 AA.
AC P11710; D6VQY8;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
DT 02-OCT-2024, entry version 185.
DE RecName: Full=Nuclear fusion protein FUS1;
GN Name=FUS1; OrderedLocusNames=YCL027W; ORFNames=YCL27W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3302672; DOI=10.1128/mcb.7.7.2316-2328.1987;
RA Trueheart J., Boeke J.D., Fink G.R.;
RT "Two genes required for cell fusion during yeast conjugation: evidence for
RT a pheromone-induced surface protein.";
RL Mol. Cell. Biol. 7:2316-2328(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3313002; DOI=10.1128/mcb.7.8.2680-2690.1987;
RA McCaffrey G., Clay F.J., Kelsay K., Sprague G.F. Jr.;
RT "Identification and regulation of a gene required for cell fusion during
RT mating of the yeast Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 7:2680-2690(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [4]
RP SEQUENCE REVISION TO 130; 482 AND 485.
RA Mewes H.-W.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP GLYCOSYLATION.
RX PubMed=2690078; DOI=10.1073/pnas.86.24.9916;
RA Trueheart J., Fink G.R.;
RT "The yeast cell fusion protein FUS1 is O-glycosylated and spans the plasma
RT membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9916-9920(1989).
RN [7]
RP FUNCTION, AND INTERACTION WITH SHO1.
RX PubMed=15020407; DOI=10.1534/genetics.166.1.67;
RA Nelson B., Parsons A.B., Evangelista M., Schaefer K., Kennedy K.,
RA Ritchie S., Petryshen T.L., Boone C.;
RT "Fus1p interacts with components of the Hog1p mitogen-activated protein
RT kinase and Cdc42p morphogenesis signaling pathways to control cell fusion
RT during yeast mating.";
RL Genetics 166:67-77(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178; SER-190; SER-256;
RP THR-281 AND THR-424, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
CC -!- FUNCTION: Required for cell fusion. Negatively regulates Sho1p
CC signaling to ensure efficient cell fusion.
CC {ECO:0000269|PubMed:15020407}.
CC -!- FUNCTION: Interacts with SHO1. {ECO:0000269|PubMed:15020407}.
CC -!- INTERACTION:
CC P11710; P40450: BNR1; NbExp=5; IntAct=EBI-7179, EBI-3711;
CC P11710; Q12753: HAA1; NbExp=3; IntAct=EBI-7179, EBI-8118;
CC P11710; P40091: PEA2; NbExp=5; IntAct=EBI-7179, EBI-13106;
CC P11710; P40073: SHO1; NbExp=7; IntAct=EBI-7179, EBI-18140;
CC P11710; P32917: STE5; NbExp=2; IntAct=EBI-7179, EBI-18373;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: FUS1 remains essentially unexpressed in vegetative cells,
CC but is strongly induced by incubation of haploid cells with the
CC appropriate mating pheromone.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:2690078}.
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DR EMBL; M17199; AAA34612.1; -; Genomic_DNA.
DR EMBL; M16717; AAA34616.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42358.2; -; Genomic_DNA.
DR EMBL; BK006937; DAA07457.1; -; Genomic_DNA.
DR PIR; S19354; S19354.
DR RefSeq; NP_009903.2; NM_001178672.1.
DR AlphaFoldDB; P11710; -.
DR SMR; P11710; -.
DR BioGRID; 30956; 89.
DR DIP; DIP-670N; -.
DR IntAct; P11710; 49.
DR MINT; P11710; -.
DR STRING; 4932.YCL027W; -.
DR GlyGen; P11710; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P11710; -.
DR PaxDb; 4932-YCL027W; -.
DR PeptideAtlas; P11710; -.
DR EnsemblFungi; YCL027W_mRNA; YCL027W; YCL027W.
DR GeneID; 850330; -.
DR KEGG; sce:YCL027W; -.
DR AGR; SGD:S000000532; -.
DR SGD; S000000532; FUS1.
DR VEuPathDB; FungiDB:YCL027W; -.
DR eggNOG; ENOG502QVI6; Eukaryota.
DR HOGENOM; CLU_040701_0_0_1; -.
DR InParanoid; P11710; -.
DR OMA; HTDGWCL; -.
DR OrthoDB; 2038551at2759; -.
DR BioCyc; YEAST:G3O-29288-MONOMER; -.
DR BioGRID-ORCS; 850330; 4 hits in 10 CRISPR screens.
DR PRO; PR:P11710; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P11710; protein.
DR GO; GO:0005938; C:cell cortex; IEA:GOC.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0000755; P:cytogamy; IMP:SGD.
DR GO; GO:0032065; P:maintenance of protein location in cell cortex; IMP:SGD.
DR CDD; cd11854; SH3_Fus1p; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035521; Fus1_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; SH3 domain;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..512
FT /note="Nuclear fusion protein FUS1"
FT /id="PRO_0000087384"
FT TRANSMEM 72..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 436..512
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 97..512
FT /note="Hydrophilic"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 424
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
SQ SEQUENCE 512 AA; 57779 MW; 705241556DAD5D1C CRC64;
MVATIMQTTT TVLTTVAAMS TTLASNYISS QASSSTSVTT VTTIATSIRS TPSNLLFSNV
AAQPKSSSAS TIGLSIGLPI GIFCFGLLIL LCYFYLKRNS VSISNPPMSA TIPREEEYCR
RTNWFSRLFW QSKCEDQNSY SNRDIEKYND TQWTSGDNMS SKIQYKISKP IIPQHILTPK
KTVKNPYAWS GKNISLDPKV NEMEEEKVVD AFLYTKPPNI VHIESSMPSY NDLPSQKTVS
SKKTALKTSE KWSYESPLSR WFLRGSTYFK DYGLSKTSLK TPTGAPQLKQ MKMLSRISKG
YFNESDIMPD ERSPILEYNN TPLDANDSVN NLGNTTPDSQ ITSYRNNNID LITARPHSVI
YGTTAQQTLE TNFNDHHDCN KSTEKHELII PTPSKPLKKR KKRRQSKMYQ HLQHLSRSKP
LPLTPNSKYN GEASVQLGKT YTVIQDYEPR LTDEIRISLG EKVKILATHT DGWCLVEKCN
TQKGSIHVSV DDKRYLNEDR GIVPGDCLQE YD
//
