FIG2_YEAST
ID FIG2_YEAST Reviewed; 1609 AA.
AC P25653; D6VR89;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Factor-induced gene 2 protein;
DE AltName: Full=Cell wall adhesin FIG2;
DE Flags: Precursor;
GN Name=FIG2; OrderedLocusNames=YCR089W; ORFNames=YCR1102, YCR89W;
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=1523889; DOI=10.1002/yea.320080708;
RA Wilson C., Grisanti P., Frontali L.;
RT "The complete sequence of a 6146 bp fragment of Saccharomyces cerevisiae
RT chromosome III contains two new open reading frames.";
RL Yeast 8:569-575(1992).
RN [2]
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 [3]
RP SEQUENCE REVISION TO 745 AND 1036.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9023939; DOI=10.1128/aem.63.2.615-620.1997;
RA Van der Vaart J.M., te Biesebeke R., Chapman J.W., Toschka H.Y., Klis F.M.,
RA Verrips C.T.;
RT "Comparison of cell wall proteins of Saccharomyces cerevisiae as anchors
RT for cell surface expression of heterologous proteins.";
RL Appl. Environ. Microbiol. 63:615-620(1997).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=9456310; DOI=10.1083/jcb.140.3.461;
RA Erdman S., Lin L., Malczynski M., Snyder M.;
RT "Pheromone-regulated genes required for yeast mating differentiation.";
RL J. Cell Biol. 140:461-483(1998).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=11027318; DOI=10.1073/pnas.220420397;
RA Guo B., Styles C.A., Feng Q., Fink G.R.;
RT "A Saccharomyces gene family involved in invasive growth, cell-cell
RT adhesion, and mating.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12158-12163(2000).
RN [8]
RP FUNCTION.
RX PubMed=12455698; DOI=10.1128/ec.1.5.811-822.2002;
RA Zhang M., Bennett D., Erdman S.E.;
RT "Maintenance of mating cell integrity requires the adhesin Fig2p.";
RL Eukaryot. Cell 1:811-822(2002).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=12455701; DOI=10.1128/ec.1.5.843-845.2002;
RA Jue C.K., Lipke P.N.;
RT "Role of Fig2p in agglutination in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 1:843-845(2002).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
CC -!- FUNCTION: Required for efficient mating. Plays a role in maintenance of
CC cell wall integrity during mating. Important for mating cell projection
CC shape and conjugation bridge diameter. Plays a role in cell fusion and
CC nuclear migration. {ECO:0000269|PubMed:11027318,
CC ECO:0000269|PubMed:12455698, ECO:0000269|PubMed:12455701,
CC ECO:0000269|PubMed:9456310}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:11027318,
CC ECO:0000269|PubMed:9023939, ECO:0000269|PubMed:9456310}. Membrane
CC {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Note=Periphery
CC of the mating cells. Localized to the mating projection.
CC -!- INDUCTION: By mating pheromones. By cells of the opposite mating type.
CC {ECO:0000269|PubMed:11027318, ECO:0000269|PubMed:12455701,
CC ECO:0000269|PubMed:9456310}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59720; CAA42254.2; -; Genomic_DNA.
DR EMBL; BK006937; DAA07558.1; -; Genomic_DNA.
DR PIR; S25345; S25345.
DR RefSeq; NP_010013.2; NM_001178795.1.
DR AlphaFoldDB; P25653; -.
DR BioGRID; 31061; 83.
DR IntAct; P25653; 1.
DR MINT; P25653; -.
DR STRING; 4932.YCR089W; -.
DR PaxDb; P25653; -.
DR PRIDE; P25653; -.
DR EnsemblFungi; YCR089W_mRNA; YCR089W; YCR089W.
DR GeneID; 850451; -.
DR KEGG; sce:YCR089W; -.
DR SGD; S000000685; FIG2.
DR VEuPathDB; FungiDB:YCR089W; -.
DR eggNOG; ENOG502S8X9; Eukaryota.
DR HOGENOM; CLU_244733_0_0_1; -.
DR InParanoid; P25653; -.
DR OMA; KTLYAFA; -.
DR BioCyc; YEAST:G3O-29383-MON; -.
DR PRO; PR:P25653; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25653; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:UniProtKB.
DR GO; GO:0005937; C:mating projection; IDA:SGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0000753; P:cell morphogenesis involved in conjugation with cellular fusion; IMP:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000755; P:cytogamy; IMP:UniProtKB.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR InterPro; IPR025928; Flocculin_t3_rpt.
DR Pfam; PF13928; Flocculin_t3; 5.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell shape; Cell wall; Cell wall biogenesis/degradation;
KW Conjugation; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Pheromone response; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1588
FT /note="Factor-induced gene 2 protein"
FT /id="PRO_0000021264"
FT PROPEP 1589..1609
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372452"
FT REGION 129..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1588
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1079
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1609 AA; 166036 MW; B9B6E08F98996B54 CRC64;
MNSFASLGLI YSVVNLLTRV EAQIVFYQNS STSLPVPTLV STSIADFHES SSTGEVQYSS
SYSYVQPSID SFTSSSFLTS FEAPTETSSS YAVSSSLITS DTFSSYSDIF DEETSSLIST
SAASSEKASS TLSSTAQPHR TSHSSSSFEL PVTAPSSSSL PSSTSLTFTS VNPSQSWTSF
NSEKSSALSS TIDFTSSEIS GSTSPKSLES FDTTGTITSS YSPSPSSKNS NQTSLLSPLE
PLSSSSGDLI LSSTIQATTN DQTSKTIPTL VDATSSLPPT LRSSSMAPTS GSDSISHNFT
SPPSKTSGNY DVLTSNSIDP SLFTTTSEYS STQLSSLNRA SKSETVNFTA SIASTPFGTD
SATSLIDPIS SVGSTASSFV GISTANFSTQ GNSNYVPEST ASGSSQYQDW SSSSLPLSQT
TWVVINTTNT QGSVTSTTSP AYVSTATKTV DGVITEYVTW CPLTQTKSQA IGVSSSISSV
PQASSFSGSS ILSSNSSTLA ASNNVPESTA SGSSQYQDWS SSSLPLSQTT WVVINTTNTQ
GSVTSTTSPA YVSTATKTVD GVITEYVTWC PLTQTKSQAI GISSSTISAT QTSKPSSILT
LGISTLQLSD ATFKGTETIN THLMTESTSI TEPTYFSGTS DSFYLCTSEV NLASSLSSYP
NFSSSEGSTA TITNSTVTFG STSKYPSTSV SNPTEASQHV SSSVNSLTDF TSNSTETIAV
ISNIHKTSSN KDYSLTTTQL KTSGMQTLVL STVTTTVNGA ATEYTTWCPA SSIAYTTSIS
YKTLVLTTEV CSHSECTPTV ITSVTATSST IPLLSTSSST VLSSTVSEGA KNPAASEVTI
NTQVSATSEA TSTSTQVSAT SATATASESS TTSQVSTASE TISTLGTQNF TTTGSLLFPA
LSTEMINTTV VSRKTLIIST EVCSHSKCVP TVITEVVTSK GTPSNGHSSQ TLQTEAVEVT
LSSHQTVTMS TEVCSNSICT PTVITSVQMR STPFPYLTSS TSSSSLASTK KSSLEASSEM
STFSVSTQSL PLAFTSSEKR STTSVSQWSN TVLTNTIMSS SSNVISTNEK PSSTTSPYNF
SSGYSLPSSS TPSQYSLSTA TTTINGIKTV YTTWCPLAEK STVAASSQSS RSVDRFVSSS
KPSSSLSQTS IQYTLSTATT TISGLKTVYT TWCPLTSKST LGATTQTSST AKVRITSASS
ATSTSISLST STESESSSGY LSKGVCSGTE CTQDVPTQSS SPASTLAYSP SVSTSSSSSF
STTTASTLTS THTSVPLLPS SSSISASSPS STSLLSTSLP SPAFTSSTLP TATAVSSSTF
IASSLPLSSK SSLSLSPVSS SILMSQFSSS SSSSSSLASL PSLSISPTVD TVSVLQPTTS
IATLTCTDSQ CQQEVSTICN GSNCDDVTST ATTPPSTVTD TMTCTGSECQ KTTSSSCDGY
SCKVSETYKS SATISACSGE GCQASATSEL NSQYVTMTSV ITPSAITTTS VEVHSTESTI
SITTVKPVTY TSSDTNGELI TITSSSQTVI PSVTTIITRT KVAITSAPKP TTTTYVEQRL
SSSGIATSFV AAASSTWITT PIVSTYAGSA SKFLCSKFFM IMVMVINFI
