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   27-MAR-2024, entry version 158.
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}.
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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; 84.
DR   IntAct; P25653; 1.
DR   MINT; P25653; -.
DR   STRING; 4932.YCR089W; -.
DR   GlyCosmos; P25653; 15 sites, No reported glycans.
DR   GlyGen; P25653; 15 sites.
DR   PaxDb; 4932-YCR089W; -.
DR   EnsemblFungi; YCR089W_mRNA; YCR089W; YCR089W.
DR   GeneID; 850451; -.
DR   KEGG; sce:YCR089W; -.
DR   AGR; SGD:S000000685; -.
DR   SGD; S000000685; FIG2.
DR   VEuPathDB; FungiDB:YCR089W; -.
DR   eggNOG; ENOG502S8X9; Eukaryota.
DR   HOGENOM; CLU_244733_0_0_1; -.
DR   InParanoid; P25653; -.
DR   OMA; PKIPEHA; -.
DR   OrthoDB; 2040108at2759; -.
DR   BioCyc; YEAST:G3O-29383-MONOMER; -.
DR   BioGRID-ORCS; 850451; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P25653; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25653; Protein.
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:0098552; C:side of membrane; IEA:UniProtKB-KW.
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
//