AGA2_YEAST
ID AGA2_YEAST Reviewed; 87 AA.
AC P32781; D6VUA6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=A-agglutinin-binding subunit;
DE Flags: Precursor;
GN Name=AGA2; OrderedLocusNames=YGL032C;
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 [MRNA], AND FUNCTION.
RC STRAIN=ATCC 26786 / X2180-1A;
RX PubMed=1756718; DOI=10.1002/j.1460-2075.1991.tb04984.x;
RA Cappellaro C., Hauser K., Mrsa V., Watzele M., Watzele G., Gruber C.,
RA Tanner W.;
RT "Saccharomyces cerevisiae a- and alpha-agglutinin: characterization of
RT their molecular interaction.";
RL EMBO J. 10:4081-4088(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
RP SUBUNIT, AND MUTAGENESIS OF CYS-25 AND CYS-68.
RX PubMed=7957044; DOI=10.1002/j.1460-2075.1994.tb06799.x;
RA Cappellaro C., Baldermann C., Rachel R., Tanner W.;
RT "Mating type-specific cell-cell recognition of Saccharomyces cerevisiae:
RT cell wall attachment and active sites of a- and alpha-agglutinin.";
RL EMBO J. 13:4737-4744(1994).
RN [5]
RP INTERACTION WITH SAG1.
RX PubMed=11292808; DOI=10.1128/jb.183.9.2874-2880.2001;
RA Zhao H., Shen Z.M., Kahn P.C., Lipke P.N.;
RT "Interaction of alpha-agglutinin and a-agglutinin, Saccharomyces cerevisiae
RT sexual cell adhesion molecules.";
RL J. Bacteriol. 183:2874-2880(2001).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Receptor binding subunit of the a-agglutinin heterodimer.
CC S.cerevisiae a and alpha cells express the complementary cell surface
CC glycoproteins a-agglutinin and alpha-agglutinin, respectively, which
CC interact with one another to promote cellular aggregation during
CC mating. {ECO:0000269|PubMed:1756718}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked (Probable). Interacts with SAG1.
CC {ECO:0000269|PubMed:11292808, ECO:0000269|PubMed:7957044, ECO:0000305}.
CC -!- INTERACTION:
CC P32781; P32323: AGA1; NbExp=2; IntAct=EBI-2347, EBI-2340;
CC -!- MISCELLANEOUS: Present with 1160 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X62877; CAA44670.1; -; mRNA.
DR EMBL; Z72554; CAA96733.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08067.1; -; Genomic_DNA.
DR PIR; S18838; S18838.
DR RefSeq; NP_011483.3; NM_001180897.3.
DR AlphaFoldDB; P32781; -.
DR BioGRID; 33214; 52.
DR ComplexPortal; CPX-1838; a-agglutinin.
DR DIP; DIP-5451N; -.
DR IntAct; P32781; 1.
DR STRING; 4932.YGL032C; -.
DR MaxQB; P32781; -.
DR PaxDb; P32781; -.
DR PRIDE; P32781; -.
DR EnsemblFungi; YGL032C_mRNA; YGL032C; YGL032C.
DR GeneID; 852851; -.
DR KEGG; sce:YGL032C; -.
DR SGD; S000003000; AGA2.
DR VEuPathDB; FungiDB:YGL032C; -.
DR eggNOG; ENOG502SCZQ; Eukaryota.
DR HOGENOM; CLU_189322_0_0_1; -.
DR InParanoid; P32781; -.
DR OMA; GVFEYYK; -.
DR BioCyc; YEAST:G3O-30548-MON; -.
DR PRO; PR:P32781; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32781; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:SGD.
DR GO; GO:0000752; P:agglutination involved in conjugation with cellular fusion; IDA:SGD.
DR InterPro; IPR014404; Aga2.
DR Pfam; PF17366; AGA2; 1.
DR PIRSF; PIRSF002695; A-agglutinin; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Reference proteome; Signal.
FT SIGNAL 1..18
FT CHAIN 19..87
FT /note="A-agglutinin-binding subunit"
FT /id="PRO_0000020642"
FT CARBOHYD 22
FT /note="O-linked (Man...) threonine"
FT CARBOHYD 30
FT /note="O-linked (Man...) serine"
FT CARBOHYD 32
FT /note="O-linked (Man...) threonine"
FT CARBOHYD 39
FT /note="O-linked (Man...) serine"
FT CARBOHYD 63
FT /note="O-linked (Man...) threonine"
FT CARBOHYD 66
FT /note="O-linked (Man...) serine"
FT CARBOHYD 75
FT /note="O-linked (Man...) threonine"
FT DISULFID 25
FT /note="Interchain (with AGA1)"
FT /evidence="ECO:0000305"
FT DISULFID 68
FT /note="Interchain (with AGA1)"
FT /evidence="ECO:0000305"
FT MUTAGEN 25
FT /note="C->S: Abolishes agglutination; when associated with
FT S-68."
FT /evidence="ECO:0000269|PubMed:7957044"
FT MUTAGEN 68
FT /note="C->S: Abolishes agglutination; when associated with
FT S-25."
FT /evidence="ECO:0000269|PubMed:7957044"
SQ SEQUENCE 87 AA; 9464 MW; EA7DA943FAD743C3 CRC64;
MQLLRCFSIF SVIASVLAQE LTTICEQIPS PTLESTPYSL STTTILANGK AMQGVFEYYK
SVTFVSNCGS HPSTTSKGSP INTQYVF
