AGA1_YEAST
ID AGA1_YEAST Reviewed; 725 AA.
AC P32323; D6W1L9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=A-agglutinin anchorage subunit;
DE AltName: Full=A-agglutinin cell wall attachment subunit;
DE Flags: Precursor;
GN Name=AGA1; OrderedLocusNames=YNR044W; ORFNames=N3431;
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=2072914; DOI=10.1128/mcb.11.8.4196-4206.1991;
RA Roy A., Lu C.F., Marykwas D.L., Lipke P.N., Kurjan J.;
RT "The AGA1 product is involved in cell surface attachment of the
RT Saccharomyces cerevisiae cell adhesion glycoprotein a-agglutinin.";
RL Mol. Cell. Biol. 11:4196-4206(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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.
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 SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=11278672; DOI=10.1074/jbc.m010421200;
RA Shen Z.M., Wang L., Pike J., Jue C.K., Zhao H., de Nobel H., Kurjan J.,
RA Lipke P.N.;
RT "Delineation of functional regions within the subunits of the Saccharomyces
RT cerevisiae cell adhesion molecule a-agglutinin.";
RL J. Biol. Chem. 276:15768-15775(2001).
RN [6]
RP GPI-ANCHOR, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=14555493; DOI=10.1128/ec.2.5.1099-1114.2003;
RA Huang G., Zhang M., Erdman S.E.;
RT "Posttranslational modifications required for cell surface localization and
RT function of the fungal adhesin Aga1p.";
RL Eukaryot. Cell 2:1099-1114(2003).
RN [7]
RP REPEATS.
RX PubMed=16086015; DOI=10.1038/ng1618;
RA Verstrepen K.J., Jansen A., Lewitter F., Fink G.R.;
RT "Intragenic tandem repeats generate functional variability.";
RL Nat. Genet. 37:986-990(2005).
CC -!- FUNCTION: Cell wall anchoring 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.
CC -!- SUBUNIT: Heterodimer; disulfide-linked. {ECO:0000305|PubMed:11278672,
CC ECO:0000305|PubMed:7957044}.
CC -!- INTERACTION:
CC P32323; P32781: AGA2; NbExp=2; IntAct=EBI-2340, EBI-2347;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:14555493}. Membrane {ECO:0000269|PubMed:14555493};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:14555493}.
CC Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
CC -!- DOMAIN: The number of the intragenic tandem repeats varies between
CC different S.cerevisiae strains.
CC -!- PTM: Extensively O-glycosylated by PMT1 and PMT2.
CC {ECO:0000269|PubMed:14555493}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
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DR EMBL; M60590; AAA34382.1; -; Genomic_DNA.
DR EMBL; Z71659; CAA96325.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10585.1; -; Genomic_DNA.
DR PIR; A41258; A41258.
DR RefSeq; NP_014442.1; NM_001183221.1.
DR AlphaFoldDB; P32323; -.
DR BioGRID; 35869; 72.
DR ComplexPortal; CPX-1838; a-agglutinin.
DR IntAct; P32323; 2.
DR STRING; 4932.YNR044W; -.
DR PaxDb; P32323; -.
DR EnsemblFungi; YNR044W_mRNA; YNR044W; YNR044W.
DR GeneID; 855780; -.
DR KEGG; sce:YNR044W; -.
DR SGD; S000005327; AGA1.
DR VEuPathDB; FungiDB:YNR044W; -.
DR eggNOG; ENOG502THFQ; Eukaryota.
DR HOGENOM; CLU_399131_0_0_1; -.
DR InParanoid; P32323; -.
DR OMA; TPEQPPC; -.
DR BioCyc; YEAST:G3O-33351-MON; -.
DR PRO; PR:P32323; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P32323; 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:SGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IMP:SGD.
DR GO; GO:0000752; P:agglutination involved in conjugation with cellular fusion; IDA:ComplexPortal.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell wall; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Pheromone response; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..699
FT /note="A-agglutinin anchorage subunit"
FT /id="PRO_0000020641"
FT PROPEP 700..725
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000296627"
FT REPEAT 53..149
FT /note="1-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 182..188
FT /note="2-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 189..195
FT /note="2-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 196..202
FT /note="2-3"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 203..209
FT /note="2-4"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 210..216
FT /note="2-5"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 217..223
FT /note="2-6"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 224..230
FT /note="2-7"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 231..237
FT /note="2-8"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 238..244
FT /note="2-9"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 245..251
FT /note="2-10"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 252..258
FT /note="2-11"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 259..265
FT /note="2-12"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 266..272
FT /note="2-13"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 273..279
FT /note="2-14"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 280..286
FT /note="2-15"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 287..293
FT /note="2-16"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 294..300
FT /note="2-17"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 301..307
FT /note="2-18"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 395..493
FT /note="1-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REGION 53..493
FT /note="2 X approximate repeats"
FT REGION 168..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..307
FT /note="18 X approximate tandem repeats, Ser/Thr-rich"
FT REGION 335..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 699
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT DISULFID 133
FT /note="Interchain (with AGA2)"
FT /evidence="ECO:0000305|PubMed:11278672"
FT DISULFID 136
FT /note="Interchain (with AGA2)"
FT /evidence="ECO:0000305|PubMed:11278672"
SQ SEQUENCE 725 AA; 73354 MW; 70420C853B0B01F8 CRC64;
MTLSFAHFTY LFTILLGLTN IALASDPETI LVTITKTNDA NGVVTTTVSP ALVSTSTIVQ
AGTTTLYTTW CPLTVSTSSA AEISPSISYA TTLSRFSTLT LSTEVCSHEA CPSSSTLPTT
TLSVTSKFTS YICPTCHTTA ISSLSEVGTT TVVSSSAIEP SSASIISPVT STLSSTTSSN
PTTTSLSSTS TSPSSTSTSP SSTSTSSSST STSSSSTSTS SSSTSTSPSS TSTSSSLTST
SSSSTSTSQS STSTSSSSTS TSPSSTSTSS SSTSTSPSSK STSASSTSTS SYSTSTSPSL
TSSSPTLAST SPSSTSISST FTDSTSSLGS SIASSSTSVS LYSPSTPVYS VPSTSSNVAT
PSMTSSTVET TVSSQSSSEY ITKSSISTTI PSFSMSTYFT TVSGVTTMYT TWCPYSSESE
TSTLTSMHET VTTDATVCTH ESCMPSQTTS LITSSIKMST KNVATSVSTS TVESSYACST
CAETSHSYSS VQTASSSSVT QQTTSTKSWV SSMTTSDEDF NKHATGKYHV TSSGTSTIST
SVSEATSTSS IDSESQEQSS HLLSTSVLSS SSLSATLSSD STILLFSSVS SLSVEQSPVT
TLQISSTSEI LQPTSSTAIA TISASTSSLS ATSISTPSTS VESTIESSSL TPTVSSIFLS
SSSAPSSLQT SVTTTEVSTT SISIQYQTSS MVTISQYMGS GSQTRLPLGK LVFAIMAVAC
NVIFS
