SAG1_YEAST
ID SAG1_YEAST Reviewed; 650 AA.
AC P20840; D6VWH8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Alpha-agglutinin;
DE AltName: Full=AG-alpha-1;
DE Flags: Precursor;
GN Name=SAG1; Synonyms=AGAL1; OrderedLocusNames=YJR004C; ORFNames=J1418;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2676603; DOI=10.1016/0014-5793(89)81108-1;
RA Hauser K., Tanner W.;
RT "Purification of the inducible alpha-agglutinin of S. cerevisiae and
RT molecular cloning of the gene.";
RL FEBS Lett. 255:290-294(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2677666; DOI=10.1128/mcb.9.8.3155-3165.1989;
RA Lipke P.N., Wojciechowicz D., Kurjan J.;
RT "AG alpha 1 is the structural gene for the Saccharomyces cerevisiae alpha-
RT agglutinin, a cell surface glycoprotein involved in cell-cell interactions
RT during mating.";
RL Mol. Cell. Biol. 9:3155-3165(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-248; SER-282; THR-289;
RP THR-299; THR-303; ASN-306; THR-307; THR-308; THR-311; SER-314; THR-315;
RP THR-316; THR-329; SER-331; SER-334; SER-335; SER-338; THR-339; THR-340;
RP THR-341; THR-342; THR-345; SER-346; THR-349 AND SER-350, LACK OF
RP GLYCOSYLATION AT ASN-348, AND DISULFIDE BONDS.
RX PubMed=7592821; DOI=10.1074/jbc.270.44.26168;
RA Chen M.-H., Shen Z.-M., Bobin S., Kahn P.C., Lipke P.N.;
RT "Structure of Saccharomyces cerevisiae alpha-agglutinin. Evidence for a
RT yeast cell wall protein with multiple immunoglobulin-like domains with
RT atypical disulfides.";
RL J. Biol. Chem. 270:26168-26177(1995).
RN [6]
RP GLYCOSYLATION, AND GPI-ANCHOR.
RX PubMed=8455628; DOI=10.1128/mcb.13.4.2554-2563.1993;
RA Wojciechowicz D., Lu C.F., Kurjan J., Lipke P.N.;
RT "Cell surface anchorage and ligand-binding domains of the Saccharomyces
RT cerevisiae cell adhesion protein alpha-agglutinin, a member of the
RT immunoglobulin superfamily.";
RL Mol. Cell. Biol. 13:2554-2563(1993).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=8007981; DOI=10.1128/mcb.14.7.4825-4833.1994;
RA Lu C.-F., Kurjan J., Lipke P.N.;
RT "A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-
RT agglutinin.";
RL Mol. Cell. Biol. 14:4825-4833(1994).
RN [8]
RP GPI-ANCHOR, AND CROSS-LINKING TO CELL WALL.
RX PubMed=7844147; DOI=10.1083/jcb.128.3.333;
RA Lu C.-F., Montijn R.C., Brown J.L., Klis F., Kurjan J., Bussey H.,
RA Lipke P.N.;
RT "Glycosyl phosphatidylinositol-dependent cross-linking of alpha-agglutinin
RT and beta 1,6-glucan in the Saccharomyces cerevisiae cell wall.";
RL J. Cell Biol. 128:333-340(1995).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF ILE-214; ASP-215; TYR-216; ASP-217; THR-289;
RP ILE-290; ASP-291; HIS-292; LEU-294; GLU-295; PHE-296; TYR-298; TYR-322;
RP GLN-323; GLY-324 AND ARG-325.
RX PubMed=8741846; DOI=10.1091/mbc.7.1.143;
RA de Nobel H., Lipke P.N., Kurjan J.;
RT "Identification of a ligand-binding site in an immunoglobulin fold domain
RT of the Saccharomyces cerevisiae adhesion protein alpha-agglutinin.";
RL Mol. Biol. Cell 7:143-153(1996).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=9613572; DOI=10.1007/s004380050706;
RA Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K.;
RT "Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall
RT proteins in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 258:53-59(1998).
RN [11]
RP INTERACTION WITH AGA2.
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).
CC -!- FUNCTION: Cell surface glycoprotein promoting cell-cell contact to
CC facilitate mating. S.cerevisiae A and alpha cells express the
CC complementary cell surface glycoproteins A-agglutinin and alpha-,
CC respectively, which interact with one another to promote cellular
CC aggregation during mating. {ECO:0000269|PubMed:8741846}.
CC -!- SUBUNIT: Interacts with AGA2. {ECO:0000269|PubMed:11292808}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-
CC CWP).
CC -!- INDUCTION: By exposition to pheromone (A-factor) secreted by the
CC opposite mating type cells (type A).
CC -!- PTM: N-glycosylated, and O-glycosylated by both PMT1 and PMT2.
CC {ECO:0000269|PubMed:7592821, ECO:0000269|PubMed:8455628}.
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.
CC -!- SIMILARITY: To C.albicans ALS1. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Alpha-agglutinin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_oth_other_801";
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DR EMBL; X16861; CAA34752.1; -; Genomic_DNA.
DR EMBL; M28164; AAA34417.1; -; Genomic_DNA.
DR EMBL; X87611; CAA60926.1; -; Genomic_DNA.
DR EMBL; Z49504; CAA89526.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08794.1; -; Genomic_DNA.
DR PIR; S22835; S22835.
DR RefSeq; NP_012537.1; NM_001181661.1.
DR AlphaFoldDB; P20840; -.
DR SMR; P20840; -.
DR BioGRID; 33760; 37.
DR DIP; DIP-5692N; -.
DR MINT; P20840; -.
DR STRING; 4932.YJR004C; -.
DR iPTMnet; P20840; -.
DR PaxDb; P20840; -.
DR PRIDE; P20840; -.
DR EnsemblFungi; YJR004C_mRNA; YJR004C; YJR004C.
DR GeneID; 853460; -.
DR KEGG; sce:YJR004C; -.
DR SGD; S000003764; SAG1.
DR VEuPathDB; FungiDB:YJR004C; -.
DR eggNOG; ENOG502RGCG; Eukaryota.
DR HOGENOM; CLU_019475_0_0_1; -.
DR InParanoid; P20840; -.
DR OMA; IIIHVET; -.
DR BioCyc; YEAST:G3O-31650-MON; -.
DR PRO; PR:P20840; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P20840; 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:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IMP:SGD.
DR GO; GO:0000752; P:agglutination involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR Gene3D; 2.60.40.1280; -; 1.
DR Gene3D; 2.60.40.2430; -; 1.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR024672; Agglutinin-like_N.
DR InterPro; IPR043063; Agglutinin-like_N_N2.
DR InterPro; IPR033504; ALS.
DR InterPro; IPR011252; Fibrogen-bd_dom1.
DR PANTHER; PTHR33793; PTHR33793; 1.
DR Pfam; PF11766; Candida_ALS_N; 1.
DR SMART; SM01056; Candida_ALS_N; 1.
DR SUPFAM; SSF49401; SSF49401; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell wall; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT CHAIN 20..627
FT /note="Alpha-agglutinin"
FT /id="PRO_0000022265"
FT PROPEP 628..650
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000022266"
FT REPEAT 339..378
FT /note="1"
FT REPEAT 384..423
FT /note="2"
FT REGION 216..322
FT /note="Ig-like fold domain important for alpha-agglutinin
FT activity, contributing to a functional binding site for a-
FT agglutinin"
FT REGION 339..423
FT /note="2 X 40 AA tandem repeats"
FT SITE 348
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:7592821"
FT LIPID 627
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 282
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 289
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 299
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 303
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 307
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 308
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 311
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 314
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 315
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 316
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 329
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 331
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 334
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 335
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 338
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 339
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 340
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 341
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 342
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 345
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 346
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 349
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 350
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:7592821"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..114
FT /evidence="ECO:0000269|PubMed:7592821"
FT DISULFID 202..300
FT /evidence="ECO:0000269|PubMed:7592821"
FT MUTAGEN 211
FT /note="T->I: Little effect on secreted alpha-agglutinin
FT activity."
FT MUTAGEN 214
FT /note="I->M: No effect on secreted alpha-agglutinin
FT activity."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 215
FT /note="D->A,N: Little or no effect on secreted alpha-
FT agglutinin activity."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 216
FT /note="Y->D: Complete loss of alpha-agglutinin activity."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 216
FT /note="Y->F: No effect on secreted alpha-agglutinin
FT activity."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 216
FT /note="Y->S: Decreases secreted alpha-agglutinin activity
FT by 100-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 216
FT /note="Y->V: Decreases secreted alpha-agglutinin activity
FT by 10-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 217
FT /note="D->A: Little effect on secreted alpha-agglutinin
FT activity."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 217
FT /note="D->N: Decreases secreted alpha-agglutinin activity
FT by 10-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 289
FT /note="T->A: Decreases secreted alpha-agglutinin activity
FT by less than 2-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 290
FT /note="I->M: Decreases secreted alpha-agglutinin activity
FT by less than 2-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 291
FT /note="D->A,N: Decreases secreted alpha-agglutinin activity
FT by 4-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 292
FT /note="H->L,R: Almost complete loss of secreted alpha-
FT agglutinin activity."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 294
FT /note="L->S: Decreases secreted alpha-agglutinin activity
FT by more than 20-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 295
FT /note="E->A,Q: Decreases secreted alpha-agglutinin activity
FT by 2-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 296
FT /note="F->Y: Decreases secreted alpha-agglutinin activity
FT by more than 20-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 298
FT /note="Y->H: Decreases secreted alpha-agglutinin activity
FT by less than 2-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 322
FT /note="Y->A: Decreases secreted alpha-agglutinin activity
FT by 60-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 322
FT /note="Y->C: Almost complete loss of secreted alpha-
FT agglutinin activity by 10-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 322
FT /note="Y->F: Decreases secreted alpha-agglutinin activity
FT by 15-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 323
FT /note="Q->L: Decreases secreted alpha-agglutinin activity
FT by 2-fold."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 324
FT /note="G->A: Little effect on secreted alpha-agglutinin
FT activity."
FT /evidence="ECO:0000269|PubMed:8741846"
FT MUTAGEN 325
FT /note="R->G: Little effect on secreted alpha-agglutinin
FT activity."
FT /evidence="ECO:0000269|PubMed:8741846"
FT CONFLICT 449
FT /note="S -> P (in Ref. 1; AAA34417)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="K -> E (in Ref. 1; AAA34417)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="V -> L (in Ref. 1; AAA34417)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 70340 MW; 8BBF7A1C44C93C2B CRC64;
MFTFLKIILW LFSLALASAI NINDITFSNL EITPLTANKQ PDQGWTATFD FSIADASSIR
EGDEFTLSMP HVYRIKLLNS SQTATISLAD GTEAFKCYVS QQAAYLYENT TFTCTAQNDL
SSYNTIDGSI TFSLNFSDGG SSYEYELENA KFFKSGPMLV KLGNQMSDVV NFDPAAFTEN
VFHSGRSTGY GSFESYHLGM YCPNGYFLGG TEKIDYDSSN NNVDLDCSSV QVYSSNDFND
WWFPQSYNDT NADVTCFGSN LWITLDEKLY DGEMLWVNAL QSLPANVNTI DHALEFQYTC
LDTIANTTYA TQFSTTREFI VYQGRNLGTA SAKSSFISTT TTDLTSINTS AYSTGSISTV
ETGNRTTSEV ISHVVTTSTK LSPTATTSLT IAQTSIYSTD SNITVGTDIH TTSEVISDVE
TISRETASTV VAAPTSTTGW TGAMNTYISQ FTSSSFATIN STPIISSSAV FETSDASIVN
VHTENITNTA AVPSEEPTFV NATRNSLNSF CSSKQPSSPS SYTSSPLVSS LSVSKTLLST
SFTPSVPTSN TYIKTKNTGY FEHTALTTSS VGLNSFSETA VSSQGTKIDT FLVSSLIAYP
SSASGSQLSG IQQNFTSTSL MISTYEGKAS IFFSAELGSI IFLLLSYLLF
