ID   GAS1_YEAST              Reviewed;         559 AA.
AC   P22146; D6W0D4; P23151;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=1,3-beta-glucanosyltransferase GAS1;
DE            EC=2.4.1.-;
DE   AltName: Full=Glycolipid-anchored surface protein 1;
DE   AltName: Full=Glycoprotein GP115;
DE   Flags: Precursor;
GN   Name=GAS1; Synonyms=GGP1; OrderedLocusNames=YMR307W;
GN   ORFNames=YM9952.09;
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], PROTEIN SEQUENCE OF 23-39; 237-240;
RP   435-437 AND 527-528, SUBCELLULAR LOCATION, AND GPI-ANCHOR AT ASN-528.
RX   PubMed=1824714; DOI=10.1128/mcb.11.1.27-37.1991;
RA   Nuoffer C., Jenoe P., Conzelmann A., Riezman H.;
RT   "Determinants for glycophospholipid anchoring of the Saccharomyces
RT   cerevisiae GAS1 protein to the plasma membrane.";
RL   Mol. Cell. Biol. 11:27-37(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DBY939;
RX   PubMed=2061310; DOI=10.1016/s0021-9258(18)98888-5;
RA   Vai M., Gatti E., Lacana E., Popolo L., Alberghina L.;
RT   "Isolation and deduced amino acid sequence of the gene encoding gp115, a
RT   yeast glycophospholipid-anchored protein containing a serine-rich region.";
RL   J. Biol. Chem. 266:12242-12248(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
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, AND GPI-ANCHOR.
RX   PubMed=3046936; DOI=10.1002/j.1460-2075.1988.tb03063.x;
RA   Conzelmann A., Riezman H., Desponds C., Bron C.;
RT   "A major 125-kd membrane glycoprotein of Saccharomyces cerevisiae is
RT   attached to the lipid bilayer through an inositol-containing
RT   phospholipid.";
RL   EMBO J. 7:2233-2240(1988).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=3072201;
RA   Popolo L., Grandori R., Vai M., Lacana E., Alberghina L.;
RT   "Immunochemical characterization of gp115, a yeast glycoprotein modulated
RT   by the cell cycle.";
RL   Eur. J. Cell Biol. 47:173-180(1988).
RN   [7]
RP   GPI-ANCHOR.
RX   PubMed=2160276; DOI=10.1016/0167-4838(90)90237-a;
RA   Vai M., Popolo L., Grandori R., Lacana E., Alberghina L.;
RT   "The cell cycle modulated glycoprotein GP115 is one of the major yeast
RT   proteins containing glycosylphosphatidylinositol.";
RL   Biochim. Biophys. Acta 1038:277-285(1990).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10564469; DOI=10.1046/j.1365-2958.1999.01585.x;
RA   De Sampaio G., Bourdineaud J.-P., Lauquin G.J.-M.;
RT   "A constitutive role for GPI anchors in Saccharomyces cerevisiae: cell wall
RT   targeting.";
RL   Mol. Microbiol. 34:247-256(1999).
RN   [9]
RP   FUNCTION.
RX   PubMed=10809732; DOI=10.1074/jbc.275.20.14882;
RA   Mouyna I., Fontaine T., Vai M., Monod M., Fonzi W.A., Diaquin M.,
RA   Popolo L., Hartland R.P., Latge J.-P.;
RT   "Glycosylphosphatidylinositol-anchored glucanosyltransferases play an
RT   active role in the biosynthesis of the fungal cell wall.";
RL   J. Biol. Chem. 275:14882-14889(2000).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF CYS-74; CYS-103; GLU-161; GLU-262 AND CYS-265.
RX   PubMed=15355340; DOI=10.1111/j.1432-1033.2004.04297.x;
RA   Carotti C., Ragni E., Palomares O., Fontaine T., Tedeschi G., Rodriguez R.,
RA   Latge J.-P., Vai M., Popolo L.;
RT   "Characterization of recombinant forms of the yeast Gas1 protein and
RT   identification of residues essential for glucanosyltransferase activity and
RT   folding.";
RL   Eur. J. Biochem. 271:3635-3645(2004).
RN   [11]
RP   SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND GPI-ANCHOR.
RX   PubMed=15781460; DOI=10.1074/jbc.m500334200;
RA   Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M.,
RA   de Koster C.G.;
RT   "Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls:
RT   identification of proteins covalently attached via
RT   glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages.";
RL   J. Biol. Chem. 280:20894-20901(2005).
RN   [12]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17142567; DOI=10.1128/ec.00203-06;
RA   Grabinska K.A., Magnelli P., Robbins P.W.;
RT   "Prenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III
RT   activity and chitin chain length.";
RL   Eukaryot. Cell 6:328-336(2007).
RN   [13]
RP   LEVEL OF PROTEIN EXPRESSION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17617218; DOI=10.1111/j.1567-1364.2007.00272.x;
RA   Yin Q.Y., de Groot P.W.J., de Jong L., Klis F.M., de Koster C.G.;
RT   "Mass spectrometric quantitation of covalently bound cell wall proteins in
RT   Saccharomyces cerevisiae.";
RL   FEMS Yeast Res. 7:887-896(2007).
RN   [14]
RP   MUTAGENESIS OF CYS-348.
RX   PubMed=18468997; DOI=10.1074/jbc.m801562200;
RA   Popolo L., Ragni E., Carotti C., Palomares O., Aardema R., Back J.W.,
RA   Dekker H.L., de Koning L.J., de Jong L., de Koster C.G.;
RT   "Disulfide bond structure and domain organization of yeast beta(1,3)-
RT   glucanosyltransferases involved in cell wall biogenesis.";
RL   J. Biol. Chem. 283:18553-18565(2008).
RN   [15]
RP   SUBCELLULAR LOCATION, GLYCOSYLATION, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=18434410; DOI=10.1128/jvi.00412-08;
RA   Luallen R.J., Lin J., Fu H., Cai K.K., Agrawal C., Mboudjeka I., Lee F.-H.,
RA   Montefiori D., Smith D.F., Doms R.W., Geng Y.;
RT   "An engineered Saccharomyces cerevisiae strain binds the broadly
RT   neutralizing human immunodeficiency virus type 1 antibody 2G12 and elicits
RT   mannose-specific gp120-binding antibodies.";
RL   J. Virol. 82:6447-6457(2008).
CC   -!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers
CC       the newly generated reducing end (the donor) to the non-reducing end of
CC       another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta
CC       linkage, resulting in the elongation of 1,3-beta-glucan chains in the
CC       cell wall. Involved in cell wall biosynthesis and morphogenesis.
CC       {ECO:0000269|PubMed:10809732, ECO:0000269|PubMed:15355340}.
CC   -!- INTERACTION:
CC       P22146; P06700: SIR2; NbExp=2; IntAct=EBI-7327, EBI-17219;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18434410,
CC       ECO:0000269|PubMed:3046936, ECO:0000269|PubMed:3072201}; Lipid-anchor,
CC       GPI-anchor {ECO:0000269|PubMed:2160276, ECO:0000269|PubMed:3046936}.
CC       Secreted, cell wall {ECO:0000269|PubMed:10564469,
CC       ECO:0000269|PubMed:15781460}. Note=Identified as GPI-anchored plasma
CC       membrane protein (GPI-PMP) as well as covalently-linked GPI-modified
CC       cell wall protein (GPI-CWP) in the outer cell wall layer.
CC       {ECO:0000269|PubMed:15781460, ECO:0000269|PubMed:3046936}.
CC   -!- PTM: Extensively N- and O-glycosylated. {ECO:0000269|PubMed:18434410}.
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   -!- DISRUPTION PHENOTYPE: Increases cellular chitin level
CC       (PubMed:17142567). Increases chitin chain length (PubMed:17142567).
CC       {ECO:0000269|PubMed:17142567}.
CC   -!- MISCELLANEOUS: Present with 11000 wall-bound molecules/cell in log
CC       phase YPD medium. {ECO:0000269|PubMed:17617218}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR   EMBL; X53424; CAA37512.1; -; Genomic_DNA.
DR   EMBL; X56399; CAA39809.1; -; Genomic_DNA.
DR   EMBL; Z49212; CAA89140.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10208.1; -; Genomic_DNA.
DR   PIR; S53977; RWBYS1.
DR   RefSeq; NP_014038.1; NM_001182818.1.
DR   AlphaFoldDB; P22146; -.
DR   SMR; P22146; -.
DR   BioGRID; 35487; 838.
DR   DIP; DIP-4390N; -.
DR   IntAct; P22146; 11.
DR   MINT; P22146; -.
DR   STRING; 4932.YMR307W; -.
DR   CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR   CAZy; GH72; Glycoside Hydrolase Family 72.
DR   GlyCosmos; P22146; 10 sites, No reported glycans.
DR   GlyGen; P22146; 10 sites.
DR   iPTMnet; P22146; -.
DR   MaxQB; P22146; -.
DR   PaxDb; 4932-YMR307W; -.
DR   PeptideAtlas; P22146; -.
DR   EnsemblFungi; YMR307W_mRNA; YMR307W; YMR307W.
DR   GeneID; 855355; -.
DR   KEGG; sce:YMR307W; -.
DR   AGR; SGD:S000004924; -.
DR   SGD; S000004924; GAS1.
DR   VEuPathDB; FungiDB:YMR307W; -.
DR   eggNOG; ENOG502QPST; Eukaryota.
DR   GeneTree; ENSGT00940000176308; -.
DR   HOGENOM; CLU_021855_2_1_1; -.
DR   InParanoid; P22146; -.
DR   OMA; CMYDASA; -.
DR   OrthoDB; 2783940at2759; -.
DR   BioCyc; YEAST:G3O-32971-MONOMER; -.
DR   BioGRID-ORCS; 855355; 6 hits in 10 CRISPR screens.
DR   PRO; PR:P22146; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P22146; Protein.
DR   GO; GO:0005621; C:cellular bud scar; IDA:SGD.
DR   GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA: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:0045121; C:membrane raft; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0000936; C:primary cell septum; IDA:SGD.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IDA:SGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:SGD.
DR   GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR   GO; GO:0031507; P:heterochromatin formation; IMP:SGD.
DR   GO; GO:1905897; P:regulation of response to endoplasmic reticulum stress; IMP:SGD.
DR   Gene3D; 1.20.58.1040; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR004886; Glucanosyltransferase.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR012946; X8.
DR   PANTHER; PTHR31468; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR   PANTHER; PTHR31468:SF2; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR   Pfam; PF03198; Glyco_hydro_72; 1.
DR   Pfam; PF07983; X8; 1.
DR   SMART; SM00768; X8; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   COMPLUYEAST-2DPAGE; P22146; -.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell wall; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Membrane; Reference proteome; Secreted; Signal; Transferase.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:1824714"
FT   CHAIN           23..528
FT                   /note="1,3-beta-glucanosyltransferase GAS1"
FT                   /id="PRO_0000010473"
FT   PROPEP          529..559
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000010474"
FT   REGION          474..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        161
FT                   /note="Proton donor"
FT   ACT_SITE        262
FT                   /note="Nucleophile"
FT   BINDING         92
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="1"
FT                   /ligand_note="donor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   BINDING         119..127
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="1"
FT                   /ligand_note="donor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   BINDING         160
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="1"
FT                   /ligand_note="donor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   BINDING         161
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="2"
FT                   /ligand_note="acceptor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   BINDING         202
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="2"
FT                   /ligand_note="acceptor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   BINDING         207
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="2"
FT                   /ligand_note="acceptor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   BINDING         294
FT                   /ligand="(1,3-beta-D-glucosyl)n"
FT                   /ligand_id="ChEBI:CHEBI:37671"
FT                   /ligand_label="1"
FT                   /ligand_note="donor substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   LIPID           528
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000269|PubMed:1824714"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        409
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        74..103
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        216..348
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        234..265
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        370..421
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        372..462
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        379..445
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        398..403
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   MUTAGEN         74
FT                   /note="C->S: Impairs the folding and stability of the
FT                   protein."
FT                   /evidence="ECO:0000269|PubMed:15355340"
FT   MUTAGEN         103
FT                   /note="C->S: Partially impairs the folding and stability of
FT                   the protein."
FT                   /evidence="ECO:0000269|PubMed:15355340"
FT   MUTAGEN         161
FT                   /note="E->Q: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:15355340"
FT   MUTAGEN         262
FT                   /note="E->Q: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:15355340"
FT   MUTAGEN         265
FT                   /note="C->S: Partially impairs the folding and stability of
FT                   the protein."
FT                   /evidence="ECO:0000269|PubMed:15355340"
FT   MUTAGEN         348
FT                   /note="C->S: Impairs the folding and stability of the
FT                   protein."
FT                   /evidence="ECO:0000269|PubMed:18468997"
FT   CONFLICT        211
FT                   /note="T -> A (in Ref. 1; CAA37512)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   559 AA;  59582 MW;  D6E39568DCB4C5AE CRC64;
     MLFKSLSKLA TAAAFFAGVA TADDVPAIEV VGNKFFYSNN GSQFYIRGVA YQADTANETS
     GSTVNDPLAN YESCSRDIPY LKKLNTNVIR VYAINTTLDH SECMKALNDA DIYVIADLAA
     PATSINRDDP TWTVDLFNSY KTVVDTFANY TNVLGFFAGN EVTNNYTNTD ASAFVKAAIR
     DVRQYISDKN YRKIPVGYSS NDDEDTRVKM TDYFACGDDD VKADFYGINM YEWCGKSDFK
     TSGYADRTAE FKNLSIPVFF SEYGCNEVTP RLFTEVEALY GSNMTDVWSG GIVYMYFEET
     NKYGLVSIDG NDVKTLDDFN NYSSEINKIS PTSANTKSYS ATTSDVACPA TGKYWSAATE
     LPPTPNGGLC SCMNAANSCV VSDDVDSDDY ETLFNWICNE VDCSGISANG TAGKYGAYSF
     CTPKEQLSFV MNLYYEKSGG SKSDCSFSGS ATLQTATTQA SCSSALKEIG SMGTNSASGS
     VDLGSGTESS TASSNASGSS SKSNSGSSGS SSSSSSSSAS SSSSSKKNAA TNVKANLAQV
     VFTSIISLSI AAGVGFALV
//