GAS1_YEAST
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 03-AUG-2022, entry version 189.
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; 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; 806.
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 iPTMnet; P22146; -.
DR COMPLUYEAST-2DPAGE; P22146; -.
DR MaxQB; P22146; -.
DR PaxDb; P22146; -.
DR PRIDE; P22146; -.
DR EnsemblFungi; YMR307W_mRNA; YMR307W; YMR307W.
DR GeneID; 855355; -.
DR KEGG; sce:YMR307W; -.
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; NWICNEV; -.
DR BioCyc; YEAST:G3O-32971-MON; -.
DR PRO; PR:P22146; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P22146; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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:0005737; C:cytoplasm; IBA:GO_Central.
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:0042124; F:1,3-beta-glucanosyltransferase activity; IDA:SGD.
DR GO; GO:0007568; P:aging; IMP:SGD.
DR GO; GO:0034411; P:cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
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 assembly; IMP:SGD.
DR GO; GO:1905897; P:regulation of response to endoplasmic reticulum stress; IMP:SGD.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012946; X8.
DR PANTHER; PTHR31468; PTHR31468; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
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
