GAS3_YEAST
ID GAS3_YEAST Reviewed; 524 AA.
AC Q03655; D6W040;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Probable 1,3-beta-glucanosyltransferase GAS3;
DE EC=2.4.1.-;
DE AltName: Full=Glycolipid-anchored surface protein 3;
DE Flags: Precursor;
GN Name=GAS3; OrderedLocusNames=YMR215W; ORFNames=YM8261.09;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP IDENTIFICATION.
RX PubMed=11079560;
RX DOI=10.1002/1522-2683(20001001)21:16<3396::aid-elps3396>3.0.co;2-j;
RA Pardo M., Ward M., Bains S., Molina M., Blackstock W., Gil C., Nombela C.;
RT "A proteomic approach for the study of Saccharomyces cerevisiae cell wall
RT biogenesis.";
RL Electrophoresis 21:3396-3410(2000).
RN [5]
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).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=17397106; DOI=10.1002/yea.1473;
RA Ragni E., Fontaine T., Gissi C., Latge J.-P., Popolo L.;
RT "The Gas family of proteins of Saccharomyces cerevisiae: characterization
RT and evolutionary analysis.";
RL Yeast 24:297-308(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:17397106}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:15781460}. Membrane {ECO:0000269|PubMed:15781460};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15781460}.
CC Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
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 -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 16400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR EMBL; Z49809; CAA89930.1; -; Genomic_DNA.
DR EMBL; AY693202; AAT93221.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10114.1; -; Genomic_DNA.
DR PIR; S55097; S55097.
DR RefSeq; NP_013942.1; NM_001182722.1.
DR AlphaFoldDB; Q03655; -.
DR SMR; Q03655; -.
DR BioGRID; 35393; 201.
DR DIP; DIP-4410N; -.
DR IntAct; Q03655; 3.
DR MINT; Q03655; -.
DR STRING; 4932.YMR215W; -.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR COMPLUYEAST-2DPAGE; Q03655; -.
DR MaxQB; Q03655; -.
DR PaxDb; Q03655; -.
DR PRIDE; Q03655; -.
DR EnsemblFungi; YMR215W_mRNA; YMR215W; YMR215W.
DR GeneID; 855255; -.
DR KEGG; sce:YMR215W; -.
DR SGD; S000004828; GAS3.
DR VEuPathDB; FungiDB:YMR215W; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR GeneTree; ENSGT00940000176308; -.
DR HOGENOM; CLU_021855_1_2_1; -.
DR InParanoid; Q03655; -.
DR OMA; VGVAYQP; -.
DR BioCyc; YEAST:G3O-32898-MON; -.
DR PRO; PR:Q03655; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03655; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; ISS:SGD.
DR GO; GO:0034411; P:cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31468; PTHR31468; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..498
FT /note="Probable 1,3-beta-glucanosyltransferase GAS3"
FT /id="PRO_0000010477"
FT PROPEP 499..524
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010478"
FT REGION 461..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 96
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 168
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 169
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 212
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 217
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 315
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 498
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..107
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 226..369
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 254..286
FT /evidence="ECO:0000250|UniProtKB:Q06135"
SQ SEQUENCE 524 AA; 56794 MW; 3A2BED0BD3ED8690 CRC64;
MQLSKSILLA ALAATPSLVN AMLPIHIKNY RFIKPSSATN SESDNEVFFV KGVDYQPGGS
SGYDADSDTD ILSDPEVCAR DAYAFQQLGV NTVRIYSLNP DLNHDKCMTI FNNAGIYAIL
DVNSGNYGES LNRADPSGTY DSLYLSRVFK FIDAFKNYPN VLGFFSGNEV INDQSDYAKI
DPPYIRAVQR DMKQYISKHA NRSIPVGYSA ADNTDLRLAT FKYLQCNSLD GNKVNDDLDI
SKSDFFGLNT YEWCSGTSSW ESSGYDKLNS TFEDAVIPLI FSEYGCNKNT PRTFDEVSEG
LYGGLKNVFS GGLVYEYTEE ANNYGLVKLD DSGSLTYKDD FVNLESQLKN VSLPTTKESE
ISSDSIYKCD NSAITNIYSG FGTNNFTLPS QPAEIANMIE YGVNGTNTGK ILTDYAVPTT
FNYTIKNNKD DTISATISYD KANSLNELDV TATTVAKSAS TSQSSSRSLT SSTSPSSSTG
SSSSTGSSSA SSSSKSKGVG NIVNVSFSQS GYLALFAGLI SALL
