GAS5_YEAST
ID GAS5_YEAST Reviewed; 484 AA.
AC Q08193; D6W235;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=1,3-beta-glucanosyltransferase GAS5;
DE EC=2.4.1.-;
DE AltName: Full=Glycolipid-anchored surface protein 5;
DE Flags: Precursor;
GN Name=GAS5; OrderedLocusNames=YOL030W;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [5]
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 [6]
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).
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: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 -!- MISCELLANEOUS: Present with 11700 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; Z74772; CAA99030.1; -; Genomic_DNA.
DR EMBL; AY693093; AAT93112.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10751.1; -; Genomic_DNA.
DR PIR; S66713; S66713.
DR RefSeq; NP_014612.1; NM_001183284.1.
DR AlphaFoldDB; Q08193; -.
DR SMR; Q08193; -.
DR BioGRID; 34370; 87.
DR DIP; DIP-4240N; -.
DR IntAct; Q08193; 4.
DR MINT; Q08193; -.
DR STRING; 4932.YOL030W; -.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR MaxQB; Q08193; -.
DR PaxDb; Q08193; -.
DR PRIDE; Q08193; -.
DR EnsemblFungi; YOL030W_mRNA; YOL030W; YOL030W.
DR GeneID; 854127; -.
DR KEGG; sce:YOL030W; -.
DR SGD; S000005390; GAS5.
DR VEuPathDB; FungiDB:YOL030W; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR GeneTree; ENSGT00940000176308; -.
DR HOGENOM; CLU_021855_1_0_1; -.
DR InParanoid; Q08193; -.
DR OMA; MFAKYDN; -.
DR BioCyc; YEAST:G3O-33446-MON; -.
DR PRO; PR:Q08193; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08193; 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:0005783; C:endoplasmic reticulum; 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:0042124; F:1,3-beta-glucanosyltransferase activity; IDA:SGD.
DR GO; GO:0006074; P:(1->3)-beta-D-glucan metabolic process; IC: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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..462
FT /note="1,3-beta-glucanosyltransferase GAS5"
FT /id="PRO_0000010481"
FT PROPEP 463..484
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010482"
FT REGION 383..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 89
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 159
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="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT BINDING 201
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 206
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 295
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 462
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..100
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 215..348
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 234..265
FT /evidence="ECO:0000250|UniProtKB:Q06135"
SQ SEQUENCE 484 AA; 51870 MW; E65B9F4689B8B34C CRC64;
MLLRSLTSAF VLSAGLAQAA SSSNSSTPSI EIKGNAFFNS ESGERFYIRG VDYQPGGSSN
LTDPLADASV CDRDVPVLKD LGINTVRVYT VDNSQDHSHC MKLLQENGIY LILDVNTPTS
AISRYDPACS YNADYLQNVF ATIDTFADYD NVLGFFAGNE VINSVNTTNT ATYVKAVVRD
MKKYIKARKY RQIPVGYSAA DIVANRQLAA EYFNCGDEAD ARIDMFGVND YSWCGESSFV
VSGYSTKMKL YQDYSVPVFL SEFGCNQVKS SRPFTEIEAI YSTQMSSVFS GGLVYEYSNE
TNNYGLVQID GDKVTKLTDF ENLKNEYSKV SNPEGNGGYS TSNNYSTCPD YEKGVWEANN
TLPAMPSAAS AYFTSGAGSP MGTGIATQQS CDAKDDDDEE DDDTSSSSSS SSSSSSSASS
SSESSSSTSK ASSSSPSASE TSLLKSAASA TSSSQSSSKS KGAAGIIEIP LIFRALAELY
NLVL
