GAS4_YEAST
ID GAS4_YEAST Reviewed; 471 AA.
AC Q08271; D6W1T6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=1,3-beta-glucanosyltransferase GAS4;
DE EC=2.4.1.-;
DE AltName: Full=Glycolipid-anchored surface protein 4;
DE Flags: Precursor;
GN Name=GAS4; OrderedLocusNames=YOL132W;
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 96604 / S288c / FY1679;
RX PubMed=8896270;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1053::aid-yea993>3.0.co;2-s;
RA Aldea M., Piedrafita L., Casas C., Casamayor A., Khalid H., Balcells L.,
RA Arino J., Herrero E.;
RT "Sequence analysis of a 12 801 bp fragment of the left arm of yeast
RT chromosome XV containing a putative 6-phosphofructo-2-kinase gene, a gene
RT for a possible glycophospholipid-anchored surface protein and six other
RT open reading frames.";
RL Yeast 12:1053-1058(1996).
RN [2]
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 [3]
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10383953; DOI=10.1128/jb.181.13.3886-3889.1999;
RA Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.;
RT "Amino acid residues in the omega-minus region participate in cellular
RT localization of yeast glycosylphosphatidylinositol-attached proteins.";
RL J. Bacteriol. 181:3886-3889(1999).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17189486; DOI=10.1128/ec.00321-06;
RA Ragni E., Coluccio A., Rolli E., Rodriguez-Pena J.M., Colasante G.,
RA Arroyo J., Neiman A.M., Popolo L.;
RT "GAS2 and GAS4, a pair of developmentally regulated genes required for
RT spore wall assembly in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 6:302-316(2007).
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 spore wall assembly.
CC {ECO:0000269|PubMed:17189486, ECO:0000269|PubMed:17397106}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10383953};
CC Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:10383953}.
CC -!- DEVELOPMENTAL STAGE: Expressed exclusively during sporulation (at
CC protein level). {ECO:0000269|PubMed:17189486}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR EMBL; X95465; CAA64738.1; -; Genomic_DNA.
DR EMBL; Z74874; CAA99152.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10652.1; -; Genomic_DNA.
DR PIR; S66829; S66829.
DR RefSeq; NP_014509.1; NM_001183386.1.
DR AlphaFoldDB; Q08271; -.
DR SMR; Q08271; -.
DR BioGRID; 34243; 84.
DR DIP; DIP-4898N; -.
DR IntAct; Q08271; 3.
DR MINT; Q08271; -.
DR STRING; 4932.YOL132W; -.
DR CAZy; GH72; Glycoside Hydrolase Family 72.
DR PaxDb; Q08271; -.
DR EnsemblFungi; YOL132W_mRNA; YOL132W; YOL132W.
DR GeneID; 853988; -.
DR KEGG; sce:YOL132W; -.
DR SGD; S000005492; GAS4.
DR VEuPathDB; FungiDB:YOL132W; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR GeneTree; ENSGT00940000176308; -.
DR HOGENOM; CLU_021855_1_2_1; -.
DR InParanoid; Q08271; -.
DR OMA; DKCMTML; -.
DR BioCyc; YEAST:G3O-33527-MON; -.
DR PRO; PR:Q08271; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08271; 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: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; IEA:UniProtKB-SubCell.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IDA:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0034411; P:cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
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 membrane; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Signal; Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..447
FT /note="1,3-beta-glucanosyltransferase GAS4"
FT /id="PRO_0000010479"
FT PROPEP 448..471
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010480"
FT ACT_SITE 161
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 88
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 203
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 208
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 298
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 447
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..99
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 217..354
FT /evidence="ECO:0000250|UniProtKB:Q06135"
FT DISULFID 238..269
FT /evidence="ECO:0000250|UniProtKB:Q06135"
SQ SEQUENCE 471 AA; 53813 MW; E1F16622F1EA09C3 CRC64;
MMVFSSTFIF LILELVVLCE ASVHTIQIKD KHFVDTVTGK PFFIKGVDYQ PGGSSDVSEK
QDPLSNPDAC ARDILLFQEL GINTVRIYSI NPDLNHDACM TMLAMAGIYL ILDVNSPLQN
QHLNRYEPWT TYNEVYLEHV FKVVEQFSHY NNTLGFFAGN EIVNDKRSAQ YSPAYVKELI
GTMKNYISAH SPRTIPVGYS AADDLNYRVS LSEYLECKDD DKPENSVDFY GVNSYQWCGQ
QTMQTSGYDT LVDAYRSYSK PVFFSEFGCN KVLPRQFQEI GYLFSEEMYS VFCGGLVYEF
SQEDNNYGLV EYQEDDSVQL LADFEKLKSH YQNIEFPSMK TLKETVQMEE TPSCAEDYEN
LKIESKIAKN LGSSLIKKGV KVEKGKYIDI HEDQLSTNVT ILDKHGDRWN GPKKIEIRQS
LTLADLEGEE QEDADEDKDD LKRKHRNSAS ISGPLLPLGL CLLFFTFSLF F
