SCW4_YEAST
ID SCW4_YEAST Reviewed; 386 AA.
AC P53334; D6VV56;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Probable family 17 glucosidase SCW4;
DE EC=3.2.1.-;
DE AltName: Full=Soluble cell wall protein 4;
DE Flags: Precursor;
GN Name=SCW4; OrderedLocusNames=YGR279C;
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=9090054;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<251::aid-yea63>3.0.co;2-r;
RA Volckaert G., Voet M., Robben J.;
RT "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right
RT arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus
RT reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2
RT genes and an ABC transporter gene.";
RL Yeast 13:251-259(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 PROTEIN SEQUENCE OF 31-40, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 96099 / S288c / SEY6210;
RX PubMed=9748433; DOI=10.1128/jb.180.19.5030-5037.1998;
RA Cappellaro C., Mrsa V., Tanner W.;
RT "New potential cell wall glucanases of Saccharomyces cerevisiae and their
RT involvement in mating.";
RL J. Bacteriol. 180:5030-5037(1998).
RN [5]
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 [6]
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: Glucanases possibly play a role in cell expansion during
CC growth, in cell-cell fusion during mating, and in spore release during
CC sporulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9748433}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 38000 wall-bound molecules/cell in log
CC phase YPD medium. {ECO:0000269|PubMed:17617218}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; Z73064; CAA97310.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08367.1; -; Genomic_DNA.
DR PIR; S64614; S64614.
DR RefSeq; NP_011795.1; NM_001181408.1.
DR AlphaFoldDB; P53334; -.
DR SMR; P53334; -.
DR BioGRID; 33529; 106.
DR DIP; DIP-6513N; -.
DR IntAct; P53334; 6.
DR MINT; P53334; -.
DR STRING; 4932.YGR279C; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR iPTMnet; P53334; -.
DR MaxQB; P53334; -.
DR PaxDb; P53334; -.
DR PRIDE; P53334; -.
DR EnsemblFungi; YGR279C_mRNA; YGR279C; YGR279C.
DR GeneID; 853196; -.
DR KEGG; sce:YGR279C; -.
DR SGD; S000003511; SCW4.
DR VEuPathDB; FungiDB:YGR279C; -.
DR eggNOG; ENOG502QTKT; Eukaryota.
DR GeneTree; ENSGT00940000176321; -.
DR HOGENOM; CLU_027285_1_0_1; -.
DR InParanoid; P53334; -.
DR OMA; GLFTIQN; -.
DR BioCyc; YEAST:YGR279C-MON; -.
DR PRO; PR:P53334; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53334; protein.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005773; C:vacuole; IDA:SGD.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IBA:GO_Central.
DR GO; GO:0015926; F:glucosidase activity; ISS:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0000747; P:conjugation with cellular fusion; IGI:SGD.
DR InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..30
FT /evidence="ECO:0000269|PubMed:9748433"
FT /id="PRO_0000011899"
FT CHAIN 31..386
FT /note="Probable family 17 glucosidase SCW4"
FT /id="PRO_0000011900"
FT REGION 88..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 323
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 35
FT /note="T -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="Q -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 40173 MW; 86CE93AEC12E7612 CRC64;
MRLSNLIASA SLLSAATLAA PANHEHKDKR AVVTTTVQKQ TTIIVNGAAS TPVAALEENA
VVNSAPAAAT STTSSAASVA TAAASSSENN SQVSAAASPA SSSAATSTQS SSSSQASSSS
SSGEDVSSFA SGVRGITYTP YESSGACKSA SEVASDLAQL TDFPVIRLYG TDCNQVENVF
KAKASNQKVF LGIYYVDQIQ DGVNTIKSAV ESYGSWDDVT TVSIGNELVN GNQATPSQVG
QYIDSGRSAL KAAGYTGPVV SVDTFIAVIN NPELCDYSDY MAVNAHAYFD KNTVAQDSGK
WLLEQIQRVW TACDGKKNVV ITESGWPSKG ETYGVAVPSK ENQKDAVSAI TSSCGADTFL
FTAFNDYWKA DGAYGVEKYW GILSNE
