ENG1_YEAST
ID ENG1_YEAST Reviewed; 1117 AA.
AC P53753; D6W1P2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Endo-1,3(4)-beta-glucanase 1;
DE Short=Endo-1,3-beta-glucanase 1;
DE Short=Endo-1,4-beta-glucanase 1;
DE EC=3.2.1.6;
DE AltName: Full=Daughter specific expression protein 4;
DE AltName: Full=Laminarinase-1;
DE Flags: Precursor;
GN Name=DSE4; Synonyms=ENG1; OrderedLocusNames=YNR067C; ORFNames=N3547;
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=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=12455695; DOI=10.1128/ec.1.5.774-786.2002;
RA Baladron V., Ufano S., Duenas E., Martin-Cuadrado A.B., del Rey F.,
RA Vazquez de Aldana C.R.;
RT "Eng1p, an endo-1,3-beta-glucanase localized at the daughter side of the
RT septum, is involved in cell separation in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 1:774-786(2002).
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).
CC -!- FUNCTION: Involved in the dissolution of the mother-daughter septum
CC during cell separation. {ECO:0000269|PubMed:12455695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans
CC when the glucose residue whose reducing group is involved in the
CC linkage to be hydrolyzed is itself substituted at C-3.; EC=3.2.1.6;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:12455695}. Note=Localizes asymmetrically to the
CC daughter side of the septum.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:12455695}.
CC -!- MISCELLANEOUS: Present with 64 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family. {ECO:0000305}.
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DR EMBL; Z71682; CAA96349.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10608.1; -; Genomic_DNA.
DR PIR; S63399; S63399.
DR RefSeq; NP_014465.1; NM_001183244.1.
DR AlphaFoldDB; P53753; -.
DR SMR; P53753; -.
DR BioGRID; 35893; 51.
DR IntAct; P53753; 1.
DR MINT; P53753; -.
DR STRING; 4932.YNR067C; -.
DR CAZy; GH81; Glycoside Hydrolase Family 81.
DR CLAE; LAM81A_YEAST; -.
DR iPTMnet; P53753; -.
DR MaxQB; P53753; -.
DR PaxDb; P53753; -.
DR PRIDE; P53753; -.
DR EnsemblFungi; YNR067C_mRNA; YNR067C; YNR067C.
DR GeneID; 855804; -.
DR KEGG; sce:YNR067C; -.
DR SGD; S000005350; DSE4.
DR VEuPathDB; FungiDB:YNR067C; -.
DR eggNOG; KOG2254; Eukaryota.
DR GeneTree; ENSGT00940000176657; -.
DR HOGENOM; CLU_005482_0_0_1; -.
DR InParanoid; P53753; -.
DR OMA; ITFMNKI; -.
DR BioCyc; YEAST:G3O-33371-MON; -.
DR PRO; PR:P53753; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53753; protein.
DR GO; GO:0030428; C:cell septum; IDA:SGD.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; 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:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IGI:SGD.
DR GO; GO:0052861; F:glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR GO; GO:0052862; F:glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:SGD.
DR InterPro; IPR005200; Endo-beta-glucanase.
DR InterPro; IPR040720; GH81_C.
DR InterPro; IPR040451; GH81_N.
DR PANTHER; PTHR31983; PTHR31983; 1.
DR Pfam; PF17652; Glyco_hydro81C; 1.
DR Pfam; PF03639; Glyco_hydro_81; 1.
PE 1: Evidence at protein level;
KW Cell wall; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1117
FT /note="Endo-1,3(4)-beta-glucanase 1"
FT /id="PRO_0000012133"
FT REGION 66..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1117 AA; 121064 MW; 87F13A07E42B0AD1 CRC64;
MQLYLTLLFL LSFVECSYIS FISNNADEIL ETDLIETLSY ATLTVGEPYV AQSVVVTRVS
AASHSPLSVS PKNRVSASPI NSQDSDSNTR TAVQLSLSLS NYASQVSQKI SAQTNNDPVT
VSNIYANDNS KSKSSVHNLS SVSGVASVMP SASTMRKVTT LLSQTASTST STLFSSSLSI
SGTQLNGTLL TSVSKGTIDP LVTQMPSYSS QETKIIPSSL TSNKTIYTIS VRTNAATATG
EDSFIASTPA SSTLFYPSNS TQDLVQTLAS TTASPAYPSN RTQITLSPSV SLYSTTSPIY
PSNITENGSS PSPSLSSTVS PVYPSSSTGN ILLSSLFSTV DSSSSPVSST LDTIYVSSSM
QATISSSSSS RQTKTSSSSL STSTSSTATT TENSSTTTIV NLFNAVSTDE PPTVFDRSPN
PMSLADGVSN DGPIQTNKFY TNLIVGSQES PAFVYPYSLW KYTSSSYGFA VQHTTVDQYS
YGGYDSSGNA EYLVNPLGIA HVVFSASNFD SSMTMQVDEM TLSSTRVVLS ESNDSSNYLE
IPLVQGMGFA TGIYHGSLNA KIGSSVGFNT IVSESSSNLA QGILKYRITL LNGVTWLCYV
IGPDDLTSTD FSLEVSSEYE IKASASVDGL IIQLAVAPSE TDYEVFYDQA AGMYVTNFKL
QGVSDGSTAT YEFSYTTQGE SASGSTMIFA LPHHESSFSD IMQDYYTGIQ LASTTKGVMN
GYLTTSLQFS TSLNRQISWL PWSSQLGSNL LEYSKEQLQL LAEVANSELQ VSISESISGL
NTYYLGKVID KYSYILLTVS EIIQDEASTK STLENIKSAF DILLQNEQTY PLIYDTKFNG
LVSSGDWGST STQYDFGNTY YNDHHFHYGY IIHAAAVIGY VDSKLNGTWA ADNKDWVNSL
VRDVANPSEK DEYFAQSRMF DWFNGHSWAA GLYENGNGKN EESSSEDYNF AYAMKLWGAT
IGDQSMELRG DLMISIMKDA MNDYFYYQND NTVEPEEIIG NKVSGILFDN IIDYTTYFGT
NTEYIHGIHM LPITPVSSNI RSETFVEEEW QTKIEPIIES IESGWTGILK LNQALFDPVD
SYAFFSDSTF DSSTYLDNGM SRTWALAFSG GLANSIA
