ENG2_YEAST
ID ENG2_YEAST Reviewed; 779 AA.
AC Q12168; D6VYD8; Q07268;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Endo-1,3(4)-beta-glucanase 2;
DE Short=Endo-1,3-beta-glucanase 2;
DE Short=Endo-1,4-beta-glucanase 2;
DE EC=3.2.1.6;
DE AltName: Full=Laminarinase-2;
GN Name=ACF2; Synonyms=ENG2, PCA1; OrderedLocusNames=YLR144C; ORFNames=L3180;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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] OF 680-779.
RC STRAIN=ATCC 204508 / S288c;
RA Delius H.;
RT "36.8 kb of S.cerevisiae chromosome XII including ACE2, CKI1, PDC5, SLS1,
RT PUT1 and tRNA-Asp.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION.
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 [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).
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 -!- INTERACTION:
CC Q12168; P38753: HSE1; NbExp=2; IntAct=EBI-32973, EBI-1382;
CC Q12168; P53281: LSB1; NbExp=4; IntAct=EBI-32973, EBI-23329;
CC Q12168; P43603: LSB3; NbExp=7; IntAct=EBI-32973, EBI-22980;
CC Q12168; P39743: RVS167; NbExp=9; IntAct=EBI-32973, EBI-14500;
CC Q12168; P32793: YSC84; NbExp=7; IntAct=EBI-32973, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12455695}.
CC -!- MISCELLANEOUS: Present with 1420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U53879; AAB82378.1; -; Genomic_DNA.
DR EMBL; Z73316; CAA97716.1; -; Genomic_DNA.
DR EMBL; X91258; CAA62664.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09454.1; -; Genomic_DNA.
DR PIR; S64993; S64993.
DR RefSeq; NP_013245.1; NM_001182031.1.
DR AlphaFoldDB; Q12168; -.
DR SMR; Q12168; -.
DR BioGRID; 31413; 74.
DR DIP; DIP-2889N; -.
DR IntAct; Q12168; 19.
DR MINT; Q12168; -.
DR STRING; 4932.YLR144C; -.
DR CAZy; GH81; Glycoside Hydrolase Family 81.
DR iPTMnet; Q12168; -.
DR MaxQB; Q12168; -.
DR PaxDb; Q12168; -.
DR PRIDE; Q12168; -.
DR EnsemblFungi; YLR144C_mRNA; YLR144C; YLR144C.
DR GeneID; 850836; -.
DR KEGG; sce:YLR144C; -.
DR SGD; S000004134; ACF2.
DR VEuPathDB; FungiDB:YLR144C; -.
DR eggNOG; KOG2254; Eukaryota.
DR GeneTree; ENSGT00940000176657; -.
DR HOGENOM; CLU_005482_2_1_1; -.
DR InParanoid; Q12168; -.
DR OMA; DWWHGHS; -.
DR BioCyc; YEAST:G3O-32281-MON; -.
DR PRO; PR:Q12168; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12168; protein.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA: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:0030036; P:actin cytoskeleton organization; IDA:SGD.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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 Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..779
FT /note="Endo-1,3(4)-beta-glucanase 2"
FT /id="PRO_0000215819"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 88403 MW; 8BCC24DF96414FA7 CRC64;
MCYSRQAIPP PVPNRPGGTT NRGPPPLPPR ANVQPPVCSS ENSSKPRENR VAGESLRTPS
SSNPLADSQV NSDNIFQSPV LSNLKAPPSV FNKVQHPVPK PNIDDQSVDP LETNKFYTNM
LLDDNTQPIW THPYSIWFSR DPELFGLAAN HTLASQRVFD TTTNPPRFYF NPTNIKSFVF
KAREFVSSND IKLEFRDMKH MSMCLLMSLS SSQFIEFPLV QGMGFVTAIY HDLGFELRSA
VGFRSLERIS VNERYGKYNI QLENNRNWIL YLTSPDYSFP QDFQISLLDS NTIISSHKIN
GLICQLSADS VPSIDMAAGC YPVYCDLSGQ TVDEHFTNYR FNYTVAGYSQ SGTTLMYALP
HHKAAFTPEM QEREIASSLD STVKGLMTGY LTNSFDMQVQ VPQELGFEPV ALSLNKKADY
SQEKLSKIRE AAVQEVQLSD PQQESNIDSM YFSGKILAKY AWILYVTHYI LHDENLTKEL
LSKLTIAMER FISNQQVLPL NYDVSWKGII SSGSSSQDFG NSYYNDHHFH YSYHVITAAI
ISLVDSDLSG VTNNSWLENN RDWVECLIRD YSGVDNDDPY FPQFRSFDWF NGHSWAKGLF
PSGDGKDEES TSEDVNSCYA IKLWGLVTGN SKLTDIANLQ LGIMRNVFQS YFLYESNNTV
QPKEFIGNKV SGILFENKID HATYFGMEPQ YIHMIHAIPI TSASSWVRTP NFVKEEWEEK
MQPIIDQVND GWKGIIMLNM ALLDPKFSYD FFSQPDFNRN FLDNGQSLTW SLAYSGAFS
