ENG1_CANAL
ID ENG1_CANAL Reviewed; 1145 AA.
AC Q5AIR7; A0A1D8PD46; Q5AHY6;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Endo-1,3(4)-beta-glucanase 1 {ECO:0000305};
DE Short=Endo-1,3-beta-glucanase 1 {ECO:0000303|PubMed:16328626};
DE Short=Endo-1,4-beta-glucanase 1 {ECO:0000305};
DE EC=3.2.1.6 {ECO:0000269|PubMed:16328626};
DE AltName: Full=Daughter specific expression protein 4 {ECO:0000303|PubMed:16987174};
DE AltName: Full=Laminarinase {ECO:0000305};
DE Flags: Precursor;
GN Name=ENG1 {ECO:0000303|PubMed:16328626};
GN Synonyms=ACF3, DSE4 {ECO:0000303|PubMed:16987174};
GN OrderedLocusNames=CAALFM_C103680WA; ORFNames=CaO19.10584, CaO19.3066;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION.
RX PubMed=14731272; DOI=10.1111/j.1365-2958.2003.03879.x;
RA Lee C.M., Nantel A., Jiang L., Whiteway M., Shen S.H.;
RT "The serine/threonine protein phosphatase SIT4 modulates yeast-to-hypha
RT morphogenesis and virulence in Candida albicans.";
RL Mol. Microbiol. 51:691-709(2004).
RN [5]
RP DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, FUNCTION, AND INDUCTION.
RX PubMed=16328626; DOI=10.1007/s00284-005-0066-2;
RA Esteban P.F., Rios I., Garcia R., Duenas E., Pla J., Sanchez M.,
RA de Aldana C.R., Del Rey F.;
RT "Characterization of the CaENG1 gene encoding an endo-1,3-beta-glucanase
RT involved in cell separation in Candida albicans.";
RL Curr. Microbiol. 51:385-392(2005).
RN [6]
RP INDUCTION.
RX PubMed=16998073; DOI=10.1128/ec.00155-06;
RA Mulhern S.M., Logue M.E., Butler G.;
RT "Candida albicans transcription factor Ace2 regulates metabolism and is
RT required for filamentation in hypoxic conditions.";
RL Eukaryot. Cell 5:2001-2013(2006).
RN [7]
RP INDUCTION.
RX PubMed=16987174; DOI=10.1111/j.1365-2958.2006.05367.x;
RA Bennett R.J., Johnson A.D.;
RT "The role of nutrient regulation and the Gpa2 protein in the mating
RT pheromone response of C. albicans.";
RL Mol. Microbiol. 62:100-119(2006).
RN [8]
RP INDUCTION.
RX PubMed=19527170; DOI=10.1086/599838;
RA Nett J.E., Lepak A.J., Marchillo K., Andes D.R.;
RT "Time course global gene expression analysis of an in vivo Candida
RT biofilm.";
RL J. Infect. Dis. 200:307-313(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21622905; DOI=10.1128/ec.05011-11;
RA Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S., de Koster C.G.,
RA de Koning L.J., Klis F.M.;
RT "Effects of fluconazole on the secretome, the wall proteome, and wall
RT integrity of the clinical fungus Candida albicans.";
RL Eukaryot. Cell 10:1071-1081(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=23243062; DOI=10.1128/ec.00278-12;
RA Heilmann C.J., Sorgo A.G., Mohammadi S., Sosinska G.J., de Koster C.G.,
RA Brul S., de Koning L.J., Klis F.M.;
RT "Surface stress induces a conserved cell wall stress response in the
RT pathogenic fungus Candida albicans.";
RL Eukaryot. Cell 12:254-264(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=23136884; DOI=10.1111/mmi.12087;
RA Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
RA Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
RT "A family of secreted pathogenesis-related proteins in Candida albicans.";
RL Mol. Microbiol. 87:132-151(2013).
CC -!- FUNCTION: Endo-1,3(4)-beta-glucanase involved in the cell separation
CC process. Plays no essential role in growth, nor is it involved in
CC hyphal morphogenesis. {ECO:0000269|PubMed:16328626}.
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 Evidence={ECO:0000269|PubMed:16328626};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:21622905,
CC ECO:0000269|PubMed:23136884, ECO:0000269|PubMed:23243062}.
CC -!- INDUCTION: Expression is decreased during the hyphal transition, in
CC biofilm, as well as by heat stress, caspofungin, fluconazole, and alpha
CC pheromone. Transcription is also regulated by ACE2 and SIT4.
CC {ECO:0000269|PubMed:14731272, ECO:0000269|PubMed:16328626,
CC ECO:0000269|PubMed:16987174, ECO:0000269|PubMed:16998073,
CC ECO:0000269|PubMed:19527170, ECO:0000269|PubMed:21622905,
CC ECO:0000269|PubMed:23136884, ECO:0000269|PubMed:23243062}.
CC -!- DISRUPTION PHENOTYPE: Leads to clusters of growing cells that have not
CC completed separation. {ECO:0000269|PubMed:16328626}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26046.1; -; Genomic_DNA.
DR RefSeq; XP_721564.1; XM_716471.2.
DR AlphaFoldDB; Q5AIR7; -.
DR SMR; Q5AIR7; -.
DR BioGRID; 1219980; 1.
DR STRING; 237561.Q5AIR7; -.
DR PRIDE; Q5AIR7; -.
DR GeneID; 3636886; -.
DR KEGG; cal:CAALFM_C103680WA; -.
DR CGD; CAL0000184614; ENG1.
DR VEuPathDB; FungiDB:C1_03680W_A; -.
DR eggNOG; KOG2254; Eukaryota.
DR HOGENOM; CLU_005482_0_1_1; -.
DR OrthoDB; 276151at2759; -.
DR PRO; PR:Q5AIR7; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0030428; C:cell septum; IEA:EnsemblFungi.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:EnsemblFungi.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IBA:GO_Central.
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:0004338; F:glucan exo-1,3-beta-glucosidase activity; IDA:CGD.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:CGD.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1145
FT /note="Endo-1,3(4)-beta-glucanase 1"
FT /id="PRO_0000429487"
FT REGION 73..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 775
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1145 AA; 124051 MW; AB439EBAE28EFE77 CRC64;
MLFKSVLLST LIAVQALAEN SAHQEIVTVT KTTHISNPCL ENYAKKLLPN NPTGLTTGIP
IVIVYAPQQP DNQVKQSESL QPTQSSKAQQ QQQIQGSSVP ASIHDTPTPT DHTKITVTST
TICNQKVCTV KTFSTIISHS ESPTTTTTTK QNEEKSIADT KSFTHKALPS SNGAVTLKTT
SVKTALTTTS TVFSATSLPS TTYTPSTSVS LVSTTKKNPV SSQSVVSTTK TISINTSLIT
DAVTITKEAT TLPNSKHSSI FTNGSISFIS TSANKVKSTV TSDISNNSQN GSSLSLTSTI
NQLASITNST LTTITKPTSL VPDFSYTNSS RVSSTMRNSS EESSMVLEKS SSKLLSSTSF
LNSSSIASTT ESSELASATT SDSSLNHSSS SSVELSSSLS SEADSSSSSE SVETGSSDET
ASNYSGDLFK AIDTNAPPTV FARSEIPLTI PAGVDNNGKP IGTNKFYTNL LLGNQDFMVY
PLPYGLYWSK TSYYGFAVQH NNVSDRVFGS INTNNKGVAS YYFNPTNNAE LIFSATSFSK
DSMHMKVSQM AELSALVTLS SSSNDESNYL DIPLVQGMGF VTGIYNGNLT PLLNSLFGVK
DLSLETSDAL LSNVLKYRAT LLNNVQWLIY VTLPDKDTDF KLEVEDFYNL KGSKPVDGLI
IQVAIAPEDN DNDKYYDAAA GMYVTGATVS GSVSQGTAAS YKFSYTTAGK SSSNNPIVFA
LPHHMDSLTG SALDALTGIT VTSTTKGEMT GFLTNELEFS ETINQDVEFL PWTENMTGSL
TYTKDQLELL ASAANKELAA NIAATVKNMN SNYFSGKVLD KYAQILLVVS EIIQDEEVTK
DALNAMKDAF KVFTQNKQYY PLMYDTKFGG VTSTSAQDGD PNADFGSAYY NDHDFHYGYF
IHAAAIVGYV DKKLGGTWAQ SNKDWVNSLV RDASNPSADD TYFPVSRMFD WFSGHSWATG
LFVTYKNIES SSESLHFAAA IKLWGKVVGD QSMEARGGLM ISIMARSFNM YFYYKSDNTV
EPKQILPNKV SGIFFENKVD YTTFFGTPAD HPEYVHGIHM LPITPSSSLV RKTSYVQEEW
KDQIAGFIDN VDSGWTGILR LNQALFDPKS SYEFFASNNW DDKWLDNGQS RTWSLAFAAG
ALNAS
