ID   EGLC_EMENI              Reviewed;         465 AA.
AC   Q5AUT0; C8V585; Q4QXR7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Probable glucan endo-1,3-beta-glucosidase eglC;
DE            EC=3.2.1.39;
DE   AltName: Full=Endo-1,3-beta-glucanase eglC;
DE   AltName: Full=Laminarinase eglC;
DE   Flags: Precursor;
GN   Name=eglC; ORFNames=AN7950;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX   PubMed=15950156; DOI=10.1016/j.fgb.2005.02.002;
RA   Choi C.J., Ju H.J., Park B.H., Qin R., Jahng K.Y., Han D.M., Chae K.S.;
RT   "Isolation and characterization of the Aspergillus nidulans eglC gene
RT   encoding a putative beta-1,3-endoglucanase.";
RL   Fungal Genet. Biol. 42:590-600(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=19585695; DOI=10.1016/j.fgb.2008.07.022;
RA   de Groot P.W., Brandt B.W., Horiuchi H., Ram A.F., de Koster C.G.,
RA   Klis F.M.;
RT   "Comprehensive genomic analysis of cell wall genes in Aspergillus
RT   nidulans.";
RL   Fungal Genet. Biol. 46:S72-S81(2009).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25043916; DOI=10.1186/1471-2164-15-613;
RA   Martins I., Hartmann D.O., Alves P.C., Martins C., Garcia H.,
RA   Leclercq C.C., Ferreira R., He J., Renaut J., Becker J.D.,
RA   Silva Pereira C.;
RT   "Elucidating how the saprophytic fungus Aspergillus nidulans uses the plant
RT   polyester suberin as carbon source.";
RL   BMC Genomics 15:613-613(2014).
CC   -!- FUNCTION: Glucanases play a role in cell expansion during growth, in
CC       cell-cell fusion during mating, and in spore release during
CC       sporulation. This enzyme may be involved in beta-glucan degradation and
CC       also function biosynthetically as a transglycosylase.
CC       {ECO:0000269|PubMed:15950156}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19585695};
CC       Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:19585695}. Secreted, cell
CC       wall {ECO:0000269|PubMed:19585695}. Secreted
CC       {ECO:0000269|PubMed:25043916}. Note=Covalently-linked GPI-modified cell
CC       wall protein.
CC   -!- INDUCTION: Expression is under the control of the nsdD transcription
CC       factor required for sexual development. Transcript level is the highest
CC       at the beginning of asexual development and decreases thereafter to
CC       increase again at the late stage. {ECO:0000269|PubMed:15950156}.
CC   -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC       reticulum and serves to target the protein to the cell surface. There,
CC       the glucosamine-inositol phospholipid moiety is cleaved off and the
CC       GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC       glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; AY684801; AAT90341.1; -; Genomic_DNA.
DR   EMBL; AACD01000135; EAA59604.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF73583.1; -; Genomic_DNA.
DR   RefSeq; XP_681219.1; XM_676127.1.
DR   AlphaFoldDB; Q5AUT0; -.
DR   SMR; Q5AUT0; -.
DR   STRING; 227321.Q5AUT0; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   GlyCosmos; Q5AUT0; 2 sites, No reported glycans.
DR   EnsemblFungi; CBF73583; CBF73583; ANIA_07950.
DR   GeneID; 2869200; -.
DR   KEGG; ani:AN7950.2; -.
DR   VEuPathDB; FungiDB:AN7950; -.
DR   eggNOG; ENOG502SI3D; Eukaryota.
DR   HOGENOM; CLU_028820_1_1_1; -.
DR   InParanoid; Q5AUT0; -.
DR   OMA; WDDVGCP; -.
DR   OrthoDB; 1110018at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR16631; GLUCAN 1,3-BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR16631:SF13; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE EGLC-RELATED; 1.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell membrane; Cell wall;
KW   Cell wall biogenesis/degradation; Glycoprotein; GPI-anchor; Hydrolase;
KW   Lipoprotein; Membrane; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..442
FT                   /note="Probable glucan endo-1,3-beta-glucosidase eglC"
FT                   /id="PRO_0000395149"
FT   PROPEP          443..465
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395150"
FT   REGION          320..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        128
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        239
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   LIPID           442
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   465 AA;  46685 MW;  C3FA8A043EAED051 CRC64;
     MFTKTQILAL ALSIASAEAV SKGFNYGANK PDGTLKVQAD FEAEFRTAKN LETTSGFNSA
     RLYTMIQGTG STPISAIPAA IAEETTLLLG LWASGGNMDN EIAALKAAIN QYGDEFAKLV
     VGISVGSEDL YRNSEIGVQA NAGIGIEPEE LVSYIQRVRE AIAGTALSGA PIGHVDTWNA
     WTNGSNAAVA EAVDWLGFDG YPFFQNTMQN SIDDAKALFD ESVQKTKAVA GNKEVWITET
     GWPVSGDSQN LAIASVENAK QFWDEVGCPL FDNVNTWWYI LQDASGSSVP NPSFGIVGNT
     LSTTPLFDLS CSASSKKNSS SASASASGSS AQSTGFVSTT KPAASPSGSS GLGHGGSLGS
     SGSFSGGHYA GVGSSSVIAS PSATPSGSAV PGSSSGPGSS SGSASGSSSG FGSGAAADST
     SGTSTSGDST SSTSATPADF TGAGSRLSGS IFGAAMLVAA LAVAL
//