EGLC_EMENI
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 25-MAY-2022, entry version 91.
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; 162425.CADANIAP00003968; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR EnsemblFungi; CBF73583; CBF73583; ANIA_07950.
DR EnsemblFungi; EAA59604; EAA59604; AN7950.2.
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; TNTWWYI; -.
DR OrthoDB; 966331at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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: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:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR SUPFAM; SSF51445; SSF51445; 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
