ID   GUN_PHACE               Reviewed;         242 AA.
AC   O97401; P81522;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
OS   Phaedon cochleariae (Mustard beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Phaedon.
OX   NCBI_TaxID=80249;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAA76931.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Larval gut {ECO:0000269|PubMed:10612046};
RX   PubMed=10612046; DOI=10.1016/s0965-1748(99)00104-6;
RA   Girard C., Jouanin L.;
RT   "Molecular cloning of cDNAs encoding a range of digestive enzymes from a
RT   phytophagous beetle, Phaedon cochleariae.";
RL   Insect Biochem. Mol. Biol. 29:1129-1142(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in larval carcasses and gut, and adult
CC       gut. {ECO:0000269|PubMed:10612046}.
CC   -!- DEVELOPMENTAL STAGE: Eggs, larvae and adult.
CC       {ECO:0000269|PubMed:10612046}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC       {ECO:0000255}.
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DR   EMBL; Y17907; CAA76931.1; -; mRNA.
DR   AlphaFoldDB; O97401; -.
DR   SMR; O97401; -.
DR   CAZy; GH45; Glycoside Hydrolase Family 45.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.40.10; -; 1.
DR   InterPro; IPR000334; Glyco_hydro_45.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   Pfam; PF02015; Glyco_hydro_45; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
DR   PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cellulose degradation; Digestion; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..242
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000147329"
FT   ACT_SITE        47
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P43316,
FT                   ECO:0000255|PROSITE-ProRule:PRU10069"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   242 AA;  25336 MW;  E57A9EC9DAE4379D CRC64;
     MQVIVLPLVF LATFATSGSL AAPDASPEIV PVDGGLSGYG TTTRYWDCCK PSCAWKENIN
     TPTMTPVQTC AIDGNTVVNA SVQSGCIGGS SYMCSNQQAF VVNSTLAFGF AAGSFTGGVD
     NNLCCSCMLL TFQGQLAGKQ FLVQITNTGG DLGSTSSIWP FPGGGVGIFT QGCHDQWTPR
     GAAGGDQYGG VYSVEQCSDL PEVLQPGCRF RFEFLENVSN PQVSFQQVQC PAEIVAISNC
     AL