ID   GUN4_HYPJE              Reviewed;         344 AA.
AC   O14405;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Endoglucanase-4;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase IV;
DE   AltName: Full=Cellulase-61A;
DE            Short=Cel61A;
DE   AltName: Full=Endo-1,4-beta-glucanase IV;
DE            Short=EGIV;
DE   AltName: Full=Endoglucanase IV;
DE   AltName: Full=Endoglucanase-61A;
DE   Flags: Precursor;
GN   Name=cel61a; Synonyms=egl4;
OS   Hypocrea jecorina (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=ATCC 56765 / Rut C-30;
RX   PubMed=9370370; DOI=10.1111/j.1432-1033.1997.00584.x;
RA   Saloheimo M., Nakari-Setaelae T., Tenkanen M., Penttilae M.;
RT   "cDNA cloning of a Trichoderma reesei cellulase and demonstration of
RT   endoglucanase activity by expression in yeast.";
RL   Eur. J. Biochem. 249:584-591(1997).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11737205; DOI=10.1046/j.0014-2956.2001.02605.x;
RA   Karlsson J., Saloheimo M., Siika-aho M., Tenkanen M., Penttilae M.,
RA   Tjerneld F.;
RT   "Homologous expression and characterization of Cel61A (EG IV) of
RT   Trichoderma reesei.";
RL   Eur. J. Biochem. 268:6498-6507(2001).
RN   [3]
RP   INDUCTION.
RX   PubMed=12788920; DOI=10.1074/jbc.m304750200;
RA   Foreman P.K., Brown D., Dankmeyer L., Dean R., Diener S.,
RA   Dunn-Coleman N.S., Goedegebuur F., Houfek T.D., England G.J., Kelley A.S.,
RA   Meerman H.J., Mitchell T., Mitchinson C., Olivares H.A., Teunissen P.J.M.,
RA   Yao J., Ward M.;
RT   "Transcriptional regulation of biomass-degrading enzymes in the filamentous
RT   fungus Trichoderma reesei.";
RL   J. Biol. Chem. 278:31988-31997(2003).
CC   -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4
CC       glycosidic bonds, like in carboxymethylcellulose (CMC),
CC       hydroxyethylcellulose (HEC) and beta-glucan. May be involved in the
CC       degradation of complex natural cellulosic substrates.
CC       {ECO:0000269|PubMed:11737205}.
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         Evidence={ECO:0000269|PubMed:11737205, ECO:0000269|PubMed:9370370};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: By cellulose, cellobiose, lactose and sophorose.
CC       {ECO:0000269|PubMed:12788920, ECO:0000269|PubMed:9370370}.
CC   -!- PTM: May also be O-glycosylated.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 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; Y11113; CAA71999.1; -; mRNA.
DR   AlphaFoldDB; O14405; -.
DR   SMR; O14405; -.
DR   CAZy; AA9; Auxiliary Activities 9.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CLAE; PMO9A_TRIRE; -.
DR   VEuPathDB; FungiDB:TrQ_007365; -.
DR   OMA; GPCERVD; -.
DR   BioCyc; MetaCyc:MON-16504; -.
DR   BRENDA; 1.14.99.54; 6451.
DR   BRENDA; 1.14.99.56; 6451.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0008810; F:cellulase activity; IDA:UniProtKB.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IDA:UniProtKB.
DR   InterPro; IPR005103; AA9.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   Pfam; PF03443; AA9; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..344
FT                   /note="Endoglucanase-4"
FT                   /id="PRO_0000008032"
FT   DOMAIN          307..343
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          22..256
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255"
FT   REGION          257..307
FT                   /note="Linker"
FT                   /evidence="ECO:0000255"
FT   REGION          262..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        315..332
FT                   /evidence="ECO:0000250"
FT   DISULFID        326..342
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   344 AA;  35511 MW;  7FBF1C4AB705350C CRC64;
     MIQKLSNLLV TALAVATGVV GHGHINDIVI NGVWYQAYDP TTFPYESNPP IVVGWTAADL
     DNGFVSPDAY QNPDIICHKN ATNAKGHASV KAGDTILFQW VPVPWPHPGP IVDYLANCNG
     DCETVDKTTL EFFKIDGVGL LSGGDPGTWA SDVLISNNNT WVVKIPDNLA PGNYVLRHEI
     IALHSAGQAN GAQNYPQCFN IAVSGSGSLQ PSGVLGTDLY HATDPGVLIN IYTSPLNYII
     PGPTVVSGLP TSVAQGSSAA TATASATVPG GGSGPTSRTT TTARTTQASS RPSSTPPATT
     SAPAGGPTQT LYGQCGGSGY SGPTRCAPPA TCSTLNPYYA QCLN