Reviewed, UniProtKB/Swiss-Prot O14405 (GUN4_TRIRE)

Names and origin

Protein names

Recommended name:
    Endoglucanase-4
    EC=3.2.1.4
Alternative name(s):
    Endoglucanase IV
    Endo-1,4-beta-glucanase IV
      Short name=EGIV
    Cellulase IV
    Endoglucanase-61A
    Cellulase-61A
      Short name=Cel61A

Gene names

Name:	cel61a
Synonyms:	egl4

Organism

Trichoderma reesei (Hypocrea jecorina)

Taxonomic identifier

51453 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. May be involved in the degradation of complex natural cellulosic substrates. Ref.2
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Ref.2 Ref.1
Subcellular location	Secreted.
Induction	By cellulose, cellobiose, lactose and sophorose. Ref.1 Ref.3
Post-translational modification	May also be O-glycosylated.
Sequence similarities	Belongs to the glycosyl hydrolase 61 family. Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	cellulose catabolic process Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	extracellular region Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	cellulase activity Ref.1 Inferred from direct assay. Source: UniProtKB cellulose binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 344	323	Endoglucanase-4		PRO_0000008032
Regions
	Domain	307 – 343	37	CBM1
	Region	22 – 256	235	Catalytic Potential
	Region	257 – 307	51	Linker Potential
Amino acid modifications
	Glycosylation	80	1	N-linked (GlcNAc...) Potential
	Glycosylation	158	1	N-linked (GlcNAc...) Potential
	Disulfide bond	315 ↔ 332		By similarity
	Disulfide bond	326 ↔ 342		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O14405-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 7FBF1C4AB705350C	FASTA	344	35,511
	10 20 30 40 50 60 MIQKLSNLLV TALAVATGVV GHGHINDIVI NGVWYQAYDP TTFPYESNPP IVVGWTAADL 70 80 90 100 110 120 DNGFVSPDAY QNPDIICHKN ATNAKGHASV KAGDTILFQW VPVPWPHPGP IVDYLANCNG 130 140 150 160 170 180 DCETVDKTTL EFFKIDGVGL LSGGDPGTWA SDVLISNNNT WVVKIPDNLA PGNYVLRHEI 190 200 210 220 230 240 IALHSAGQAN GAQNYPQCFN IAVSGSGSLQ PSGVLGTDLY HATDPGVLIN IYTSPLNYII 250 260 270 280 290 300 PGPTVVSGLP TSVAQGSSAA TATASATVPG GGSGPTSRTT TTARTTQASS RPSSTPPATT 310 320 330 340 SAPAGGPTQT LYGQCGGSGY SGPTRCAPPA TCSTLNPYYA QCLN

References

[1]	"cDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast." Saloheimo M., Nakari-Setaelae T., Tenkanen M., Penttilae M. Eur. J. Biochem. 249:584-591(1997) [PubMed: 9370370] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, INDUCTION. Strain: QM9414 / Rut C-30.
[2]	"Homologous expression and characterization of Cel61A (EG IV) of Trichoderma reesei." Karlsson J., Saloheimo M., Siika-aho M., Tenkanen M., Penttilae M., Tjerneld F. Eur. J. Biochem. 268:6498-6507(2001) [PubMed: 11737205] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[3]	"Transcriptional regulation of biomass-degrading enzymes in the filamentous fungus Trichoderma reesei." Foreman P.K., Brown D., Dankmeyer L., Dean R., Diener S., Dunn-Coleman N.S., Goedegebuur F., Houfek T.D., England G.J., Kelley A.S., Meerman H.J., Mitchell T., Mitchinson C., Olivares H.A., Teunissen P.J.M., Yao J., Ward M. J. Biol. Chem. 278:31988-31997(2003) [PubMed: 12788920] [Abstract] Cited for: INDUCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y11113 mRNA. Translation: CAA71999.1.
3D structure databases
SMR	O14405. Positions 308-343.
ModBase	Search...
Protein family/group databases
CAZy	CBM1. Carbohydrate-Binding Module Family 1. GH61. Glycoside Hydrolase Family 61.
Enzyme and pathway databases
BRENDA	3.2.1.4. 280374.
Family and domain databases
InterPro	IPR000254. Cellulose-bd_dom_fun. IPR005103. Glyco_hydro_61. [Graphical view]
Pfam	PF00734. CBM_1. 1 hit. PF03443. Glyco_hydro_61. 1 hit. [Graphical view]
ProDom	PD001821. CBD_fun. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00236. fCBD. 1 hit. [Graphical view]
PROSITE	PS00562. CBM1_1. 1 hit. PS51164. CBM1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUN4_TRIRE

Accession

Primary (citable) accession number: O14405

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	January 1, 1998
Last modified:	January 19, 2010
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)