ID   ENASE_DANRE             Reviewed;         713 AA.
AC   A1L251;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Cytosolic endo-beta-N-acetylglucosaminidase;
DE            Short=ENGase;
DE            EC=3.2.1.96;
GN   Name=engase; ORFNames=zgc:158649;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoglycosidase that releases N-glycans from glycoproteins by
CC       cleaving the beta-1,4-glycosidic bond in the N,N'-diacetylchitobiose
CC       core. Involved in the processing of free oligosaccharides in the
CC       cytosol (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-
CC         mannose glycopeptides and glycoproteins containing the
CC         -[Man(GlcNAc)2]Asn- structure. One N-acetyl-D-glucosamine residue
CC         remains attached to the protein, the rest of the oligosaccharide is
CC         released intact.; EC=3.2.1.96;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 85 family. {ECO:0000305}.
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DR   EMBL; BC129351; AAI29352.1; -; mRNA.
DR   RefSeq; NP_001074047.2; NM_001080578.2.
DR   AlphaFoldDB; A1L251; -.
DR   SMR; A1L251; -.
DR   STRING; 7955.ENSDARP00000005952; -.
DR   CAZy; GH85; Glycoside Hydrolase Family 85.
DR   PaxDb; A1L251; -.
DR   PeptideAtlas; A1L251; -.
DR   PRIDE; A1L251; -.
DR   GeneID; 561239; -.
DR   KEGG; dre:561239; -.
DR   CTD; 64772; -.
DR   ZFIN; ZDB-GENE-070112-1332; engase.
DR   eggNOG; KOG2331; Eukaryota.
DR   InParanoid; A1L251; -.
DR   OrthoDB; 722800at2759; -.
DR   Reactome; R-DRE-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   PRO; PR:A1L251; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006517; P:protein deglycosylation; IBA:GO_Central.
DR   InterPro; IPR032979; ENGase.
DR   InterPro; IPR005201; Glyco_hydro_85.
DR   PANTHER; PTHR13246; PTHR13246; 1.
DR   Pfam; PF03644; Glyco_hydro_85; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..713
FT                   /note="Cytosolic endo-beta-N-acetylglucosaminidase"
FT                   /id="PRO_0000328870"
FT   DOMAIN          270..362
FT                   /note="BRCT"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  80255 MW;  C168C63E9C587DED CRC64;
     MIARKRKSNG SETTSGKIPK DDVSSESCLD QPADESVHEV VTFEPSTLPS VHYDPDTTEP
     ISCSLKSLDE LLSWKRNEAS IFNVSSVPLA SRYPPLESCP RRTLVSHDMM GGYLEDRFIQ
     GAEVETPYAF YHWEYIDIFN YFSHQMVTIP PAVWTNAAHR HGVLSIGTFI TEWTDGAKTC
     EAFLADEESY RAAADKLVQI SHCNGFDGWL INIENELSET AVNNTGPFLR YLTDQMHERV
     PGSVVIWYDS VLKDGKLLWQ NELNDNNRMF FDACDGFFTN YNWTEQSLEG MKSYAAAQGR
     FADIYVGVDV FARGKVIGGK YETNKALELI RKYDLSTAIF APDWVYECHE KADFRQNQDK
     FWSLLSDFLY IHRPSSNLPF VSSFCQGFGK SLYWRGKVET ERSWFNLHAQ EIQPLYLSES
     FGNGGWLRTR GCSEDAWIGG SSLMLEGMIP SGLSDVCARI FSLHVPLAAR TFVSFVFKPP
     VGVKVSLELK TIDGPLCTFD GTEEIASRSV FPEALAESNQ LVEQFAQNCG QWASDGWATR
     CFLLKMIGCS LREVCIRVSR DGGDEDINFN CRIGEIMLLD ADNLQAPLQS VEGICVNDVV
     WQTGVLKGDG HTLKVLLNAT LRWQYPTRQV RHFRIHWRHL RGPDPRIPSG PLTLIGRSYS
     ALYRVVELEV PAAPGLIELV VEPVSKEGFS VPEAQWGRQT LSYSQSPSGN PSH