ID   ENASE_CHICK             Reviewed;         728 AA.
AC   P0C7A1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   08-NOV-2023, entry version 75.
DE   RecName: Full=Cytosolic endo-beta-N-acetylglucosaminidase;
DE            Short=ENGase;
DE            EC=3.2.1.96;
GN   Name=ENGASE;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 51-76, AND SUBCELLULAR LOCATION.
RX   PubMed=12114544; DOI=10.1073/pnas.152333599;
RA   Suzuki T., Yano K., Sugimoto S., Kitajima K., Lennarz W.J., Inoue S.,
RA   Inoue Y., Emori Y.;
RT   "Endo-beta-N-acetylglucosaminidase, an enzyme involved in processing of
RT   free oligosaccharides in the cytosol.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9691-9696(2002).
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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-
CC         D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-
CC         [protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-
CC         beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-
CC         asparaginyl-[protein]; Xref=Rhea:RHEA:73067, Rhea:RHEA-COMP:12603,
CC         Rhea:RHEA-COMP:18176, ChEBI:CHEBI:15377, ChEBI:CHEBI:132248,
CC         ChEBI:CHEBI:192714, ChEBI:CHEBI:192715; EC=3.2.1.96;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:12114544}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 85 family. {ECO:0000305}.
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DR   AlphaFoldDB; P0C7A1; -.
DR   SMR; P0C7A1; -.
DR   STRING; 9031.ENSGALP00000019265; -.
DR   ChEMBL; CHEMBL1075083; -.
DR   PaxDb; 9031-ENSGALP00000019265; -.
DR   VEuPathDB; HostDB:geneid_430102; -.
DR   eggNOG; KOG2331; Eukaryota.
DR   InParanoid; P0C7A1; -.
DR   PhylomeDB; P0C7A1; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR   GO; GO:0005764; C:lysosome; TAS:AgBase.
DR   GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IDA:AgBase.
DR   GO; GO:0016787; F:hydrolase activity; TAS:AgBase.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd06547; GH85_ENGase; 1.
DR   Gene3D; 2.60.120.40; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR032979; ENGase.
DR   InterPro; IPR005201; Glyco_hydro_85.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   PANTHER; PTHR13246:SF1; CYTOSOLIC ENDO-BETA-N-ACETYLGLUCOSAMINIDASE; 1.
DR   PANTHER; PTHR13246; ENDO BETA N-ACETYLGLUCOSAMINIDASE; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF03644; Glyco_hydro_85; 1.
DR   SUPFAM; SSF49842; TNF-like; 1.
DR   PROSITE; PS50871; C1Q; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..728
FT                   /note="Cytosolic endo-beta-N-acetylglucosaminidase"
FT                   /id="PRO_0000328869"
FT   DOMAIN          287..381
FT                   /note="BRCT"
SQ   SEQUENCE   728 AA;  80889 MW;  CAA311512C095918 CRC64;
     MQSQSVMLEL REQDEVWVRL YKGERENAVF SDEYDTYITF SGHLINFQPA AEPLGTTVLH
     AAVDTRPQPA RYFDTGTTEP VSFFLSGLEE LLAWHPSSDD EFNVCAVPLA QRQPPLHSRR
     PRTLLCHDMR GGYLEDRFIQ GSATRNPYVF YHWRYVDIFV YFSHHTVTIP PVCWTNAAHR
     NGVPVLGTFI TEWADGEKLC EAFLAGGEDA YRAVSHQLAR IAQHYRFDGW LINIENALSA
     AAVGNLSPFL RHLTAEVHGA VPGGLVIWYD SILESGTLRW QNELNQQNRV FFDACDGLFV
     NYNWKEEHLE RTRELAGQRH ADVYIGVDVF ARGDVVGGGF DTNKSLSLIR KHGLSAAIFA
     PGWVYKHLGE ENFLLNEDKF WGLLEDYLPT HSICTLPLAT SFSVGMGTGM FLAGKEEEAG
     PWYNLSAQEI QPLYPERRGW LSTSCCLQDA WCGGSSLRVQ GTIPPGEERV AIRLSLWVDL
     GSSGFSLSIC GTLASGPHRD DFTVALELTT WHSSRCHDGT VTVLPSEDEP HGRHHPHLLP
     APPPALSRML AACSHGAQGW TSRCYEQELR GCSLRDLSLL VSRQQASPQE TSFSCLLGEL
     RVLDAGSMAA SPPQVQSLTA SQLWWQDGPS AEQLSLSLTL RWAFPPGRAA CFRVLSQGAR
     CHRAQPAQPQ LLGLAHGCQY RAVGLAVPRP APGQSCQLEL LVEPVLPSEL PVGPERWGRL
     LLVYSEPA
//