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 05-DEC-2018, entry version 61. 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; OC Phasianidae; 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., RA Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., RA Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., RA Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C., RA Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., RA Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., RA Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., RA Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., RA Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., RA Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., RA van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., RA Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., RA 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., RA Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., RA Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., RA Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., RA Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., RA Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., RA King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., RA Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., RA Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., RA Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., RA Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., RA Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., RA 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., RA Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., RA Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., RA Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., RA Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., RA Mardis E.R., Wilson R.K.; RT "Sequence and comparative analysis of the chicken genome provide RT unique 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 RT of 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 CC glycoproteins by cleaving the beta-1,4-glycosidic bond in the CC N,N'-diacetylchitobiose core. Involved in the processing of free CC oligosaccharides in the cytosol. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of the N,N'-diacetylchitobiosyl unit in CC high-mannose glycopeptides and glycoproteins containing the CC -(Man(GlcNAc)(2))Asn-structure. One N-acetyl-D-glucosamine CC residue remains attached to the protein, the rest of the CC oligosaccharide is released intact.; EC=3.2.1.96; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000305|PubMed:12114544}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 85 family. CC {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 ProteinModelPortal; P0C7A1; -. DR STRING; 9031.ENSGALP00000019265; -. DR ChEMBL; CHEMBL1075083; -. DR PaxDb; P0C7A1; -. DR PRIDE; P0C7A1; -. DR eggNOG; KOG2331; Eukaryota. DR eggNOG; COG4724; LUCA. DR HOGENOM; HOG000082678; -. DR HOVERGEN; HBG107848; -. DR InParanoid; P0C7A1; -. DR PhylomeDB; P0C7A1; -. DR Proteomes; UP000000539; Unplaced. 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:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0051672; P:catabolism by organism of cell wall peptidoglycan in other organism; TAS:AgBase. DR GO; GO:0006517; P:protein deglycosylation; IBA:GO_Central. DR Gene3D; 2.60.120.260; -; 1. DR Gene3D; 2.60.120.40; -; 1. DR InterPro; IPR001073; C1q_dom. DR InterPro; IPR032979; ENGase. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR005201; Glyco_hydro_85. DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom. DR PANTHER; PTHR13246; PTHR13246; 1. DR Pfam; PF00386; C1q; 1. DR Pfam; PF03644; Glyco_hydro_85; 1. DR SUPFAM; SSF49842; SSF49842; 1. DR PROSITE; PS50871; C1Q; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Direct protein sequencing; Glycosidase; KW Hydrolase; Reference proteome. FT CHAIN 1 728 Cytosolic endo-beta-N- FT acetylglucosaminidase. FT /FTId=PRO_0000328869. FT DOMAIN 287 381 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 //