ID ENASE_HUMAN Reviewed; 743 AA. AC Q8NFI3; Q659F0; Q8TB86; Q9H6U4; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 24-JAN-2024, entry version 137. DE RecName: Full=Cytosolic endo-beta-N-acetylglucosaminidase; DE Short=ENGase; DE EC=3.2.1.96; GN Name=ENGASE; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY. 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). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Hepatoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 224-680 (ISOFORM 3). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-743 (ISOFORM 1), AND VARIANT RP ASN-596. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). 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. {ECO:0000269|PubMed:12114544}. 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:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8NFI3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NFI3-2; Sequence=VSP_032836, VSP_032837; CC Name=3; CC IsoId=Q8NFI3-3; Sequence=VSP_032835, VSP_032838; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in CC thymus and spleen. {ECO:0000269|PubMed:12114544}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 85 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH24213.2; Type=Frameshift; Evidence={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; AF512564; AAM80487.1; -; mRNA. DR EMBL; AK025518; BAB15158.1; -; mRNA. DR EMBL; CH471099; EAW89562.1; -; Genomic_DNA. DR EMBL; AL110283; CAH56405.1; -; mRNA. DR EMBL; BC024213; AAH24213.2; ALT_FRAME; mRNA. DR CCDS; CCDS42394.1; -. [Q8NFI3-1] DR RefSeq; NP_001036038.1; NM_001042573.2. [Q8NFI3-1] DR AlphaFoldDB; Q8NFI3; -. DR SMR; Q8NFI3; -. DR BioGRID; 122283; 11. DR IntAct; Q8NFI3; 3. DR STRING; 9606.ENSP00000462333; -. DR BindingDB; Q8NFI3; -. DR ChEMBL; CHEMBL5172; -. DR CAZy; GH85; Glycoside Hydrolase Family 85. DR GlyCosmos; Q8NFI3; 1 site, 1 glycan. DR GlyGen; Q8NFI3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8NFI3; -. DR PhosphoSitePlus; Q8NFI3; -. DR SwissPalm; Q8NFI3; -. DR BioMuta; ENGASE; -. DR DMDM; 74715557; -. DR EPD; Q8NFI3; -. DR jPOST; Q8NFI3; -. DR MassIVE; Q8NFI3; -. DR MaxQB; Q8NFI3; -. DR PaxDb; 9606-ENSP00000462333; -. DR PeptideAtlas; Q8NFI3; -. DR ProteomicsDB; 73312; -. [Q8NFI3-1] DR ProteomicsDB; 73313; -. [Q8NFI3-2] DR ProteomicsDB; 73314; -. [Q8NFI3-3] DR Pumba; Q8NFI3; -. DR Antibodypedia; 9971; 91 antibodies from 20 providers. DR DNASU; 64772; -. DR Ensembl; ENST00000311595.14; ENSP00000308158.10; ENSG00000167280.17. [Q8NFI3-3] DR Ensembl; ENST00000579016.6; ENSP00000462333.1; ENSG00000167280.17. [Q8NFI3-1] DR GeneID; 64772; -. DR KEGG; hsa:64772; -. DR MANE-Select; ENST00000579016.6; ENSP00000462333.1; NM_001042573.3; NP_001036038.1. DR UCSC; uc002jwv.5; human. [Q8NFI3-1] DR AGR; HGNC:24622; -. DR CTD; 64772; -. DR DisGeNET; 64772; -. DR GeneCards; ENGASE; -. DR HGNC; HGNC:24622; ENGASE. DR HPA; ENSG00000167280; Low tissue specificity. DR MIM; 611898; gene. DR neXtProt; NX_Q8NFI3; -. DR OpenTargets; ENSG00000167280; -. DR PharmGKB; PA164719123; -. DR VEuPathDB; HostDB:ENSG00000167280; -. DR eggNOG; KOG2331; Eukaryota. DR GeneTree; ENSGT00390000018512; -. DR HOGENOM; CLU_015297_0_0_1; -. DR InParanoid; Q8NFI3; -. DR OMA; SQVRWQP; -. DR OrthoDB; 1437624at2759; -. DR PhylomeDB; Q8NFI3; -. DR TreeFam; TF314391; -. DR BRENDA; 3.2.1.96; 2681. DR PathwayCommons; Q8NFI3; -. DR Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle. DR SignaLink; Q8NFI3; -. DR BioGRID-ORCS; 64772; 13 hits in 1158 CRISPR screens. DR ChiTaRS; ENGASE; human. DR GenomeRNAi; 64772; -. DR Pharos; Q8NFI3; Tchem. DR PRO; PR:Q8NFI3; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q8NFI3; Protein. DR Bgee; ENSG00000167280; Expressed in mucosa of transverse colon and 195 other cell types or tissues. DR ExpressionAtlas; Q8NFI3; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. 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; IDA:FlyBase. DR GO; GO:0006457; P:protein folding; TAS:Reactome. DR CDD; cd06547; GH85_ENGase; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR032979; ENGase. DR InterPro; IPR005201; Glyco_hydro_85. DR PANTHER; PTHR13246:SF1; CYTOSOLIC ENDO-BETA-N-ACETYLGLUCOSAMINIDASE; 1. DR PANTHER; PTHR13246; ENDO BETA N-ACETYLGLUCOSAMINIDASE; 1. DR Pfam; PF03644; Glyco_hydro_85; 1. DR PROSITE; PS50172; BRCT; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cytoplasm; Glycosidase; Hydrolase; KW Phosphoprotein; Reference proteome. FT CHAIN 1..743 FT /note="Cytosolic endo-beta-N-acetylglucosaminidase" FT /id="PRO_0000328867" FT DOMAIN 291..383 FT /note="BRCT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT REGION 1..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 33..55 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 66 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 347..406 FT /note="SLELIRKHGFSVALFAPGWVYECLEKKDFFQNQDKFWGRLERYLPTHSICSL FT PFVTSFCL -> VGGGFRPRASGPVPPLGPHFLMDLPFPSAPQRNDSSCSSQSGDPVAL FT RNRCPAPAKLCPH (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_032835" FT VAR_SEQ 364..377 FT /note="GWVYECLEKKDFFQ -> SCSVFPGVGNLLCC (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_032836" FT VAR_SEQ 378..743 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_032837" FT VAR_SEQ 407..743 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_032838" FT VARIANT 596 FT /note="S -> N (in dbSNP:rs4789879)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_060188" FT VARIANT 731 FT /note="E -> K (in dbSNP:rs11871357)" FT /id="VAR_060189" FT CONFLICT 152 FT /note="F -> L (in Ref. 2; BAB15158)" FT /evidence="ECO:0000305" FT CONFLICT 224 FT /note="T -> A (in Ref. 4; CAH56405)" FT /evidence="ECO:0000305" SQ SEQUENCE 743 AA; 83987 MW; 384DA533AE549FC5 CRC64; MEAAAVTVTR SATRRRRRQL QGLAAPEAGT QEEQEDQEPR PRRRRPGRSI KDEEEETVFR EVVSFSPDPL PVRYYDKDTT KPISFYLSSL EELLAWKPRL EDGFNVALEP LACRQPPLSS QRPRTLLCHD MMGGYLDDRF IQGSVVQTPY AFYHWQCIDV FVYFSHHTVT IPPVGWTNTA HRHGVCVLGT FITEWNEGGR LCEAFLAGDE RSYQAVADRL VQITQFFRFD GWLINIENSL SLAAVGNMPP FLRYLTTQLH RQVPGGLVLW YDSVVQSGQL KWQDELNQHN RVFFDSCDGF FTNYNWREEH LERMLGQAGE RRADVYVGVD VFARGNVVGG RFDTDKSLEL IRKHGFSVAL FAPGWVYECL EKKDFFQNQD KFWGRLERYL PTHSICSLPF VTSFCLGMGA RRVCYGQEEA VGPWYHLSAQ EIQPLFGEHR LGGDGRGWVR THCCLEDAWH GGSSLLVRGV IPPEVGNVAV RLFSLQAPVP PKIYLSMVYK LEGPTDVTVA LELTTGDAGS CHIGGISVLN AETSSRHSLR PLRVPPTKLA RWVGRCGRQL SGGWVQHCYE VSLRGCLLLD LLVCFSRPPG SREEESFTCR LGEIQVVDAA SLLAPLPQVQ AVTISHIRWQ PSASEREGPP ALLQLSCTLH WSFLLSQVRC FRIHCWGGMS DDSPGRELPR PEMPMFLGLA FATQYRIVDL LVEAAGPGQD RRMEFLVEPV PKEGFRVPQA EWGRAVLLYS APA //