ENASE_HUMAN
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 03-AUG-2022, entry version 131.
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=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 -!- 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};
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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; 10.
DR IntAct; Q8NFI3; 3.
DR STRING; 9606.ENSP00000462333; -.
DR BindingDB; Q8NFI3; -.
DR ChEMBL; CHEMBL5172; -.
DR CAZy; GH85; Glycoside Hydrolase Family 85.
DR GlyGen; Q8NFI3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NFI3; -.
DR PhosphoSitePlus; Q8NFI3; -.
DR BioMuta; ENGASE; -.
DR DMDM; 74715557; -.
DR EPD; Q8NFI3; -.
DR jPOST; Q8NFI3; -.
DR MassIVE; Q8NFI3; -.
DR MaxQB; Q8NFI3; -.
DR PaxDb; Q8NFI3; -.
DR PeptideAtlas; Q8NFI3; -.
DR PRIDE; Q8NFI3; -.
DR ProteomicsDB; 73312; -. [Q8NFI3-1]
DR ProteomicsDB; 73313; -. [Q8NFI3-2]
DR ProteomicsDB; 73314; -. [Q8NFI3-3]
DR Antibodypedia; 9971; 78 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 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; 722800at2759; -.
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; 12 hits in 1080 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 193 other 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:0006517; P:protein deglycosylation; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; TAS:Reactome.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR032979; ENGase.
DR InterPro; IPR005201; Glyco_hydro_85.
DR PANTHER; PTHR13246; PTHR13246; 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
