ENASE_MOUSE
ID ENASE_MOUSE Reviewed; 734 AA.
AC Q8BX80; Q3TK58; Q8BJF1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytosolic endo-beta-N-acetylglucosaminidase;
DE Short=ENGase;
DE EC=3.2.1.96;
GN Name=Engase;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Eye, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BX80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BX80-2; Sequence=VSP_039763, VSP_039764;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 85 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39149.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AK048667; BAC33415.1; -; mRNA.
DR EMBL; AK167142; BAE39287.1; -; mRNA.
DR EMBL; AK084254; BAC39149.1; ALT_SEQ; mRNA.
DR EMBL; AL591075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120924; AAI20925.1; -; mRNA.
DR CCDS; CCDS25704.1; -. [Q8BX80-1]
DR RefSeq; NP_766161.1; NM_172573.2. [Q8BX80-1]
DR AlphaFoldDB; Q8BX80; -.
DR SMR; Q8BX80; -.
DR STRING; 10090.ENSMUSP00000117538; -.
DR CAZy; GH85; Glycoside Hydrolase Family 85.
DR iPTMnet; Q8BX80; -.
DR PhosphoSitePlus; Q8BX80; -.
DR EPD; Q8BX80; -.
DR MaxQB; Q8BX80; -.
DR PaxDb; Q8BX80; -.
DR PeptideAtlas; Q8BX80; -.
DR PRIDE; Q8BX80; -.
DR ProteomicsDB; 277872; -. [Q8BX80-1]
DR Antibodypedia; 9971; 78 antibodies from 20 providers.
DR Ensembl; ENSMUST00000043447; ENSMUSP00000126050; ENSMUSG00000033857. [Q8BX80-2]
DR Ensembl; ENSMUST00000135383; ENSMUSP00000117538; ENSMUSG00000033857. [Q8BX80-1]
DR Ensembl; ENSMUST00000172279; ENSMUSP00000130097; ENSMUSG00000033857. [Q8BX80-2]
DR GeneID; 217364; -.
DR KEGG; mmu:217364; -.
DR UCSC; uc007mpi.1; mouse. [Q8BX80-1]
DR CTD; 64772; -.
DR MGI; MGI:2443788; Engase.
DR VEuPathDB; HostDB:ENSMUSG00000033857; -.
DR eggNOG; KOG2331; Eukaryota.
DR GeneTree; ENSGT00390000018512; -.
DR HOGENOM; CLU_015297_0_0_1; -.
DR InParanoid; Q8BX80; -.
DR OMA; SQVRWQP; -.
DR OrthoDB; 722800at2759; -.
DR PhylomeDB; Q8BX80; -.
DR TreeFam; TF314391; -.
DR BRENDA; 3.2.1.96; 3474.
DR Reactome; R-MMU-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR BioGRID-ORCS; 217364; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Engase; mouse.
DR PRO; PR:Q8BX80; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BX80; protein.
DR Bgee; ENSMUSG00000033857; Expressed in ectoplacental cone and 128 other tissues.
DR ExpressionAtlas; Q8BX80; baseline and differential.
DR Genevisible; Q8BX80; MM.
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; IDA:MGI.
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 Reference proteome.
FT CHAIN 1..734
FT /note="Cytosolic endo-beta-N-acetylglucosaminidase"
FT /id="PRO_0000328868"
FT DOMAIN 281..375
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFI3"
FT VAR_SEQ 41..45
FT /note="INEDQ -> CARLG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039763"
FT VAR_SEQ 46..734
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039764"
SQ SEQUENCE 734 AA; 82945 MW; AB95B9B7411F2EC1 CRC64;
METSSVLTRG AARQRSPAAP EKQARDQTER RPGRRRQGRR INEDQEEEAV FREVVSFTPD
PLPARYYDKD TTRPISFYLS TLEELLAWTP LMEDGFNVAL EPLVCRRPPL SSPRPRTLLC
HDMMGGYLED RFIQGSEVQN PYSFYHWQYI DIFVYFSHHT VTIPPVCWTN AAHRHGVCVL
GTFITEWQEG GRLCEAFLAG DEPSFQAVAD RLVQIAQFFR FDGWLINIEN SLTPAAVRNT
PLFLQYLTAQ LHQQVPGGLV LWYDSVVQSG QLKWQDELND QNRVFFDSCD GFFTNYNWRE
DHLQRMVAQA GERLADVYVG VDVFARSNVV GGRFDTDKSL ELIRKHGFSA ALFAPGWVYE
CLEKSDFFQN QDKFWSLLER FLPTHSICSL PFVTSFCLGL GTRRVCYGKE QAVGPWYHPS
AQETQPLFGE HKLAGDSRGW VKTHCCLTDA WHGGSSLLLR GLIPPEVDSV AVRLFSLHIP
VPPKVFLSMV YKFEGSTDVQ VALELTTGDA SSCHVGGMLV LNETGSRHSP RPLRVPPTRL
ARWASSCGQQ LSGGWIQRCY EVNLRGCLLQ DLLVSFSRPP GSREEESFIC RLGEIQVVDA
SSLLAPLPRV QNVTISQIRW LPLITGSEGL PTRLLLSCTL HWSYLLLRAR CFRIHCWKRT
GSSSSVAESP ETEKPTFLGL AFANQYRVVD LAVEAAGFGQ DGRVEFLVEP VPREGFLVPQ
AEWGKAVLLF SVPQ
