ID ASPG_CAEEL Reviewed; 363 AA. AC Q21697; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 16-JUN-2009, entry version 57. DE RecName: Full=Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase; DE EC=3.5.1.26; DE AltName: Full=Glycosylasparaginase; DE AltName: Full=Aspartylglucosaminidase; DE Short=AGA; DE AltName: Full=N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase; DE Contains: DE RecName: Full=Glycosylasparaginase alpha chain; DE Contains: DE RecName: Full=Glycosylasparaginase beta chain; DE Flags: Precursor; GN ORFNames=R04B3.2; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides CC to the peptide of asparagine-linked glycoproteins (By similarity). CC -!- CATALYTIC ACTIVITY: N(4)-(beta-N-acetyl-D-glucosaminyl)-L- CC asparagine + H(2)O = N-acetyl-beta-D-glucosaminylamine + L- CC aspartate. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged CC as a dimer of alpha/beta heterodimers (By similarity). CC -!- SUBCELLULAR LOCATION: Lysosome (By similarity). CC -!- PTM: Autocleaved. Generates the alpha and beta subunits. The N- CC terminal residue of the beta subunit is thought to be responsible CC for the nucleophile hydrolase activity (By similarity). CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U50198; AAA91260.2; -; Genomic_DNA. DR PIR; T30965; T30965. DR RefSeq; NP_508448.1; -. DR UniGene; Cel.593; -. DR HSSP; P20933; 1APY. DR MEROPS; T02.001; -. DR Ensembl; R04B3.2; Caenorhabditis elegans. DR GeneID; 180550; -. DR KEGG; cel:R04B3.2; -. DR NMPDR; fig|6239.3.peg.22677; -. DR WormBase; WBGene00019867; R04B3.2. DR WormPep; R04B3.2; CE28745. DR OMA; Q21697; PLVLNTW. DR BRENDA; 3.5.1.26; 672. DR NextBio; 909836; -. DR ArrayExpress; Q21697; -. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparagina...; IEA:EC. DR InterPro; IPR000246; Peptidase_T2. DR PANTHER; PTHR10188; Peptidase_T2; 1. DR Pfam; PF01112; Asparaginase_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; KW Signal. FT SIGNAL 1 17 Potential. FT CHAIN 18 211 Glycosylasparaginase alpha chain (By FT similarity). FT /FTId=PRO_0000002343. FT CHAIN 212 363 Glycosylasparaginase beta chain (By FT similarity). FT /FTId=PRO_0000002344. FT ACT_SITE 212 212 Nucleophile (By similarity). FT CARBOHYD 15 15 N-linked (GlcNAc...) (Potential). FT CARBOHYD 118 118 N-linked (GlcNAc...) (Potential). FT CARBOHYD 196 196 N-linked (GlcNAc...) (Potential). FT CARBOHYD 336 336 N-linked (GlcNAc...) (Potential). FT DISULFID 161 177 By similarity. FT DISULFID 322 346 By similarity. SQ SEQUENCE 363 AA; 39359 MW; 4A34D1450AAB1BC7 CRC64; MRRFYIFLLL IPYINGTIND DSLPMVITTW GSDGFKKATK NAVDATLLGG RMFGLVEGLS TCEALQCDTT VGYGGSPDEN GETCLDSLVI DADGMRVGAV ANLHRIRDAA RVAWGVMNFT KHTLLVGESA TQFAKTLGFK EEDLSTEETK SWISKWKTEK CQPNFWKNVS PDPSSSCGPY KTNPLTKSMR YYSLVNQSDE AGYLVEKTNH DTIGMVVRDT ENIFSAGTSS NGARFKIPGR VGDSPIPGAG AYANKFGGAA ATGDGDVMMR FLPSFFAVTQ MELGTKPSKA AYKAITRILK VFPKFSGAVV AMNVKGRIGA SCANINKFGY NVAFQNGTVV TYSISCLKEV NSLKYLKEGI EFA //