ID Q08B23_XENLA Unreviewed; 635 AA.
AC Q08B23;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase {ECO:0000256|ARBA:ARBA00018546};
DE EC=3.5.1.52 {ECO:0000256|ARBA:ARBA00012158};
DE AltName: Full=N-glycanase 1 {ECO:0000256|ARBA:ARBA00029604};
DE AltName: Full=Peptide:N-glycanase {ECO:0000256|ARBA:ARBA00032901};
GN Name=ngly1.S {ECO:0000313|RefSeq:NP_001116357.1,
GN ECO:0000313|Xenbase:XB-GENE-963944};
GN Synonyms=LOC733299 {ECO:0000313|EMBL:AAI24907.1}, ngly1
GN {ECO:0000313|RefSeq:NP_001116357.1,
GN ECO:0000313|Xenbase:XB-GENE-963944};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI24907.1};
RN [1] {ECO:0000313|RefSeq:NP_001116357.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI24907.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000313|EMBL:AAI24907.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001116357.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Specifically deglycosylates the denatured form of N-linked
CC glycoproteins in the cytoplasm and assists their proteasome-mediated
CC degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the
CC glycan and the amide side chain of Asn, converting Asn to Asp. Prefers
CC proteins containing high-mannose over those bearing complex type
CC oligosaccharides. Can recognize misfolded proteins in the endoplasmic
CC reticulum that are exported to the cytosol to be destroyed and
CC deglycosylate them, while it has no activity toward native proteins.
CC Deglycosylation is a prerequisite for subsequent proteasome-mediated
CC degradation of some, but not all, misfolded glycoproteins.
CC {ECO:0000256|ARBA:ARBA00024870}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine
CC residue in which the glucosamine residue may be further glycosylated,
CC to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a
CC peptide containing an aspartate residue.; EC=3.5.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001650};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000256|ARBA:ARBA00009390, ECO:0000256|PROSITE-
CC ProRule:PRU00731}.
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DR EMBL; BC124906; AAI24907.1; -; mRNA.
DR RefSeq; NP_001116357.1; NM_001122885.1.
DR STRING; 8355.Q08B23; -.
DR PaxDb; 8355-Q08B23; -.
DR DNASU; 733299; -.
DR GeneID; 733299; -.
DR KEGG; xla:733299; -.
DR AGR; Xenbase:XB-GENE-963944; -.
DR CTD; 733299; -.
DR Xenbase; XB-GENE-963944; ngly1.S.
DR OMA; WANVFTL; -.
DR OrthoDB; 5051at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 733299; Expressed in pancreas and 19 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006516; P:glycoprotein catabolic process; IEA:InterPro.
DR CDD; cd10459; PUB_PNGase; 1.
DR Gene3D; 1.20.58.2190; -; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 3.10.620.30; -; 1.
DR Gene3D; 2.60.120.1020; Peptide N glycanase, PAW domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR038680; PAW_sf.
DR InterPro; IPR006588; Peptide_N_glycanase_PAW_dom.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR018997; PUB_domain.
DR InterPro; IPR002931; Transglutaminase-like.
DR PANTHER; PTHR12143; PEPTIDE N-GLYCANASE PNGASE -RELATED; 1.
DR PANTHER; PTHR12143:SF19; PEPTIDE-N(4)-(N-ACETYL-BETA-GLUCOSAMINYL)ASPARAGINE AMIDASE; 1.
DR Pfam; PF04721; PAW; 1.
DR Pfam; PF09409; PUB; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00613; PAW; 1.
DR SMART; SM00580; PUG; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF143503; PUG domain-like; 1.
DR PROSITE; PS51398; PAW; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 435..635
FT /note="PAW"
FT /evidence="ECO:0000259|PROSITE:PS51398"
FT REGION 103..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 72546 MW; 6F3C0DC813EB373B CRC64;
MAAQESPAVD ELCQNERQEF LDASQLLLTY ADNILRSPNE EKYRSIRIGN TAFSTRLLPV
RGAIECLFEM GFEEEETHLV FPKMASVEKL RNVRDHIAIE RNKRMSAANP TPPATSSTPP
AFSRTPVPNP VPPSIPLPAT EDISNFLASE VRYLKTLQSN SQHVLIYEEP EIQQRALQEI
PVSDLKTRAQ KKLIEAKSLD SDTSVNLEDF LLLELLRWFK QDFFQWVNSL PCSHCGGETQ
ARDALSPSDE DLRWGANRVE NHYCEKCKHS NRFPRYNHPE KLLETRRGRC GEWANCFTLC
CRALGFEARY VWDSTDHVWT EVYSSSQNRW LHCDPCENAC DKPLLYEVGW GKKLSYIIAF
SKDEVVDVTW RYSCKHEDVI ARRKEVRESW LRETIVGLNK MRQQSVPEHR KQELLGRLIV
ELVEFMSPKT TKPGELGGRV SGSVAWRVAR GETSLQSTKS VIFIPSESEK TSKRFHLQYN
VVEDTYTRTS NNNVVIAGWE NGAWKAESIC RKVESDWKMV YLARTEGSSS AAISWKIECA
SAGLQIESIS VRTSSQTFHS GKIIWKLSSP EAEVEVNSDT NFHSYPEFLN ASEVELKAEL
CDGDGNTAWQ HTQIFRQTLD CKENSLEIII MLKDA
//