ID A0A1L8FWC2_XENLA Unreviewed; 635 AA.
AC A0A1L8FWC2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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.L {ECO:0000313|RefSeq:XP_018122949.1,
GN ECO:0000313|Xenbase:XB-GENE-17334231};
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|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018122949.1};
RN [1] {ECO:0000313|RefSeq:XP_018122949.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018122949.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018122949.1};
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 RefSeq; XP_018122949.1; XM_018267460.2.
DR AlphaFoldDB; A0A1L8FWC2; -.
DR STRING; 8355.A0A1L8FWC2; -.
DR PaxDb; 8355-A0A1L8FWC2; -.
DR GeneID; 108718927; -.
DR KEGG; xla:108718927; -.
DR AGR; Xenbase:XB-GENE-17334231; -.
DR CTD; 108718927; -.
DR Xenbase; XB-GENE-17334231; ngly1.L.
DR OMA; DLQDVTW; -.
DR OrthoDB; 5051at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 108718927; Expressed in blastula 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 3: Inferred from homology;
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}.
SQ SEQUENCE 635 AA; 72530 MW; 22AF55C2E8B28D4D CRC64;
MATQDSSAVA ELCQNKRQEF LDASQLLLTY ADNILRSPNE EKYRSIRIGN TAFSTRLLPV
RGAIECLFEM GFEEGETHLV FPKMASVEKL RKVRDHIATE RNSRMTGANP TPPATSSTPP
SFSRTPVPNA VPPSIPLQAT EDISNFLASE VRYLKTLQSN SQRVLIYEEP ELQQKALQKI
PVSDLKTRAQ KNLIEAKSLD SDTSVILEDF LLLELLRWFK QDFFQWVNSL PCSRCGGDTQ
ARDALSPSAE DLRWGADRVE NHYCEKCKHS NRFPRYNHPE KLLETRRGRC GEWANCFTLC
CRALEFEARY VWDSTDHVWT EVYATSQNRW LHCDPCENAC DKPLLYEVGW GKKLSYIIAF
SKDEVMDVTW RYSCKHEDVI ARRKDVRESW LRETIVGLNK MKQQSLPEHR KQELLGRLIV
ELVEFMSPKT PKPGELGGRV SGSLAWRVTR GETSLQPNKS VVFIPSESEK ISKRFHLQYN
VVEDTYTRAS NNNEVIAGWE NGTWKAESIC RKVENDWKMV YLARTEGSSS AAISWKIECA
SAGLQIESLS VRTSSQTFHN GKIIWKLSSP EAEVEVNSDT SFHSYTEFLN ASEVELKAEL
CDGDGNTAWQ HTQIFREKLD CKANSLEIII ILKDV
//
