ID G1QUL8_NOMLE Unreviewed; 654 AA.
AC G1QUL8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 {ECO:0000313|Ensembl:ENSNLEP00000004638.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000004638.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000004638.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000004638.1}
RP IDENTIFICATION.
RG Ensembl;
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; ADFV01171750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01171751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01171752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01171753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01171754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01171755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01171756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003256823.1; XM_003256775.2.
DR AlphaFoldDB; G1QUL8; -.
DR STRING; 61853.ENSNLEP00000004638; -.
DR Ensembl; ENSNLET00000004877.3; ENSNLEP00000004638.1; ENSNLEG00000003792.3.
DR GeneID; 100598050; -.
DR KEGG; nle:100598050; -.
DR CTD; 55768; -.
DR eggNOG; KOG0909; Eukaryota.
DR GeneTree; ENSGT00390000006540; -.
DR HOGENOM; CLU_030187_1_0_1; -.
DR InParanoid; G1QUL8; -.
DR OMA; WANVFTL; -.
DR OrthoDB; 5051at2759; -.
DR TreeFam; TF315254; -.
DR Proteomes; UP000001073; Chromosome 4.
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:Ensembl.
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:UP000001073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 454..654
FT /note="PAW"
FT /evidence="ECO:0000259|PROSITE:PS51398"
FT REGION 115..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 74550 MW; 76BEB783E8AD2D3E CRC64;
MAAAALGSSS GSASPAVAEL CQNTPETFLE ASKLLLTYAD NILRNPNDEK YRSIRIGNTA
FSTRLLPVRG AVECLFEMGF EEGETHLIFP KKASVEQLQK IRDLIAIERS SRLDGSNKSH
KIESSQQPAA STQLPTTPSS NPSGLNQHTR NRQGQSSDPP SASTVTADSA ILEVLQSNIQ
HVLVYENPAL QEKALACIPV QELNRKSQEK LSRARRLDKG TNISDEDFLL LELLHWFKEE
FFHWVNNILC SKCGGQTRSR DRSLLPNDDE LKWGAKKVED HYCDACQFSN RFPRYNNPEK
LLETRCGRCG EWANCFTLCC RALGFEARYV WDYTDHVWTE VYSPSQQRWL HCDACEDVCD
KPLLYEIGWG KKLSYVIAFS KDEVVDVTWR YSCKHEEVIA RRTKVKEALL RETINGLNKQ
RQLFLSENRR KELLQRIIVE LVEFISPKTP RPGELGGRIS GSVAWRVARG EMGLQRKETS
FIPCENEKIS KQLHLCYDIV KDRYVRVSNN NQTISGWENG VWKMESIFRK VETDWHMVYL
ARKEGSSFAY ISWKFECGSV GLKVDSISIR TSSQTFQTGT IEWKLRSDTA RVELTGDNNL
HSYADFSGAT EVILEAELSR GDGDVAWQHT QLFRQSLNDH EESCLEIIIK FSDL
//
