ID H2PBB4_PONAB Unreviewed; 599 AA.
AC H2PBB4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 52.
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:ENSPPYP00000015731.3};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000015731.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000015731.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000015731.3}
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 AlphaFoldDB; H2PBB4; -.
DR Ensembl; ENSPPYT00000016352.3; ENSPPYP00000015731.3; ENSPPYG00000014060.3.
DR eggNOG; KOG0909; Eukaryota.
DR GeneTree; ENSGT00390000006540; -.
DR HOGENOM; CLU_030187_1_0_1; -.
DR InParanoid; H2PBB4; -.
DR TreeFam; TF315254; -.
DR Proteomes; UP000001595; Chromosome 3.
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; 1.10.1740.90; -; 1.
DR Gene3D; 1.20.58.2190; -; 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:UP000001595};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 397..599
FT /note="PAW"
FT /evidence="ECO:0000259|PROSITE:PS51398"
FT REGION 112..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 599 AA; 68357 MW; 12434B0EDA02812E CRC64;
MAAAALGSSS GSESPAVAEL CQNTPETFLE ASKLLLTYAD NILRNPNDEK YRSIRIGNTA
FSTRLLPVRG AVECLFEMGF EEGETHLIFP KKASVEQLQK IRDLIAIERS SRLDGSNKSH
KVKSSQQPAA STQLPTTPSS NPSGLNQHTR NHQGQSSDPP SASTVTADSA ILEVLQSNIQ
HVLVYENPAL QEKALACIPV QELKRKSQEK LSRARKLDKG TNISDEDFLL LELLHWFKEE
FFQWVNNILC SKCGGQTRSR DRSLLPNDDE LKWGAKKVED HYCDACQFSN RFPRYNNPEK
LLETRCGRCG EWANCFTLCC RALGFEARYV WDYTDHVWTE VYSPSQQRWL HCDACEDVCD
KPLLYEIGWG KKLSYVIAFS KDEVVDVTWR YSCKHEEVIA RRTKVKEALL RETINGLNKQ
RKETSFIPCE NEKISKQLHL CYNIVKDCYV RVSNNNETIS GWENGVWKME SIFRKVETDW
HMVYLARKEG SSFSYISWKF ECGSVRLKVD SISIRTSSQT FQTGTIEWKL RSDTARVELT
GDNSLHSYAD FSGATEVILE AELSRGDGDV AWQHTQLFRQ SLNDHEEDCL EIIIKFSDL
//
