ID A0A091EMJ1_CORBR Unreviewed; 612 AA.
AC A0A091EMJ1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
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};
DE Flags: Fragment;
GN ORFNames=N302_12278 {ECO:0000313|EMBL:KFO57827.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO57827.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO57827.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO57827.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK718644; KFO57827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091EMJ1; -.
DR STRING; 85066.A0A091EMJ1; -.
DR Proteomes; UP000052976; Unassembled WGS sequence.
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 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:UP000052976};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 411..612
FT /note="PAW"
FT /evidence="ECO:0000259|PROSITE:PS51398"
FT REGION 72..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO57827.1"
FT NON_TER 612
FT /evidence="ECO:0000313|EMBL:KFO57827.1"
SQ SEQUENCE 612 AA; 70185 MW; 19B3863DCF3A616F CRC64;
NFFRNPYEEK YRLIRIGNPA FSTRLLPVRG AVECLFEMGF QEGETHLVFP KEASIEQLRK
IRDLIAGERS SRLNESNQIH RSGSSETVSS TQTAAPRPSR PVDSVLAPAR QQPETSLVQS
LEMAANILKT LQTKFEDLVL MYEDPSVQQK ALAAIPLQEL KRKAQKKLAQ ATRLDKGAHV
NEEDFLLLEL LDWFKTSFFC WVNSLPCSRC GGQTEPKSDY LLPTDDDLRW DASRVENHYC
NQCQLCNRFP RYNNPEKLLE TRRGRCGEWA NCFTLCCRAV GFEARYVWDY TDHVWTEVYS
SSQKRWLHCD PCENVCDKPL LYETGWGKKL SYIIAFSKDE VVDVTWRYSC KHEEVLSRRT
ALSEATLRET INALNRTRQK SLSENRKREL LERTIVELVE FISPKTPKPG EYGGRTSGSM
AWRIARGEIG PEKRKEVVFI PSEKEKTSKL FHLIYNVIDD SYTRVSNNNE KIHGWEAGVW
KAESIWRKVE TDWKMVYLAR KEGSSSASIS WKFECKSVGL KIDNVSVRTS SQTFQSGRIQ
WRLHSPTAEI SLIGDKNLCS YSDFSGATEV VLEAVLNGGD GEAAWQHTQL FRESLTGYGE
NCLEIIIKLS DL
//
