ID W5MJ39_LEPOC Unreviewed; 650 AA.
AC W5MJ39;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000008398.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000008398.1}
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; AHAT01018100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01018101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01018102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MJ39; -.
DR STRING; 7918.ENSLOCP00000008398; -.
DR Ensembl; ENSLOCT00000008408.1; ENSLOCP00000008398.1; ENSLOCG00000006940.1.
DR eggNOG; KOG0909; Eukaryota.
DR GeneTree; ENSGT00390000006540; -.
DR HOGENOM; CLU_030187_1_0_1; -.
DR InParanoid; W5MJ39; -.
DR OMA; WANVFTL; -.
DR Proteomes; UP000018468; Linkage group LG11.
DR Bgee; ENSLOCG00000006940; Expressed in pharyngeal gill and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
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:UP000018468};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 450..650
FT /note="PAW"
FT /evidence="ECO:0000259|PROSITE:PS51398"
FT REGION 108..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 73062 MW; 7B3B728816225BE3 CRC64;
NPKVELGQQE IMAGSQGVNA LCENPNDVFL DVSKLLLTYA DNILRNPSED KYRSIRIGNP
TFSTRLLPIK GAVECLFEMG FQEAETHLVF PKSASVEQLR RIRETIAAER DMRLRGPLPV
SAPAPGPSST RGQPAAAPAS GETPAPPSAP LPAPASQPTP TDSRMTFFRT LQSNFQHVML
YEDVALQEKA LAHIPAERLW TAAKEKLQEA QKADPVTWKL NVEDLLLLEL LRWFKSEFFS
WVNSLPCSRC GGPTQASGQL PPSTDDLRWD AHRVENHFCT ECQLVNRFPR YNNPEKLLET
RRGRCGEWAN CFTLCCRAMG LEARYIWDST DHVWTEVYST SQSRWLHCDP CENVCDKPLL
YEIGWGKKLS YIIAFSKDEV VDVTWRYSCK HEEVLSRRTK VQEDWLRQTI NGQSAAIQVS
VITTRASGVL LLLVRVELAG GFLPSCAPVS PVASHLLAVC ARLGGGKLYL QNPGFVFIPS
EGEKKEKIFH LQYNPAKDQY CRISNKSETI QGWENGVWKK ESIFRKVEND WQMVYIACTE
GSSSGNISWK FDCGPVGLKI RSVSLRVSSK TFHSGKVSWR INLKQETIDV LGDNTLHSFP
NLSDTTELVL EADLSGGESE TSWQHAQLFR QSLKEAEETS LEIIIHMEDA
//
