NGLY1_DANRE
ID NGLY1_DANRE Reviewed; 644 AA.
AC Q503I8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase;
DE Short=PNGase;
DE EC=3.5.1.52;
DE AltName: Full=N-glycanase 1;
DE AltName: Full=Peptide:N-glycanase;
GN Name=ngly1; ORFNames=zgc:110561;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) 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 (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00731}.
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DR EMBL; BC095313; AAH95313.1; -; mRNA.
DR RefSeq; NP_001018437.1; NM_001020601.1.
DR AlphaFoldDB; Q503I8; -.
DR SMR; Q503I8; -.
DR STRING; 7955.ENSDARP00000008500; -.
DR PaxDb; Q503I8; -.
DR GeneID; 553627; -.
DR KEGG; dre:553627; -.
DR CTD; 55768; -.
DR ZFIN; ZDB-GENE-050522-535; ngly1.
DR eggNOG; KOG0909; Eukaryota.
DR InParanoid; Q503I8; -.
DR OrthoDB; 917526at2759; -.
DR PhylomeDB; Q503I8; -.
DR Reactome; R-DRE-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR PRO; PR:Q503I8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0006517; P:protein deglycosylation; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR Gene3D; 2.60.120.1020; -; 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 Pfam; PF04721; PAW; 1.
DR Pfam; PF09409; PUB; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00613; PAW; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF143503; SSF143503; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51398; PAW; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..644
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /id="PRO_0000248976"
FT DOMAIN 20..81
FT /note="PUB"
FT DOMAIN 439..644
FT /note="PAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00731"
FT REGION 98..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 321
FT /evidence="ECO:0000250"
FT ACT_SITE 338
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 644 AA; 72489 MW; 2A7C2D94C4B12A20 CRC64;
MPGSQGVLAL CENTTEVFLD VSKLLITYAD NILRNPNEEK YRSIRIGNPT FSTKLLPVKG
AVECLFEMGF EEAETHLVFP RSASVEKLRQ VRETIAAERD QRLGASNTAS SPQNASVPPV
PAPPPSLSST ASAGPAAAAV PTPAPASIPF TSSSATFQRT VQSNFQHVLV YEDPELQQKA
LECIPHELLR SRAKERLKQA NDADAACSLG EEDMLVLDLL QWFKSDFFSW VDNLPCIQCG
GKTQPSGSLS PSSDDLHWDA GRVENHFCHT CQLSTRFPRY NNPEKLLETR KGRCGEWANC
FTLLCRALGL EARYIWDSTD HVWTEVYSQS QRRWIHCDPC ENACDKPLLY EVGWGKKLSY
ILAFSKDQVA DVTWRYSCKH PEVLSRRTQV QETWLLHMLN KLNAERQQFL GAERKQQLLQ
RLLVELVEFI SPKSPQPGEL GGRMSGSLAW RAARGETGAS NAKEDTQENV FTPSESEKES
KRFHICYNVT KDCYYRVSNG QETIQGWQKG AWRTENMFRK EEHDWQMVYL ARTEGASFGR
MSWKFNCAPA GMKMKSASVR VFSQTFHSGT VRWSLSTNET TTEFPGDGEL HSFSNVSGGT
ELIVEAELTG GDGSTSWQHA QLFRQSLKDT EKVLFEVMVE MEKS
