NGLY1_DROPS
ID NGLY1_DROPS Reviewed; 632 AA.
AC Q28YQ7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase;
DE EC=3.5.1.52;
DE AltName: Full=Peptide:N-glycanase;
GN Name=PNGase; ORFNames=GA20643;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000071; EAL25908.2; -; Genomic_DNA.
DR RefSeq; XP_001361330.2; XM_001361293.3.
DR AlphaFoldDB; Q28YQ7; -.
DR SMR; Q28YQ7; -.
DR IntAct; Q28YQ7; 1.
DR STRING; 7237.FBpp0276277; -.
DR EnsemblMetazoa; FBtr0277839; FBpp0276277; FBgn0080637.
DR KEGG; dpo:Dpse_GA20643; -.
DR eggNOG; KOG0909; Eukaryota.
DR HOGENOM; CLU_030187_1_0_1; -.
DR InParanoid; Q28YQ7; -.
DR OMA; IKPSVEY; -.
DR Proteomes; UP000001819; Genome assembly.
DR Bgee; FBgn0080637; Expressed in insect adult head and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0030246; F:carbohydrate binding; IEA:EnsemblMetazoa.
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; ISS:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0006517; P:protein deglycosylation; IEA:EnsemblMetazoa.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR GO; GO:0007495; P:visceral mesoderm-endoderm interaction involved in midgut development; IEA:EnsemblMetazoa.
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; IPR018325; Rad4/PNGase_transGLS-fold.
DR InterPro; IPR002931; Transglutaminase-like.
DR Pfam; PF04721; PAW; 1.
DR Pfam; PF09409; PUB; 1.
DR Pfam; PF03835; Rad4; 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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..632
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /id="PRO_0000248980"
FT DOMAIN 33..96
FT /note="PUB"
FT DOMAIN 442..632
FT /note="PAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00731"
FT ACT_SITE 297
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 324
FT /evidence="ECO:0000250"
FT ACT_SITE 341
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 632 AA; 73644 MW; 999AA6AF427CDD81 CRC64;
MVDINLECVH FIEPKNTRST EQQQQNVKNA YLEAVRILLV LLENVLSQPN NTKFRTIRLD
NKAIKEKLLS LPGCEKLLYA IGFRHTPSSN SYTLPGEVSL QQIQKYYDVL RERRTAWLSG
AMPKSPAHPK AACSTPSPLF IKTSVPYRQR ITFPRVLRTS NRFLQSLELY SDAVMQYEDE
LLLATGRSLI PVDDLTSKAS EKMMAMQDLI ASGECSEKEP CIRDLLLVEL TNWFNTQFFE
WVNNIQCQVC GSEESKLRRT QTEGDVRVEV NVCCGQESKF YRYNDISQLL VSRKGRCGEY
ANCFTFLCRC LDYDARLVHS HFDHVWTEVF SETQMRWLHV DPSDNVVDSP LMYQHGWKRG
IDYVFAYSRD DAQDVTWRYT NNHQEILKLR KLCDEKELIQ TLNAIREKRQ QNCSAERKNF
LSQRNMFEVI GLTLERKPTE NELKGRSSGS LSWRQSRGEH TFTNIFVFSP NEAELKKCQL
NLRYSCATDT YERYTKDDGQ ITLLNTYKTW QSAQFSSKNI YRKVERDWKM AYLARLEDTD
CAEIIWKFDL TKTNLKVKSY KLVFETKTFG EGKIDVSVQT NDGKTFIENS SEFQVVAKLM
GGKGDVAWQH TQLFRQSLNS REYPFDLQVE LH
