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Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) (Peptide:N-glycanase) (PNGase)

 NGLY1_CAEEL             Reviewed;         606 AA.
Q9TW67; Q9NBD6;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-JUN-2018, entry version 141.
RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase;
EC=3.5.1.52;
AltName: Full=Peptide:N-glycanase;
Short=PNGase;
Name=png-1; ORFNames=F56G4.5;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 65-606.
PubMed=10831608; DOI=10.1083/jcb.149.5.1039;
Suzuki T., Park H., Hollingsworth N.M., Sternglanz R., Lennarz W.J.;
"PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase.";
J. Cell Biol. 149:1039-1052(2000).
[3]
FUNCTION, AND MUTAGENESIS OF CYS-251.
PubMed=17509531; DOI=10.1016/j.bbrc.2007.04.199;
Suzuki T., Tanabe K., Hara I., Taniguchi N., Colavita A.;
"Dual enzymatic properties of the cytoplasmic peptide: N-glycanase in
C. elegans.";
Biochem. Biophys. Res. Commun. 358:837-841(2007).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=17522090; DOI=10.1093/jb/mvm117;
Kato T., Kawahara A., Ashida H., Yamamoto K.;
"Unique peptide:N-glycanase of Caenorhabditis elegans has activity of
protein disulphide reductase as well as of deglycosylation.";
J. Biochem. 142:175-181(2007).
[5]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-498.
PubMed=27528192; DOI=10.7554/eLife.17721;
Lehrbach N.J., Ruvkun G.;
"Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the
aspartic protease DDI-1.";
Elife 5:0-0(2016).
-!- FUNCTION: Specifically deglycosylates the denatured form of N-
linked glycoproteins in the cytoplasm and assists their
proteasome-mediated degradation (PubMed:17509531,
PubMed:17522090). Cleaves the beta-aspartyl-glucosamine (GlcNAc)
of the glycan and the amide side chain of Asn, converting Asn to
Asp (PubMed:17522090). Prefers proteins containing high-mannose
over those bearing complex type oligosaccharides
(PubMed:17522090). Can recognize misfolded proteins in the
endoplasmic reticulum that are exported to the cytosol to be
destroyed and deglycosylate them, while it has no activity toward
native proteins (PubMed:17509531). Deglycosylation is a
prerequisite for subsequent proteasome-mediated degradation of
some, but not all, misfolded glycoproteins (PubMed:17509531). Also
displays oxidoreductase (thioredoxin) activity (PubMed:17509531,
PubMed:17522090). Involved in regulating the expression of
proteasomal subunits such as rpt-3 in order to confer resistance
to proteasomal dysfunction (PubMed:27528192).
{ECO:0000269|PubMed:17509531, ECO:0000269|PubMed:17522090,
ECO:0000269|PubMed:27528192}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(4)-(acetyl-beta-D-
glucosaminyl)asparagine residue in which the glucosamine residue
may be further glycosylated, to yield a (substituted) N-acetyl-
beta-D-glucosaminylamine and a peptide containing an aspartate
residue.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by Zn(2+) and z-VAD-fmk (caspase
inhibitor) but unaffected by EDTA. {ECO:0000269|PubMed:17522090}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17522090}.
Endoplasmic reticulum {ECO:0000269|PubMed:17522090}. Note=ER
localization inferred from partial colocalization with an ER
marker, membrane protein PIG-X.
-!- DISRUPTION PHENOTYPE: Double knockout with rpt-5 RNAi results in
failed expression of the proteasomal subunit rpt-3.
{ECO:0000269|PubMed:27528192}.
-!- SIMILARITY: Belongs to the transglutaminase-like superfamily.
PNGase family. {ECO:0000255|PROSITE-ProRule:PRU00731}.
-----------------------------------------------------------------------
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EMBL; Z81552; CAB04487.2; -; Genomic_DNA.
EMBL; AL117201; CAB04487.2; JOINED; Genomic_DNA.
EMBL; AF250925; AAF74721.1; -; mRNA.
PIR; E87921; E87921.
PIR; T31557; T31557.
RefSeq; NP_492913.1; NM_060512.4.
UniGene; Cel.18605; -.
ProteinModelPortal; Q9TW67; -.
SMR; Q9TW67; -.
BioGrid; 38436; 2.
DIP; DIP-24462N; -.
IntAct; Q9TW67; 2.
STRING; 6239.F56G4.5.1; -.
EPD; Q9TW67; -.
PaxDb; Q9TW67; -.
PeptideAtlas; Q9TW67; -.
PRIDE; Q9TW67; -.
EnsemblMetazoa; F56G4.5; F56G4.5; WBGene00010160.
GeneID; 173028; -.
KEGG; cel:CELE_F56G4.5; -.
CTD; 173028; -.
WormBase; F56G4.5; CE23786; WBGene00010160; png-1.
eggNOG; KOG0907; Eukaryota.
eggNOG; KOG0909; Eukaryota.
eggNOG; ENOG410XP69; LUCA.
GeneTree; ENSGT00390000006540; -.
InParanoid; Q9TW67; -.
KO; K01456; -.
OMA; VWNEVYL; -.
OrthoDB; EOG091G09YB; -.
PhylomeDB; Q9TW67; -.
BRENDA; 3.5.1.52; 1045.
Reactome; R-CEL-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
PRO; PR:Q9TW67; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00010160; -.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IDA:WormBase.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IDA:WormBase.
GO; GO:0047134; F:protein-disulfide reductase activity; IDA:WormBase.
GO; GO:0045454; P:cell redox homeostasis; IGI:WormBase.
GO; GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB.
GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:WormBase.
GO; GO:0006517; P:protein deglycosylation; IDA:WormBase.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IGI:WormBase.
Gene3D; 2.60.120.1020; -; 1.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR038680; PAW_sf.
InterPro; IPR006588; Peptide_N_glycanase_PAW_dom.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
InterPro; IPR002931; Transglutaminase-like.
Pfam; PF04721; PAW; 1.
Pfam; PF00085; Thioredoxin; 1.
Pfam; PF01841; Transglut_core; 1.
SMART; SM00613; PAW; 1.
SMART; SM00460; TGc; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52833; SSF52833; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS51398; PAW; 1.
PROSITE; PS00194; THIOREDOXIN_1; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Hydrolase;
Metal-binding; Reference proteome; Zinc.
CHAIN 1 606 Peptide-N(4)-(N-acetyl-beta-
glucosaminyl)asparagine amidase.
/FTId=PRO_0000248978.
DOMAIN 2 108 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 404 606 PAW. {ECO:0000255|PROSITE-
ProRule:PRU00731}.
ACT_SITE 251 251 Nucleophile.
ACT_SITE 278 278 {ECO:0000250}.
ACT_SITE 295 295 {ECO:0000250}.
METAL 191 191 Zinc. {ECO:0000250}.
METAL 194 194 Zinc. {ECO:0000250}.
METAL 225 225 Zinc. {ECO:0000250}.
METAL 228 228 Zinc. {ECO:0000250}.
MUTAGEN 251 251 C->Y: Loss of PNGase activity.
{ECO:0000269|PubMed:17509531}.
MUTAGEN 498 498 G->R: In mg561; defective expression of
the proteasomal subunit rpt-3 in a pbs-5
(proteasomal subunit) mutant background.
{ECO:0000269|PubMed:27528192}.
SEQUENCE 606 AA; 69148 MW; 1D3EA2EBDFB40769 CRC64;
MPVTEVGSLP ELNNILERSD ANRLIIIDFF ANWCGPCRMI SPIFEQFSAE YGNATFLKVN
CDVARDIVQR YNISAMPTFI FLKNRQQVDM VRGANQQAIA EKIRQHYSPT PANPNAASDS
EKRFLEQFVK CSNVPRSYQD EVFKALARSV MPEELVGRAM TEGPRDEKAI LKDLLHWFKT
QFFTWFDRPT CPKCTLKCST DGLQGTPTRE EQKEGGASRV EVYICDGCNT EMRFPRYNNP
AKLLQTRTGR CGEWANCFGL LLAALNLESR FIYDTTDHVW NEVYLLAEQR WCHVDPCENT
MDRPLLYTRG WGKTLGYCIG YGSDHVVDVT WRYIWDSKKL VTQRNEVRQP VFENFLSKLN
SRQAEGQTEP RKRELAVRRV CELMEMMAQE AKNHKIGWEK IGDDLGGRIT GSEEWRRERG
ELGESGPKLL AEPIKLAPPT GPAQNYLEFN YDVITDTYSQ PPEIGFSAQA FELENVQRVE
ETDWNMTYLC RKRGDAPGNI SWHFDLKSLK KSIEKIEIRM AGIQKFEKGK AMAIACLGDS
CMRLPIDCSA LTIEDPKNAE ILKITATLSG GEGAIGFQQA QIFRTELKRG GGARTESFSV
KIWMKN


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