NGLY1_CAEBR
ID NGLY1_CAEBR Reviewed; 602 AA.
AC Q5WNE3; A8X5N2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase;
DE EC=3.5.1.52;
DE AltName: Full=Peptide:N-glycanase;
DE Short=PNGase;
GN Name=png-1; ORFNames=CBG08042;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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. Also
CC displays oxidoreductase (thioredoxin) activity (By similarity).
CC {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. Endoplasmic reticulum {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00731}.
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DR EMBL; HE600996; CAP27943.3; -; Genomic_DNA.
DR RefSeq; XP_002646157.1; XM_002646111.1.
DR AlphaFoldDB; Q5WNE3; -.
DR SMR; Q5WNE3; -.
DR STRING; 6238.CBG08042; -.
DR PRIDE; Q5WNE3; -.
DR GeneID; 8588084; -.
DR KEGG; cbr:CBG_08042; -.
DR CTD; 8588084; -.
DR WormBase; CBG08042; CBP38491; WBGene00029910; Cbr-png-1.
DR eggNOG; KOG0907; Eukaryota.
DR eggNOG; KOG0909; Eukaryota.
DR HOGENOM; CLU_030187_2_0_1; -.
DR InParanoid; Q5WNE3; -.
DR OMA; IKPSVEY; -.
DR OrthoDB; 917526at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR002931; Transglutaminase-like.
DR Pfam; PF04721; PAW; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00613; PAW; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51398; PAW; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endoplasmic reticulum; Hydrolase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..602
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /id="PRO_0000248977"
FT DOMAIN 2..130
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 400..602
FT /note="PAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00731"
FT ACT_SITE 248
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /evidence="ECO:0000250"
FT ACT_SITE 292
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 602 AA; 69212 MW; 0450AEAB14419DE1 CRC64;
MPVREVSRLP ELNEILEKSD SNRLIIVDFF ANWCGPCRMI SPAFERLSME FGNATFLKVN
TDLARDIVMR YSISAMPTFL FFKNKQQVDS VRGANESAII STIRKHYSST PANPNAASDE
EKKFLERFVG YTELRKMHTD EVFKALARSV MPDGISDRLE NGEDEKKVLQ ELLDWFKNDF
FTWFDRPTCL KCTLKCTTEG LNGTPTKEEK EGGAGRVEVF ICNGCNSEMR FPRYNDPSKL
LQTRTGRCGE WANCFGLILS AAGLENRFVL DTTDHVWNEV YLKKEQRWIH VDPCENTMDR
PLLYTRGWKK QLKYCIAYGH DHVTDVTWRY VFDSKKLVTQ ERVRQGVLEN FLGKLNARQM
AGATEERKRE LAVRRVCELM GMMVQEAKNQ RIGWEKLGED MGGRTTGSKE WRRARGELGD
NPEAQVLGKP IEFRIQNDAN HVEFSYDVNR DSYSQTPEKG FVAQTFECNN IQRKVENDWK
MVYLCREDGK KEGNISWHFN LAPLVATDSK KTIEKVEIRM AGIRKFENGN ILIIACLGDT
CMRIPASGNL TIEDPKPEVL KITVTLSGGE RNQAFQHAQL FRTEKDDVAE ATESMVVRVY
MK
