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NGLY1_CAEEL
ID   NGLY1_CAEEL             Reviewed;         606 AA.
AC   Q9TW67; Q9NBD6;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 159.
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=F56G4.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 65-606.
RX   PubMed=10831608; DOI=10.1083/jcb.149.5.1039;
RA   Suzuki T., Park H., Hollingsworth N.M., Sternglanz R., Lennarz W.J.;
RT   "PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase.";
RL   J. Cell Biol. 149:1039-1052(2000).
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF CYS-251.
RX   PubMed=17509531; DOI=10.1016/j.bbrc.2007.04.199;
RA   Suzuki T., Tanabe K., Hara I., Taniguchi N., Colavita A.;
RT   "Dual enzymatic properties of the cytoplasmic peptide: N-glycanase in C.
RT   elegans.";
RL   Biochem. Biophys. Res. Commun. 358:837-841(2007).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX   PubMed=17522090; DOI=10.1093/jb/mvm117;
RA   Kato T., Kawahara A., Ashida H., Yamamoto K.;
RT   "Unique peptide:N-glycanase of Caenorhabditis elegans has activity of
RT   protein disulphide reductase as well as of deglycosylation.";
RL   J. Biochem. 142:175-181(2007).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-498.
RX   PubMed=27528192; DOI=10.7554/elife.17721;
RA   Lehrbach N.J., Ruvkun G.;
RT   "Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the aspartic
RT   protease DDI-1.";
RL   Elife 5:0-0(2016).
CC   -!- FUNCTION: Specifically deglycosylates the denatured form of N-linked
CC       glycoproteins in the cytoplasm and assists their proteasome-mediated
CC       degradation (PubMed:17509531, PubMed:17522090). Cleaves the beta-
CC       aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of
CC       Asn, converting Asn to Asp (PubMed:17522090). Prefers proteins
CC       containing high-mannose over those bearing complex type
CC       oligosaccharides (PubMed:17522090). Can recognize misfolded proteins in
CC       the endoplasmic reticulum that are exported to the cytosol to be
CC       destroyed and deglycosylate them, while it has no activity toward
CC       native proteins (PubMed:17509531). Deglycosylation is a prerequisite
CC       for subsequent proteasome-mediated degradation of some, but not all,
CC       misfolded glycoproteins (PubMed:17509531). Also displays oxidoreductase
CC       (thioredoxin) activity (PubMed:17509531, PubMed:17522090). Involved in
CC       regulating the expression of proteasomal subunits such as rpt-3 in
CC       order to confer resistance to proteasomal dysfunction
CC       (PubMed:27528192). {ECO:0000269|PubMed:17509531,
CC       ECO:0000269|PubMed:17522090, ECO:0000269|PubMed:27528192}.
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   -!- ACTIVITY REGULATION: Inhibited by Zn(2+) and z-VAD-fmk (caspase
CC       inhibitor) but unaffected by EDTA. {ECO:0000269|PubMed:17522090}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17522090}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:17522090}. Note=ER
CC       localization inferred from partial colocalization with an ER marker,
CC       membrane protein PIG-X.
CC   -!- DISRUPTION PHENOTYPE: Double knockout with rpt-5 RNAi results in failed
CC       expression of the proteasomal subunit rpt-3.
CC       {ECO:0000269|PubMed:27528192}.
CC   -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00731}.
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DR   EMBL; Z81552; CAB04487.2; -; Genomic_DNA.
DR   EMBL; AL117201; CAB04487.2; JOINED; Genomic_DNA.
DR   EMBL; AF250925; AAF74721.1; -; mRNA.
DR   PIR; E87921; E87921.
DR   PIR; T31557; T31557.
DR   RefSeq; NP_492913.1; NM_060512.4.
DR   AlphaFoldDB; Q9TW67; -.
DR   SMR; Q9TW67; -.
DR   BioGRID; 38436; 4.
DR   DIP; DIP-24462N; -.
DR   IntAct; Q9TW67; 2.
DR   STRING; 6239.F56G4.5; -.
DR   EPD; Q9TW67; -.
DR   PaxDb; Q9TW67; -.
DR   PeptideAtlas; Q9TW67; -.
DR   PRIDE; Q9TW67; -.
DR   EnsemblMetazoa; F56G4.5.1; F56G4.5.1; WBGene00010160.
DR   GeneID; 173028; -.
DR   KEGG; cel:CELE_F56G4.5; -.
DR   CTD; 173028; -.
DR   WormBase; F56G4.5; CE23786; WBGene00010160; png-1.
DR   eggNOG; KOG0907; Eukaryota.
DR   eggNOG; KOG0909; Eukaryota.
DR   GeneTree; ENSGT00390000006540; -.
DR   HOGENOM; CLU_030187_2_0_1; -.
DR   InParanoid; Q9TW67; -.
DR   OMA; IKPSVEY; -.
DR   OrthoDB; 917526at2759; -.
DR   PhylomeDB; Q9TW67; -.
DR   BRENDA; 3.5.1.52; 1045.
DR   Reactome; R-CEL-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   PRO; PR:Q9TW67; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00010160; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
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; IDA:WormBase.
DR   GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IDA:WormBase.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IDA:WormBase.
DR   GO; GO:0045454; P:cell redox homeostasis; IGI:WormBase.
DR   GO; GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB.
DR   GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:WormBase.
DR   GO; GO:0006517; P:protein deglycosylation; IDA:WormBase.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IGI:WormBase.
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   1: Evidence at protein level;
KW   Cytoplasm; Endoplasmic reticulum; Hydrolase; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..606
FT                   /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT                   amidase"
FT                   /id="PRO_0000248978"
FT   DOMAIN          2..108
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          404..606
FT                   /note="PAW"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00731"
FT   ACT_SITE        251
FT                   /note="Nucleophile"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        295
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
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"
FT   BINDING         228
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         251
FT                   /note="C->Y: Loss of PNGase activity."
FT                   /evidence="ECO:0000269|PubMed:17509531"
FT   MUTAGEN         498
FT                   /note="G->R: In mg561; defective expression of the
FT                   proteasomal subunit rpt-3 in a pbs-5 (proteasomal subunit)
FT                   mutant background."
FT                   /evidence="ECO:0000269|PubMed:27528192"
SQ   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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