PNG1_ORYSJ
ID PNG1_ORYSJ Reviewed; 447 AA.
AC Q7F0R1; Q0D6A2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=PNG1; OrderedLocusNames=Os07g0497400, LOC_Os07g31460;
GN ORFNames=OJ1197_D06.103, P0005E02.110;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(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 (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:0000305}.
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DR EMBL; AP004006; BAD30444.1; -; Genomic_DNA.
DR EMBL; AP004259; BAC79717.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21621.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT01614.1; -; Genomic_DNA.
DR EMBL; AK068275; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q7F0R1; -.
DR SMR; Q7F0R1; -.
DR STRING; 4530.OS07T0497400-01; -.
DR PRIDE; Q7F0R1; -.
DR EnsemblPlants; Os07t0497400-01; Os07t0497400-01; Os07g0497400.
DR Gramene; Os07t0497400-01; Os07t0497400-01; Os07g0497400.
DR eggNOG; KOG0909; Eukaryota.
DR HOGENOM; CLU_031058_0_1_1; -.
DR InParanoid; Q7F0R1; -.
DR OMA; YVIAITK; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q7F0R1; baseline and differential.
DR Genevisible; Q7F0R1; OS.
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; IBA:GO_Central.
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 GO; GO:0010188; P:response to microbial phytotoxin; IEA:EnsemblPlants.
DR GO; GO:0010193; P:response to ozone; IEA:EnsemblPlants.
DR GO; GO:0009751; P:response to salicylic acid; IEA:EnsemblPlants.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..447
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /id="PRO_0000248982"
FT ACT_SITE 267
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 294
FT /evidence="ECO:0000250"
FT ACT_SITE 311
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 447 AA; 50513 MW; 69BD6BB06D117CC9 CRC64;
MVARRFVVRQ GGGGGGGGEA EEHEVEYDTE HGLDILRLQI FSLTSVPPEL QKIVVEADGS
VVDDGTDLEA ISEGLRLVAI TGEEEEAEAA AAAEAARAQE KSDEELARMI QAEEEALLLQ
QYSIRNDGGE EFRERVEPYM HQVLMYEDPM RQEAARKTVP MDELQEKALV SLAKEGNFSP
SKDEEDHAFL LQLLFWFKQS FRWVNAPPCD SCGRETFNVG MGTALPSEIK FGANRVEIYR
CNYCSSTTRF PRYNDPYKLL ETRKGRCGEW ANCFTFYCRS FGYEARLILD FTDHVWTECF
SNLYGRWMHL DPCEGVYDNP LLYEKGWNKK LDYVIAISKD GVRDVTKRYT RKWHEVLSRR
IITSEDTVSA ILSSITGKYR SGLSIDGLTA LENRDKKESE ELSKAAYLEV DTSISLPGRQ
SGSVEWRKAS QKCSTYILSI TSGNGCG
