PNG1_ARATH
ID PNG1_ARATH Reviewed; 721 AA.
AC Q9FGY9; Q84WJ1;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=AtPNG1;
GN Name=PNG1; OrderedLocusNames=At5g49570; ORFNames=K6M13.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=11587532; DOI=10.1006/bbrc.2001.5688;
RA Suzuki T., Park H., Till E.A., Lennarz W.J.;
RT "The PUB domain: a putative protein-protein interaction domain implicated
RT in the ubiquitin-proteasome pathway.";
RL Biochem. Biophys. Res. Commun. 287:1083-1087(2001).
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; AB023033; BAB10770.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95831.1; -; Genomic_DNA.
DR EMBL; AY140065; AAM98206.1; -; mRNA.
DR EMBL; BT003161; AAO24593.1; -; mRNA.
DR EMBL; BT003398; AAO30061.1; -; mRNA.
DR EMBL; AK228156; BAF00112.1; -; mRNA.
DR RefSeq; NP_199768.1; NM_124335.3.
DR AlphaFoldDB; Q9FGY9; -.
DR SMR; Q9FGY9; -.
DR BioGRID; 20265; 1.
DR STRING; 3702.AT5G49570.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR iPTMnet; Q9FGY9; -.
DR PaxDb; Q9FGY9; -.
DR PRIDE; Q9FGY9; -.
DR ProteomicsDB; 234789; -.
DR EnsemblPlants; AT5G49570.1; AT5G49570.1; AT5G49570.
DR GeneID; 835019; -.
DR Gramene; AT5G49570.1; AT5G49570.1; AT5G49570.
DR KEGG; ath:AT5G49570; -.
DR Araport; AT5G49570; -.
DR TAIR; locus:2157869; AT5G49570.
DR eggNOG; KOG0909; Eukaryota.
DR HOGENOM; CLU_027996_1_0_1; -.
DR InParanoid; Q9FGY9; -.
DR OMA; GIRSSKW; -.
DR OrthoDB; 1273717at2759; -.
DR PhylomeDB; Q9FGY9; -.
DR BioCyc; ARA:AT5G49570-MON; -.
DR BRENDA; 3.5.1.52; 399.
DR PRO; PR:Q9FGY9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGY9; baseline and differential.
DR Genevisible; Q9FGY9; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
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:TAIR.
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; IEP:TAIR.
DR GO; GO:0010193; P:response to ozone; IEP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR InterPro; IPR002931; Transglutaminase-like.
DR Pfam; PF03835; Rad4; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..721
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /id="PRO_0000248981"
FT ACT_SITE 251
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 278
FT /evidence="ECO:0000250"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 196
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 CONFLICT 346
FT /note="L -> P (in Ref. 3; AAO24593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 721 AA; 82446 MW; BD516DD961C0CC91 CRC64;
MVARKFVVRH EDSSFDVDYN TEDGLEVLRF LIFSLTLVPP EEQKIVAEDD NRLVSDESDL
ASLSERLRLV SVGEDSVENS DAEMLKSDEE LARMLQAEED AIMFQQFVAA RDNGEFEGRI
RPYVSQVLMY EDPVRQDAAR KTVPKDELEE KALVSLAKEG NFEPSKEERD YAFLLQLLFW
FKKSFRWVNE PPCDFCGNKT IGQGMGNPLT SELAYGANRV EIYRCTMCPT TTRFPRYNDP
LKLVETKKGR CGEWANCFTL YCRTFGYDSR LIMDFTDHVW TECYSHSLKR WIHLDPCEGV
YDKPMLYEKG WNKKLNYVIA ISKDGVCDVT KRYTKKWHEV LSRRTLTTES SLQDGLRTLT
RERRRSLMFE SLSKLELRDR NEQEELERNL HSADNASVSL PGRQSGDREW RIMRSEFGSD
ENSSVSSSSC PVRKCVDDHV TNIYDSFLPI LTQFVEDGLP VARTNEVLKM IKQVLVDLKN
APYKTRKARL TLDSDNSSSF PEQFLPALGD LLLALSLKSE RDTNGKSVTI SVDGKLTKTA
IALPVALDAL RELVADLSKY QNLNKDSLSF PLVKQNRVCS GSVLASGEEL PSGIATAAFD
GIQESKWEEP NGAKGCWIVY KTLYNQMHQL IAYELMSAND APERDPKDWI LEGSNDGGST
WCVLDKQTSQ VFEERFQRKS YKITTPGFQA NLFRFRFLSV RDVNSTSRLQ LGSIDLYRSH
Q
