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Protein

Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase

Gene

PNG1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. 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. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).By similarity

Catalytic activityi

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.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi193 – 1931ZincBy similarity
Metal bindingi196 – 1961ZincBy similarity
Metal bindingi225 – 2251ZincBy similarity
Metal bindingi228 – 2281ZincBy similarity
Active sitei251 – 2511NucleophileBy similarity
Active sitei278 – 2781By similarity
Active sitei295 – 2951By similarity

GO - Molecular functioni

GO - Biological processi

  • response to microbial phytotoxin Source: TAIR
  • response to ozone Source: TAIR
  • response to salicylic acid Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT5G49570-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC:3.5.1.52)
Alternative name(s):
Peptide:N-glycanase
Short name:
AtPNG1
Gene namesi
Name:PNG1
Ordered Locus Names:At5g49570
ORF Names:K6M13.12
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G49570.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 721721Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidasePRO_0000248981Add
BLAST

Proteomic databases

PaxDbiQ9FGY9.
PRIDEiQ9FGY9.

PTM databases

iPTMnetiQ9FGY9.

Expressioni

Gene expression databases

ExpressionAtlasiQ9FGY9. baseline and differential.
GenevisibleiQ9FGY9. AT.

Interactioni

Protein-protein interaction databases

BioGridi20265. 1 interaction.
STRINGi3702.AT5G49570.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FGY9.
SMRiQ9FGY9. Positions 124-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0909. Eukaryota.
ENOG410XP69. LUCA.
HOGENOMiHOG000285938.
InParanoidiQ9FGY9.
KOiK01456.
OMAiKEERDYA.
PhylomeDBiQ9FGY9.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR018325. Rad4/PNGase_transGLS-fold.
IPR002931. Transglutaminase-like.
[Graphical view]
PfamiPF03835. Rad4. 1 hit.
[Graphical view]
SMARTiSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9FGY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVARKFVVRH EDSSFDVDYN TEDGLEVLRF LIFSLTLVPP EEQKIVAEDD
60 70 80 90 100
NRLVSDESDL ASLSERLRLV SVGEDSVENS DAEMLKSDEE LARMLQAEED
110 120 130 140 150
AIMFQQFVAA RDNGEFEGRI RPYVSQVLMY EDPVRQDAAR KTVPKDELEE
160 170 180 190 200
KALVSLAKEG NFEPSKEERD YAFLLQLLFW FKKSFRWVNE PPCDFCGNKT
210 220 230 240 250
IGQGMGNPLT SELAYGANRV EIYRCTMCPT TTRFPRYNDP LKLVETKKGR
260 270 280 290 300
CGEWANCFTL YCRTFGYDSR LIMDFTDHVW TECYSHSLKR WIHLDPCEGV
310 320 330 340 350
YDKPMLYEKG WNKKLNYVIA ISKDGVCDVT KRYTKKWHEV LSRRTLTTES
360 370 380 390 400
SLQDGLRTLT RERRRSLMFE SLSKLELRDR NEQEELERNL HSADNASVSL
410 420 430 440 450
PGRQSGDREW RIMRSEFGSD ENSSVSSSSC PVRKCVDDHV TNIYDSFLPI
460 470 480 490 500
LTQFVEDGLP VARTNEVLKM IKQVLVDLKN APYKTRKARL TLDSDNSSSF
510 520 530 540 550
PEQFLPALGD LLLALSLKSE RDTNGKSVTI SVDGKLTKTA IALPVALDAL
560 570 580 590 600
RELVADLSKY QNLNKDSLSF PLVKQNRVCS GSVLASGEEL PSGIATAAFD
610 620 630 640 650
GIQESKWEEP NGAKGCWIVY KTLYNQMHQL IAYELMSAND APERDPKDWI
660 670 680 690 700
LEGSNDGGST WCVLDKQTSQ VFEERFQRKS YKITTPGFQA NLFRFRFLSV
710 720
RDVNSTSRLQ LGSIDLYRSH Q
Length:721
Mass (Da):82,446
Last modified:March 1, 2001 - v1
Checksum:iBD516DD961C0CC91
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti346 – 3461L → P in AAO24593 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023033 Genomic DNA. Translation: BAB10770.1.
CP002688 Genomic DNA. Translation: AED95831.1.
AY140065 mRNA. Translation: AAM98206.1.
BT003161 mRNA. Translation: AAO24593.1.
BT003398 mRNA. Translation: AAO30061.1.
AK228156 mRNA. Translation: BAF00112.1.
RefSeqiNP_199768.1. NM_124335.2.
UniGeneiAt.27656.
At.29778.

Genome annotation databases

EnsemblPlantsiAT5G49570.1; AT5G49570.1; AT5G49570.
GeneIDi835019.
GrameneiAT5G49570.1; AT5G49570.1; AT5G49570.
KEGGiath:AT5G49570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023033 Genomic DNA. Translation: BAB10770.1.
CP002688 Genomic DNA. Translation: AED95831.1.
AY140065 mRNA. Translation: AAM98206.1.
BT003161 mRNA. Translation: AAO24593.1.
BT003398 mRNA. Translation: AAO30061.1.
AK228156 mRNA. Translation: BAF00112.1.
RefSeqiNP_199768.1. NM_124335.2.
UniGeneiAt.27656.
At.29778.

3D structure databases

ProteinModelPortaliQ9FGY9.
SMRiQ9FGY9. Positions 124-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi20265. 1 interaction.
STRINGi3702.AT5G49570.1.

PTM databases

iPTMnetiQ9FGY9.

Proteomic databases

PaxDbiQ9FGY9.
PRIDEiQ9FGY9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G49570.1; AT5G49570.1; AT5G49570.
GeneIDi835019.
GrameneiAT5G49570.1; AT5G49570.1; AT5G49570.
KEGGiath:AT5G49570.

Organism-specific databases

TAIRiAT5G49570.

Phylogenomic databases

eggNOGiKOG0909. Eukaryota.
ENOG410XP69. LUCA.
HOGENOMiHOG000285938.
InParanoidiQ9FGY9.
KOiK01456.
OMAiKEERDYA.
PhylomeDBiQ9FGY9.

Enzyme and pathway databases

BioCyciARA:AT5G49570-MONOMER.

Miscellaneous databases

PROiQ9FGY9.

Gene expression databases

ExpressionAtlasiQ9FGY9. baseline and differential.
GenevisibleiQ9FGY9. AT.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR018325. Rad4/PNGase_transGLS-fold.
IPR002931. Transglutaminase-like.
[Graphical view]
PfamiPF03835. Rad4. 1 hit.
[Graphical view]
SMARTiSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
    DNA Res. 7:31-63(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "The PUB domain: a putative protein-protein interaction domain implicated in the ubiquitin-proteasome pathway."
    Suzuki T., Park H., Till E.A., Lennarz W.J.
    Biochem. Biophys. Res. Commun. 287:1083-1087(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiPNG1_ARATH
AccessioniPrimary (citable) accession number: Q9FGY9
Secondary accession number(s): Q84WJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.