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Protein

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

Gene

Ngly1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.3 Publications

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+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Enzyme regulationi

Inhibited by Z-VAD-fmk, a well-known caspase inhibitor, which inhibits enzyme activity through covalent binding of the carbohydrate to the single Cys-306 residue.1 Publication

Kineticsi

  1. KM=114 µM for fetuin glycopeptide I1 Publication
  1. Vmax=0.0964 nmol/min/mg enzyme with fetuin glycopeptide I as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi247Zinc1
Metal bindingi250Zinc1
Metal bindingi280Zinc1
Metal bindingi283Zinc1
Active sitei306Nucleophile1
Active sitei3331
Active sitei3501

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.1.52. 3474.
ReactomeiR-MMU-532668. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC:3.5.1.52)
Short name:
PNGase
Short name:
mPNGase
Alternative name(s):
N-glycanase 1
Peptide:N-glycanase
Gene namesi
Name:Ngly1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1913276. Ngly1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: GO_Central
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi41N → P: Abolishes interaction with VCP. 1 Publication1
Mutagenesisi58N → A: Does not affect the interaction with VCP. 1 Publication1
Mutagenesisi79 – 80GF → AA: Abolishes interaction with VCP. 1 Publication2
Mutagenesisi306C → A: Abolishes enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002489732 – 651Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidaseAdd BLAST650

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9JI78.
MaxQBiQ9JI78.
PaxDbiQ9JI78.
PeptideAtlasiQ9JI78.
PRIDEiQ9JI78.

PTM databases

iPTMnetiQ9JI78.
PhosphoSitePlusiQ9JI78.

Expressioni

Tissue specificityi

Ubiquitously expressed with highest level in testis.2 Publications

Gene expression databases

BgeeiENSMUSG00000021785.
CleanExiMM_NGLY1.
GenevisibleiQ9JI78. MM.

Interactioni

Subunit structurei

Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts with the proteasome components RAD23B and PSMC1. Interacts with directly with VCP. Interacts with DERL1, bringing it close to the endoplasmic reticulum membrane. Interacts with SAKS1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AmfrQ9R0495EBI-3648128,EBI-3648125
RAD23AP547252EBI-3648128,EBI-746453From a different organism.
VcpQ018533EBI-3648128,EBI-80597

Protein-protein interaction databases

BioGridi208478. 7 interactors.
DIPiDIP-41155N.
IntActiQ9JI78. 5 interactors.
MINTiMINT-214719.
STRINGi10090.ENSMUSP00000022310.

Structurei

Secondary structure

1651
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 20Combined sources6
Helixi25 – 43Combined sources19
Beta strandi45 – 47Combined sources3
Helixi49 – 52Combined sources4
Beta strandi53 – 55Combined sources3
Helixi59 – 64Combined sources6
Turni65 – 67Combined sources3
Helixi71 – 78Combined sources8
Beta strandi84 – 88Combined sources5
Helixi95 – 109Combined sources15
Helixi167 – 180Combined sources14
Helixi181 – 183Combined sources3
Helixi185 – 194Combined sources10
Helixi197 – 211Combined sources15
Helixi223 – 236Combined sources14
Turni248 – 250Combined sources3
Beta strandi255 – 261Combined sources7
Helixi266 – 269Combined sources4
Beta strandi275 – 280Combined sources6
Turni281 – 284Combined sources4
Beta strandi285 – 290Combined sources6
Helixi295 – 301Combined sources7
Beta strandi303 – 305Combined sources3
Helixi306 – 319Combined sources14
Beta strandi324 – 329Combined sources6
Turni330 – 332Combined sources3
Beta strandi333 – 340Combined sources8
Turni341 – 344Combined sources4
Beta strandi345 – 350Combined sources6
Turni351 – 354Combined sources4
Beta strandi355 – 357Combined sources3
Helixi359 – 361Combined sources3
Turni362 – 365Combined sources4
Beta strandi373 – 376Combined sources4
Beta strandi381 – 383Combined sources3
Helixi385 – 388Combined sources4
Helixi392 – 398Combined sources7
Helixi404 – 419Combined sources16
Helixi424 – 441Combined sources18
Beta strandi458 – 462Combined sources5
Helixi482 – 487Combined sources6
Beta strandi489 – 495Combined sources7
Turni496 – 499Combined sources4
Beta strandi500 – 503Combined sources4
Helixi504 – 506Combined sources3
Beta strandi509 – 513Combined sources5
Helixi514 – 517Combined sources4
Beta strandi519 – 529Combined sources11
Turni530 – 533Combined sources4
Beta strandi534 – 539Combined sources6
Beta strandi544 – 553Combined sources10
Helixi555 – 557Combined sources3
Beta strandi559 – 567Combined sources9
Beta strandi569 – 572Combined sources4
Beta strandi577 – 583Combined sources7
Beta strandi588 – 591Combined sources4
Beta strandi598 – 600Combined sources3
Turni602 – 605Combined sources4
Beta strandi607 – 616Combined sources10
Helixi620 – 625Combined sources6
Beta strandi626 – 633Combined sources8
Beta strandi641 – 650Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D5UNMR-A1-119[»]
2F4MX-ray1.85A164-450[»]
2F4OX-ray2.26A164-450[»]
2G9FX-ray1.90A451-651[»]
2G9GX-ray2.00A451-651[»]
2HPJX-ray1.70A12-110[»]
2HPLX-ray1.80A12-111[»]
2I74X-ray1.75A/B471-651[»]
ProteinModelPortaliQ9JI78.
SMRiQ9JI78.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JI78.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 91PUBAdd BLAST62
Domaini451 – 651PAWPROSITE-ProRule annotationAdd BLAST201

Domaini

The PUB domain mediates the interaction with VCP.1 Publication

Sequence similaritiesi

Belongs to the transglutaminase-like superfamily. PNGase family.PROSITE-ProRule annotation
Contains 1 PAW domain.PROSITE-ProRule annotation
Contains 1 PUB (PUG) domain.Curated

Phylogenomic databases

eggNOGiKOG0909. Eukaryota.
ENOG410XP69. LUCA.
GeneTreeiENSGT00390000006540.
HOGENOMiHOG000247069.
HOVERGENiHBG082026.
InParanoidiQ9JI78.
KOiK01456.
OMAiDVAWQHT.
OrthoDBiEOG091G09YB.
PhylomeDBiQ9JI78.
TreeFamiTF315254.

Family and domain databases

InterProiIPR008979. Galactose-bd-like.
IPR006588. Peptide_N_glycanase_PAW_dom.
IPR018997. PUB_domain.
IPR002931. Transglutaminase-like.
[Graphical view]
PfamiPF04721. PAW. 1 hit.
PF09409. PUB. 1 hit.
PF01841. Transglut_core. 1 hit.
[Graphical view]
SMARTiSM00613. PAW. 1 hit.
SM00580. PUG. 1 hit.
SM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF143503. SSF143503. 1 hit.
SSF49785. SSF49785. 1 hit.
PROSITEiPS51398. PAW. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JI78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASATLGSSS SSASPAVAEL CQNTPETFLE ASKLLLTYAD NILRNPSDEK
60 70 80 90 100
YRSIRIGNTA FSTRLLPVRG AVECLFEMGF EEGETHLIFP KKASVEQLQK
110 120 130 140 150
IRDLIAIERS SRLDGSSKKV QFSQHPAAAK LPLEQSEDPA GLIRHSGNQT
160 170 180 190 200
GQLPSLPSAP MVVGDSTILK VLQSNIQHVQ LYENPVLQEK ALTCIPVSEL
210 220 230 240 250
KRKAQEKLFR ARKLDKGTNV SDEDFLLLEL LHWFKEEFFR WVNNIVCSKC
260 270 280 290 300
GGETRSRDEA LLPNDDELKW GAKNVENHYC DACQLSNRFP RYNNPEKLLE
310 320 330 340 350
TRCGRCGEWA NCFTLCCRAL GFEARYVWDY TDHVWTEVYS PSQQRWLHCD
360 370 380 390 400
ACEDVCDKPL LYEIGWGKKL SYIIAFSKDE VVDVTWRYSC KHDEVMSRRT
410 420 430 440 450
KVKEELLRET INGLNKQRQL SLSESRRKEL LQRIIVELVE FISPKTPRPG
460 470 480 490 500
ELGGRVSGSL AWRVARGETG LERKEILFIP SENEKISKQF HLRYDIVRDR
510 520 530 540 550
YIRVSDNNIN ISGWENGVWK MESIFRKVEK DWNMVYLARK EGSSFAYISW
560 570 580 590 600
KFECGSAGLK VDTVSIRTSS QSFESGSVRW KLRSETAQVN LLGDKNLRSY
610 620 630 640 650
NDFSGATEVT LEAELSRGDG DVAWQHTQLF RQSLNDSGEN GLEIIITFND

L
Length:651
Mass (Da):74,275
Last modified:September 5, 2006 - v2
Checksum:iF9D7A35726482F81
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti509I → T in AAF74723 (PubMed:10831608).Curated1
Sequence conflicti509I → T in AAP03060 (PubMed:12711318).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250927 mRNA. Translation: AAF74723.1.
AY225417 Genomic DNA. Translation: AAP03060.1.
AK003279 mRNA. Translation: BAB22686.1.
AK028248 mRNA. Translation: BAC25839.1.
BC028961 mRNA. Translation: AAH28961.1.
CCDSiCCDS26832.1.
RefSeqiNP_067479.2. NM_021504.3.
UniGeneiMm.258381.

Genome annotation databases

EnsembliENSMUST00000022310; ENSMUSP00000022310; ENSMUSG00000021785.
GeneIDi59007.
KEGGimmu:59007.
UCSCiuc007sgz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250927 mRNA. Translation: AAF74723.1.
AY225417 Genomic DNA. Translation: AAP03060.1.
AK003279 mRNA. Translation: BAB22686.1.
AK028248 mRNA. Translation: BAC25839.1.
BC028961 mRNA. Translation: AAH28961.1.
CCDSiCCDS26832.1.
RefSeqiNP_067479.2. NM_021504.3.
UniGeneiMm.258381.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D5UNMR-A1-119[»]
2F4MX-ray1.85A164-450[»]
2F4OX-ray2.26A164-450[»]
2G9FX-ray1.90A451-651[»]
2G9GX-ray2.00A451-651[»]
2HPJX-ray1.70A12-110[»]
2HPLX-ray1.80A12-111[»]
2I74X-ray1.75A/B471-651[»]
ProteinModelPortaliQ9JI78.
SMRiQ9JI78.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208478. 7 interactors.
DIPiDIP-41155N.
IntActiQ9JI78. 5 interactors.
MINTiMINT-214719.
STRINGi10090.ENSMUSP00000022310.

PTM databases

iPTMnetiQ9JI78.
PhosphoSitePlusiQ9JI78.

Proteomic databases

EPDiQ9JI78.
MaxQBiQ9JI78.
PaxDbiQ9JI78.
PeptideAtlasiQ9JI78.
PRIDEiQ9JI78.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022310; ENSMUSP00000022310; ENSMUSG00000021785.
GeneIDi59007.
KEGGimmu:59007.
UCSCiuc007sgz.1. mouse.

Organism-specific databases

CTDi55768.
MGIiMGI:1913276. Ngly1.

Phylogenomic databases

eggNOGiKOG0909. Eukaryota.
ENOG410XP69. LUCA.
GeneTreeiENSGT00390000006540.
HOGENOMiHOG000247069.
HOVERGENiHBG082026.
InParanoidiQ9JI78.
KOiK01456.
OMAiDVAWQHT.
OrthoDBiEOG091G09YB.
PhylomeDBiQ9JI78.
TreeFamiTF315254.

Enzyme and pathway databases

BRENDAi3.5.1.52. 3474.
ReactomeiR-MMU-532668. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.

Miscellaneous databases

EvolutionaryTraceiQ9JI78.
PROiQ9JI78.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021785.
CleanExiMM_NGLY1.
GenevisibleiQ9JI78. MM.

Family and domain databases

InterProiIPR008979. Galactose-bd-like.
IPR006588. Peptide_N_glycanase_PAW_dom.
IPR018997. PUB_domain.
IPR002931. Transglutaminase-like.
[Graphical view]
PfamiPF04721. PAW. 1 hit.
PF09409. PUB. 1 hit.
PF01841. Transglut_core. 1 hit.
[Graphical view]
SMARTiSM00613. PAW. 1 hit.
SM00580. PUG. 1 hit.
SM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF143503. SSF143503. 1 hit.
SSF49785. SSF49785. 1 hit.
PROSITEiPS51398. PAW. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNGLY1_MOUSE
AccessioniPrimary (citable) accession number: Q9JI78
Secondary accession number(s): Q8K113, Q9CTK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: November 2, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.