Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

Ngly1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi247 – 2471ZincBy similarity
Metal bindingi250 – 2501ZincBy similarity
Metal bindingi280 – 2801ZincBy similarity
Metal bindingi283 – 2831ZincBy similarity
Active sitei306 – 3061NucleophileBy similarity
Active sitei333 – 3331By similarity
Active sitei350 – 3501By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.1.52. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC:3.5.1.52)
Short name:
PNGase
Alternative name(s):
N-glycanase 1
Peptide:N-glycanase
Gene namesi
Name:Ngly1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi1308518. Ngly1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 651650Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidasePRO_0000248974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ5XI55.
PRIDEiQ5XI55.

PTM databases

iPTMnetiQ5XI55.
PhosphoSiteiQ5XI55.

Expressioni

Gene expression databases

GenevisibleiQ5XI55. RN.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi262367. 1 interaction.
STRINGi10116.ENSRNOP00000008289.

Structurei

3D structure databases

ProteinModelPortaliQ5XI55.
SMRiQ5XI55. Positions 19-119, 164-450, 454-651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 9162PUBAdd
BLAST
Domaini451 – 651201PAWPROSITE-ProRule annotationAdd
BLAST

Domaini

The PUB domain mediates the interaction with VCP.By similarity

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.
InParanoidiQ5XI55.
KOiK01456.
OMAiRVEDHYC.
OrthoDBiEOG780RMR.
PhylomeDBiQ5XI55.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5XI55-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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
IRDLIAVERR SRLDGSSQKV EFSQHPAAVR LPAEQPEDPT GLMQHSGNQP
160 170 180 190 200
GQPLSLPSAP LVVGDSTIFK VLQSNIQHVQ LYENPVLQEK ALACIPVNEL
210 220 230 240 250
KRKSQEKLFR ARKLDKGTKV SDEDFLLLEL LHWFKEEFFH WVNNVVCSRC
260 270 280 290 300
GRETRSRDEA LPPNDDELKW GAKNVEDHYC DACQLSNRFP RYNNPEKLLE
310 320 330 340 350
TRCGRCGEWA NCFTLCCRAL GFEARYVWDY TDHVWTEVYS PSQQRWLHCD
360 370 380 390 400
ACEDVCDKPL LYEIGWGKKL SYIIAFSKDE VVDVTWRYSC KHEEVMSRRT
410 420 430 440 450
KVKEELLRET INGLNKQRQL LLSESRRKEL LQRIIVELVE FISPKTPRPG
460 470 480 490 500
ELGGRVSGSL AWRVARGETC LERKEILFIP SENEKISKQF HLRYDIVRDR
510 520 530 540 550
YIRVSDNNAN ISGWENGVWK MESIFRKVEK DWNMVYLARK EGSSFAYISW
560 570 580 590 600
KFECGSAGLK VDNVSIRTSS QSFETGSVRW KLRSEMAQVN LLGDRNLRSY
610 620 630 640 650
DDFCGATEVT LEAELSRGDG DVAWQHTQLF RQSLNDHAEN GLEIIITFSD

L
Length:651
Mass (Da):74,677
Last modified:September 5, 2006 - v2
Checksum:i7F080A86D9A4E870
GO
Isoform 2 (identifier: Q5XI55-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     594-651: DRNLRSYDDFCGATEVTLEAELSRGDGDVAWQHTQLFRQSLNDHAENGLEIIITFSDL → GRSRQKSAFL

Note: No experimental confirmation available.
Show »
Length:603
Mass (Da):69,242
Checksum:i12BDDE24D4BEA5A2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei594 – 65158DRNLR…TFSDL → GRSRQKSAFL in isoform 2. 1 PublicationVSP_020347Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03096885 Genomic DNA. No translation available.
AABR03096708 Genomic DNA. No translation available.
AABR03096256 Genomic DNA. No translation available.
BC083837 mRNA. Translation: AAH83837.1.
RefSeqiNP_001014158.1. NM_001014136.1. [Q5XI55-2]
UniGeneiRn.108552.

Genome annotation databases

EnsembliENSRNOT00000008289; ENSRNOP00000008289; ENSRNOG00000006143. [Q5XI55-1]
GeneIDi361014.
KEGGirno:361014.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03096885 Genomic DNA. No translation available.
AABR03096708 Genomic DNA. No translation available.
AABR03096256 Genomic DNA. No translation available.
BC083837 mRNA. Translation: AAH83837.1.
RefSeqiNP_001014158.1. NM_001014136.1. [Q5XI55-2]
UniGeneiRn.108552.

3D structure databases

ProteinModelPortaliQ5XI55.
SMRiQ5XI55. Positions 19-119, 164-450, 454-651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi262367. 1 interaction.
STRINGi10116.ENSRNOP00000008289.

PTM databases

iPTMnetiQ5XI55.
PhosphoSiteiQ5XI55.

Proteomic databases

PaxDbiQ5XI55.
PRIDEiQ5XI55.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000008289; ENSRNOP00000008289; ENSRNOG00000006143. [Q5XI55-1]
GeneIDi361014.
KEGGirno:361014.

Organism-specific databases

CTDi55768.
RGDi1308518. Ngly1.

Phylogenomic databases

eggNOGiKOG0909. Eukaryota.
ENOG410XP69. LUCA.
GeneTreeiENSGT00390000006540.
HOGENOMiHOG000247069.
HOVERGENiHBG082026.
InParanoidiQ5XI55.
KOiK01456.
OMAiRVEDHYC.
OrthoDBiEOG780RMR.
PhylomeDBiQ5XI55.

Enzyme and pathway databases

BRENDAi3.5.1.52. 5301.

Miscellaneous databases

NextBioi674886.
PROiQ5XI55.

Gene expression databases

GenevisibleiQ5XI55. RN.

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...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.

Entry informationi

Entry nameiNGLY1_RAT
AccessioniPrimary (citable) accession number: Q5XI55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: May 11, 2016
This is version 89 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

Complete proteome, Reference proteome

Documents

  1. 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.