| Tag | Content |
|---|
| CPLM ID | CPLM-019350 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase |
Protein Synonyms/Alias | PNGase; hPNGase; N-glycanase 1; Peptide:N-glycanase |
Gene Name | NGLY1 |
Gene Synonyms/Alias | PNG1 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 123 | SNKSHKVKSSQQPAA | ubiquitination | [1] | | 401 | DTINGLNKQRQLFLS | ubiquitination | [1] |
|
Reference | [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW. Nature. 2013 Apr 18;496(7445):372-6. [ PMID: 23503661] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 30 91 PUB.
DOMAIN 454 654 PAW.
ACT_SITE 309 309 Nucleophile (By similarity).
ACT_SITE 336 336 By similarity.
ACT_SITE 353 353 By similarity.
METAL 250 250 Zinc (By similarity).
METAL 253 253 Zinc (By similarity).
METAL 283 283 Zinc (By similarity).
METAL 286 286 Zinc (By similarity).
MOD_RES 2 2 N-acetylalanine. |
Keyword | 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Polymorphism; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 654 AA |
Protein Sequence | MAAAALGSSS GSASPAVAEL CQNTPETFLE ASKLLLTYAD NILRNPNDEK YRSIRIGNTA 60
FSTRLLPVRG AVECLFEMGF EEGETHLIFP KKASVEQLQK IRDLIAIERS SRLDGSNKSH 120
KVKSSQQPAA STQLPTTPSS NPSGLNQHTR NRQGQSSDPP SASTVAADSA ILEVLQSNIQ 180
HVLVYENPAL QEKALACIPV QELKRKSQEK LSRARKLDKG INISDEDFLL LELLHWFKEE 240
FFHWVNNVLC SKCGGQTRSR DRSLLPSDDE LKWGAKEVED HYCDACQFSN RFPRYNNPEK 300
LLETRCGRCG EWANCFTLCC RAVGFEARYV WDYTELQRTL SLKLTTLKEI GKTFLRISKR 360
QKLIQVVDVT WRYSCKHEEV IARRTKVKEA LLRDTINGLN KQRQLFLSEN RRKELLQRII 420
VELVEFISPK TPKPGELGGR ISGSVAWRVA RGEMGLQRKE TLFIPCENEK ISKQLHLCYN 480
IVKDRYVRVS NNNQTISGWE NGVWKMESIF RKVETDWHMV YLARKEGSSF AYISWKFECG 540
SVGLKVDSIS IRTSSQTFQT GTVEWKLRSD TAQVELTGDN SLHSYADFSG ATEVILEAEL 600
SRGDGDVAWQ HTQLFRQSLN DHEENCLEII IKFSDL 636 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:UniProtKB. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IEA:EC. GO:0006516; P:glycoprotein catabolic process; IDA:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |