| Tag | Content |
|---|
| CPLM ID | CPLM-021747 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase |
Protein Synonyms/Alias | PNGase; mPNGase; N-glycanase 1; Peptide:N-glycanase |
Gene Name | Ngly1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 50 | LRNPSDEKYRSIRIG | ubiquitination | [1] | | 119 | RLDGSSKKVQFSQHP | ubiquitination | [1] | | 130 | SQHPAAAKLPLEQSE | ubiquitination | [1] | | 201 | CIPVSELKRKAQEKL | ubiquitination | [1] | | 269 | LPNDDELKWGAKNVE | ubiquitination | [1] | | 273 | DELKWGAKNVENHYC | ubiquitination | [1] | | 403 | MSRRTKVKEELLRET | ubiquitination | [1] | | 416 | ETINGLNKQRQLSLS | ubiquitination | [1] | | 474 | GETGLERKEILFIPS | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
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 451 651 PAW.
ACT_SITE 306 306 Nucleophile.
ACT_SITE 333 333
ACT_SITE 350 350
METAL 247 247 Zinc.
METAL 250 250 Zinc.
METAL 280 280 Zinc.
METAL 283 283 Zinc.
MOD_RES 2 2 N-acetylalanine (By similarity). |
Keyword | 3D-structure; Acetylation; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 651 AA |
Protein Sequence | MASATLGSSS SSASPAVAEL CQNTPETFLE ASKLLLTYAD NILRNPSDEK YRSIRIGNTA 60
FSTRLLPVRG AVECLFEMGF EEGETHLIFP KKASVEQLQK IRDLIAIERS SRLDGSSKKV 120
QFSQHPAAAK LPLEQSEDPA GLIRHSGNQT GQLPSLPSAP MVVGDSTILK VLQSNIQHVQ 180
LYENPVLQEK ALTCIPVSEL KRKAQEKLFR ARKLDKGTNV SDEDFLLLEL LHWFKEEFFR 240
WVNNIVCSKC GGETRSRDEA LLPNDDELKW GAKNVENHYC DACQLSNRFP RYNNPEKLLE 300
TRCGRCGEWA NCFTLCCRAL GFEARYVWDY TDHVWTEVYS PSQQRWLHCD ACEDVCDKPL 360
LYEIGWGKKL SYIIAFSKDE VVDVTWRYSC KHDEVMSRRT KVKEELLRET INGLNKQRQL 420
SLSESRRKEL LQRIIVELVE FISPKTPRPG ELGGRVSGSL AWRVARGETG LERKEILFIP 480
SENEKISKQF HLRYDIVRDR YIRVSDNNIN ISGWENGVWK MESIFRKVEK DWNMVYLARK 540
EGSSFAYISW KFECGSAGLK VDTVSIRTSS QSFESGSVRW KLRSETAQVN LLGDKNLRSY 600
NDFSGATEVT LEAELSRGDG DVAWQHTQLF RQSLNDSGEN GLEIIITFND L 651 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:UniProtKB. GO:0005634; C:nucleus; ISS:MGI. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; ISS:MGI. GO:0006516; P:glycoprotein catabolic process; IDA:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |