| Tag | Content |
|---|
| CPLM ID | CPLM-014163 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase |
Protein Synonyms/Alias | PNGase; N-glycanase 1; Peptide:N-glycanase |
Gene Name | Ngly1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 216 | FRARKLDKGTKVSDE | ubiquitination | [1] | | 416 | ETINGLNKQRQLLLS | ubiquitination | [1] |
|
Reference | [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis. Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J. J Proteome Res. 2012 Sep 7;11(9):4722-32. [ PMID: 22871113] |
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 (By similarity). |
Sequence Annotation | DOMAIN 30 91 PUB.
DOMAIN 451 651 PAW.
ACT_SITE 306 306 Nucleophile (By similarity).
ACT_SITE 333 333 By similarity.
ACT_SITE 350 350 By similarity.
METAL 247 247 Zinc (By similarity).
METAL 250 250 Zinc (By similarity).
METAL 280 280 Zinc (By similarity).
METAL 283 283 Zinc (By similarity).
MOD_RES 2 2 N-acetylalanine (By similarity). |
Keyword | Acetylation; Alternative splicing; 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 IRDLIAVERR SRLDGSSQKV 120
EFSQHPAAVR LPAEQPEDPT GLMQHSGNQP GQPLSLPSAP LVVGDSTIFK VLQSNIQHVQ 180
LYENPVLQEK ALACIPVNEL KRKSQEKLFR ARKLDKGTKV SDEDFLLLEL LHWFKEEFFH 240
WVNNVVCSRC GRETRSRDEA LPPNDDELKW GAKNVEDHYC DACQLSNRFP RYNNPEKLLE 300
TRCGRCGEWA NCFTLCCRAL GFEARYVWDY TDHVWTEVYS PSQQRWLHCD ACEDVCDKPL 360
LYEIGWGKKL SYIIAFSKDE VVDVTWRYSC KHEEVMSRRT KVKEELLRET INGLNKQRQL 420
LLSESRRKEL LQRIIVELVE FISPKTPRPG ELGGRVSGSL AWRVARGETC LERKEILFIP 480
SENEKISKQF HLRYDIVRDR YIRVSDNNAN ISGWENGVWK MESIFRKVEK DWNMVYLARK 540
EGSSFAYISW KFECGSAGLK VDNVSIRTSS QSFETGSVRW KLRSEMAQVN LLGDRNLRSY 600
DDFCGATEVT LEAELSRGDG DVAWQHTQLF RQSLNDHAEN GLEIIITFSD L 651 |
Gene Ontology | GO:0005737; C:cytoplasm; ISS: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; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |