CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015727
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase 
Protein Synonyms/Alias
 Peptide:N-glycanase 
Gene Name
 Pngl 
Gene Synonyms/Alias
 PNGase; CG7865 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
517QKAQFSSKNIFRKVEacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702
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 34 97 PUB.
 DOMAIN 441 631 PAW.
 ACT_SITE 296 296 Nucleophile (By similarity).
 ACT_SITE 323 323 By similarity.
 ACT_SITE 340 340 By similarity.
 METAL 246 246 Zinc (By similarity).
 METAL 249 249 Zinc (By similarity).
 METAL 272 272 Zinc (By similarity).
 METAL 273 273 Zinc (By similarity).
 MOD_RES 126 126 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 631 AA 
Protein Sequence
MVDINLECVH QIEPKTRSAG QQQQERGLKE AYLEAVRILL VLLENILAQP ENSMFRTIRQ 60
ENKAIKEKLL SLPGCERLLE AIGFVRAPSS NAYTLPTEVS LQQVKKYRDA LSERRTAWLN 120
GTVSKSPPQQ STTSTTPLFI KPSVEYRHRI AFPRVLRTNN NFLQSLELYS DAVMQYEDNL 180
LLATGRTLIP VEELTEMASE KLIDIQDQIA SGERQEKEPC VRDLLLVELV NWFNTQFFQW 240
VNNIPCRVCG SEESRLRRTE REGDIRVEVT VCCGQESKFY RYNDISQLLV SRKGRCGEYA 300
NCFTFLCRAL DYDARIVHSH FDHVWTEVYS EAQMRWLHVD PSENVIDSPL MYQHGWKRHI 360
DYILAYSRDD IQDVTWRYTN DHQKILHLRK LCGEKEMVQT LDAIRAKRRQ NCTADRKLFL 420
SQRNMYEVIG LTLERKPTEN ELKGRSSGSL SWRQSRGEHT FTNIFVFNLS ATELQKRQLN 480
VRYSCATDTY ERYAKEGEHI TILDSYKTWQ KAQFSSKNIF RKVERDWKMA YLARLEDTDC 540
GEIAWTFDFS KTNLKVKSYN LVFETKTFGD GKISVTVDAT DGSASVENAT GFKIVAKLTG 600
GKGDVAWQHT QLFRQSLNSR DYPFDLQVQL H 631 
Gene Ontology
 GO:0005829; C:cytosol; IDA:FlyBase.
 GO:0030246; F:carbohydrate binding; IDA:FlyBase.
 GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB. 
Interpro
 IPR008979; Galactose-bd-like.
 IPR006588; Peptide_N_glycanase_PAW_dom.
 IPR018997; PUB_domain.
 IPR006567; PUG-dom.
 IPR002931; Transglutaminase-like. 
Pfam
 PF09409; PUB
 PF01841; Transglut_core 
SMART
 SM00613; PAW
 SM00580; PUG
 SM00460; TGc 
PROSITE
 PS51398; PAW 
PRINTS