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png-1

Gene
png-1
Protein
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
Organism
Caenorhabditis elegans
Length
606 amino acids
Function
Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation (PubMed:17509531, PubMed:17522090). Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp (PubMed:17522090). Prefers proteins containing high-mannose over those bearing complex type oligosaccharides (PubMed:17522090). 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 (PubMed:17509531). Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (PubMed:17509531). Also displays oxidoreductase (thioredoxin) activity (PubMed:17509531, PubMed:17522090). Involved in regulating the expression of proteasomal subunits such as rpt-3 in order to confer resistance to proteasomal dysfunction (PubMed:27528192).
Similarity
Belongs to the transglutaminase-like superfamily. PNGase family.
Mass
69.148 kDa
Sequence
MPVTEVGSLPELNNILERSDANRLIIIDFFANWCGPCRMISPIFEQFSAEYGNATFLKVNCDVARDIVQRYNISAMPTFIFLKNRQQVDMVRGANQQAIAEKIRQHYSPTPANPNAASDSEKRFLEQFVKCSNVPRSYQDEVFKALARSVMPEELVGRAMTEGPRDEKAILKDLLHWFKTQFFTWFDRPTCPKCTLKCSTDGLQGTPTREEQKEGGASRVEVYICDGCNTEMRFPRYNNPAKLLQTRTGRCGEWANCFGLLLAALNLESRFIYDTTDHVWNEVYLLAEQRWCHVDPCENTMDRPLLYTRGWGKTLGYCIGYGSDHVVDVTWRYIWDSKKLVTQRNEVRQPVFENFLSKLNSRQAEGQTEPRKRELAVRRVCELMEMMAQEAKNHKIGWEKIGDDLGGRITGSEEWRRERGELGESGPKLLAEPIKLAPPTGPAQNYLEFNYDVITDTYSQPPEIGFSAQAFELENVQRVEETDWNMTYLCRKRGDAPGNISWHFDLKSLKKSIEKIEIRMAGIQKFEKGKAMAIACLGDSCMRLPIDCSALTIEDPKNAEILKITATLSGGEGAIGFQQAQIFRTELKRGGGARTESFSVKIWMKN

Gene
png-1
Protein
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase
Organism
Caenorhabditis briggsae
Length
602 amino acids
Function
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. Also displays oxidoreductase (thioredoxin) activity (By similarity).
Similarity
Belongs to the transglutaminase-like superfamily. PNGase family.
Mass
69.212 kDa
Sequence
MPVREVSRLPELNEILEKSDSNRLIIVDFFANWCGPCRMISPAFERLSMEFGNATFLKVNTDLARDIVMRYSISAMPTFLFFKNKQQVDSVRGANESAIISTIRKHYSSTPANPNAASDEEKKFLERFVGYTELRKMHTDEVFKALARSVMPDGISDRLENGEDEKKVLQELLDWFKNDFFTWFDRPTCLKCTLKCTTEGLNGTPTKEEKEGGAGRVEVFICNGCNSEMRFPRYNDPSKLLQTRTGRCGEWANCFGLILSAAGLENRFVLDTTDHVWNEVYLKKEQRWIHVDPCENTMDRPLLYTRGWKKQLKYCIAYGHDHVTDVTWRYVFDSKKLVTQERVRQGVLENFLGKLNARQMAGATEERKRELAVRRVCELMGMMVQEAKNQRIGWEKLGEDMGGRTTGSKEWRRARGELGDNPEAQVLGKPIEFRIQNDANHVEFSYDVNRDSYSQTPEKGFVAQTFECNNIQRKVENDWKMVYLCREDGKKEGNISWHFNLAPLVATDSKKTIEKVEIRMAGIRKFENGNILIIACLGDTCMRIPASGNLTIEDPKPEVLKITVTLSGGERNQAFQHAQLFRTEKDDVAEATESMVVRVYMK