Q9BXD5 · NPL_HUMAN
- ProteinN-acetylneuraminate lyase
- GeneNPL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids320 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate (PubMed:33895133).
It prevents sialic acids from being recycled and returning to the cell surface (PubMed:33895133).
Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway (PubMed:22692205, PubMed:33895133).
Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded (Probable)
It prevents sialic acids from being recycled and returning to the cell surface (PubMed:33895133).
Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway (PubMed:22692205, PubMed:33895133).
Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded (Probable)
Catalytic activity
- aceneuramate = aldehydo-N-acetyl-D-mannosamine + pyruvate
Pathway
Amino-sugar metabolism; N-acetylneuraminate degradation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 51 | aceneuramate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 52 | aceneuramate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 143 | Proton donor | ||||
Sequence: Y | ||||||
Active site | 173 | Schiff-base intermediate with substrate | ||||
Sequence: K | ||||||
Binding site | 175 | aceneuramate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 199 | aceneuramate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 201 | aceneuramate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 202 | aceneuramate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 218 | aceneuramate (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | identical protein binding | |
Molecular Function | N-acetylneuraminate lyase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | N-acetylneuraminate catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN-acetylneuraminate lyase
- EC number
- Short namesNALase
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BXD5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 376 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000273352 | 1-320 | N-acetylneuraminate lyase | |||
Sequence: MAFPKKKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDKLDQVIIHVGALSLKESQELAQHAAEIGADGIAVIAPFFLKPWTKDILINFLKEVAAAAPALPFYYYHIPALTGVKIRAEELLDGILDKIPTFQGLKFSDTDLLDFGQCVDQNRQQQFAFLFGVDEQLLSALVMGATGAVGSTYNYLGKKTNQMLEAFEQKDFSLALNYQFCIQRFINFVVKLGFGVSQTKAIMTLVSGIPMGPPRLPLQKASREFTDSAEAKLKSLDFLSFTDLKDGNLEAGS |
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 2 is expressed in placenta, liver, kidney, pancreas, spleen, thymus, ovary, small intestine and peripheral blood leukocyte.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homotetramer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BXD5 | NPL Q9BXD5 | 4 | EBI-10287915, EBI-10287915 | |
BINARY | Q9BXD5 | NTAQ1 Q96HA8 | 3 | EBI-10287915, EBI-741158 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q9BXD5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length320
- Mass (Da)35,163
- Last updated2001-06-01 v1
- ChecksumFC0EBA9B05FE9E62
Q9BXD5-2
- Name2
- Differences from canonical
- 1-77: MAFPKKKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDK → MSRAPGILASWRRAPSLSVQKGSQTARHTCHPEVPLGNCFLPVYKASPLTVTRLWAER
Q9BXD5-3
- Name3
- Differences from canonical
- 260-320: GFGVSQTKAIMTLVSGIPMGPPRLPLQKASREFTDSAEAKLKSLDFLSFTDLKDGNLEAGS → ENSKLKVSKNQRTLPLGTTNFPFLH
Q9BXD5-4
- Name4
Q9BXD5-5
- Name5
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A087WZ70 | A0A087WZ70_HUMAN | NPL | 230 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_022518 | 1-77 | in isoform 2 | |||
Sequence: MAFPKKKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTTGEGLSLSVSERRQVAEEWVTKGKDK → MSRAPGILASWRRAPSLSVQKGSQTARHTCHPEVPLGNCFLPVYKASPLTVTRLWAER | ||||||
Sequence conflict | 4 | in Ref. 5; BC034966 | ||||
Sequence: P → S | ||||||
Alternative sequence | VSP_022519 | 78-109 | in isoform 5 | |||
Sequence: LDQVIIHVGALSLKESQELAQHAAEIGADGIA → SNHHKLGTIRTTQSRQSSFRRQLKAWHSGSHL | ||||||
Sequence conflict | 98 | in Ref. 5; BC042003 | ||||
Sequence: Q → E | ||||||
Alternative sequence | VSP_022520 | 110-320 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022521 | 203-246 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 212 | in Ref. 5; BC042003 | ||||
Sequence: A → E | ||||||
Sequence conflict | 260 | in Ref. 3; BAG36036 | ||||
Sequence: G → V | ||||||
Alternative sequence | VSP_022522 | 260-320 | in isoform 3 and isoform 4 | |||
Sequence: GFGVSQTKAIMTLVSGIPMGPPRLPLQKASREFTDSAEAKLKSLDFLSFTDLKDGNLEAGS → ENSKLKVSKNQRTLPLGTTNFPFLH |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF338436 EMBL· GenBank· DDBJ | AAK25795.1 EMBL· GenBank· DDBJ | mRNA | ||
AY336748 EMBL· GenBank· DDBJ | AAQ82432.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313225 EMBL· GenBank· DDBJ | BAG36036.1 EMBL· GenBank· DDBJ | mRNA | ||
AL355999 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL513344 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC034966 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC042003 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC058003 EMBL· GenBank· DDBJ | AAH58003.1 EMBL· GenBank· DDBJ | mRNA | ||
BC125051 EMBL· GenBank· DDBJ | AAI25052.1 EMBL· GenBank· DDBJ | mRNA |