Q9NL38 · MA66_PINMA
- ProteinN66 matrix protein
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids568 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Acts as a negative regulator for calcification in the shells of mollusks. May function both as a calcium concentrator and as a carbonic anhydrase required for production of carbonate ions, which are assembled to CaCO3 at mineralization sites. Is important for shell formation in both the calcitic prismatic layer and the aragonitic nacreous layer (By similarity).
Miscellaneous
Sulfite and sialic acid may provide the necessary negative charge in the N-glycan to promote calcium uptake.
Catalytic activity
- H+ + hydrogencarbonate = CO2 + H2O
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | carbonate dehydratase activity | |
Molecular Function | zinc ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameN66 matrix protein
- EC number
Organism names
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Mollusca > Bivalvia > Autobranchia > Pteriomorphia > Pterioida > Pterioidea > Pteriidae > Pinctada
Accessions
- Primary accessionQ9NL38
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MWRMTTLLHLTALLVLIPLCHC | ||||||
Chain | PRO_0000379791 | 23-568 | N66 matrix protein | |||
Sequence: ASMHRHDHYMDMDQTYPNGLGYCEPSGESSCKAGFSYNRDICQGPYHWHTISSCYKACGHKRRQSPINIWSHKAVFLPYLPRLKFKPHMKSLDTDVTNHQNRAPEFEPEDGDKLHVKLKNLVDGHYKFHNLHIHNGKSRRKGSEHSVNRHFTPMEAHLVFHHDDKKEIKPPRVKLGGVYAGRNKFVVVGVFLEVGDEGYGDEPDDDECKRILKGHCENNGDNGNNCDNGNNGNNDNNGNNGNNGNGNNGYNGNNGDNGNNGNGNGNNGYNGNNGYNGNNGNNGNGNNDNNGNDNNGNNGGNGNNGNNGNGNNGNNGNGNNGNNGGNGNNGNNGNSNNGNNGNGNNGNNGGNGNNGNNGNGNNENNGNGSNGNNGGNGNNGNNGDNGNGDNGYNGDNGNSDGRLRRWDLANVRRMHAERYHFSGGCIVKKAKRLSRILECAYRHKKVREFKRNGEEKGLDVDITPEMVLPPMKYRHYYTYEGSLTTPPCNETVLWVVEKCHVQVSRRVLDALRNVEGYEDGTTLSKYGTRRPTQRNKHPLRVYKNSI | ||||||
Glycosylation | 389 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 511 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Expression
Tissue specificity
Expressed in both the dorsal region of the mantle and the mantle edge. Is dispersed in calcium carbonate and also linked by disulfide bonds to the organic core of nacre.
Interaction
Subunit
Homooligomer; disulfide-linked. May also be disulfide-linked to insoluble organic matrix.
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 55-567 | Alpha-carbonic anhydrase | ||||
Sequence: AGFSYNRDICQGPYHWHTISSCYKACGHKRRQSPINIWSHKAVFLPYLPRLKFKPHMKSLDTDVTNHQNRAPEFEPEDGDKLHVKLKNLVDGHYKFHNLHIHNGKSRRKGSEHSVNRHFTPMEAHLVFHHDDKKEIKPPRVKLGGVYAGRNKFVVVGVFLEVGDEGYGDEPDDDECKRILKGHCENNGDNGNNCDNGNNGNNDNNGNNGNNGNGNNGYNGNNGDNGNNGNGNGNNGYNGNNGYNGNNGNNGNGNNDNNGNDNNGNNGGNGNNGNNGNGNNGNNGNGNNGNNGGNGNNGNNGNSNNGNNGNGNNGNNGGNGNNGNNGNGNNENNGNGSNGNNGGNGNNGNNGDNGNGDNGYNGDNGNSDGRLRRWDLANVRRMHAERYHFSGGCIVKKAKRLSRILECAYRHKKVREFKRNGEEKGLDVDITPEMVLPPMKYRHYYTYEGSLTTPPCNETVLWVVEKCHVQVSRRVLDALRNVEGYEDGTTLSKYGTRRPTQRNKHPLRVYKNS | ||||||
Compositional bias | 259-419 | Polar residues | ||||
Sequence: NGNNGNNGNGNNGYNGNNGDNGNNGNGNGNNGYNGNNGYNGNNGNNGNGNNDNNGNDNNGNNGGNGNNGNNGNGNNGNNGNGNNGNNGGNGNNGNNGNSNNGNNGNGNNGNNGGNGNNGNNGNGNNENNGNGSNGNNGGNGNNGNNGDNGNGDNGYNGDNG | ||||||
Region | 259-421 | Disordered | ||||
Sequence: NGNNGNNGNGNNGYNGNNGDNGNNGNGNGNNGYNGNNGYNGNNGNNGNGNNDNNGNDNNGNNGGNGNNGNNGNGNNGNNGNGNNGNNGGNGNNGNNGNSNNGNNGNGNNGNNGGNGNNGNNGNGNNENNGNGSNGNNGGNGNNGNNGDNGNGDNGYNGDNGNS |
Sequence similarities
Belongs to the alpha-carbonic anhydrase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length568
- Mass (Da)62,376
- Last updated2000-10-01 v1
- Checksum4AD9242A96EB642F
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 34-37 | in Ref. 1; AA sequence | ||||
Sequence: MDQT → GRQW | ||||||
Compositional bias | 259-419 | Polar residues | ||||
Sequence: NGNNGNNGNGNNGYNGNNGDNGNNGNGNGNNGYNGNNGYNGNNGNNGNGNNDNNGNDNNGNNGGNGNNGNNGNGNNGNNGNGNNGNNGGNGNNGNNGNSNNGNNGNGNNGNNGGNGNNGNNGNGNNENNGNGSNGNNGGNGNNGNNGDNGNGDNGYNGDNG |
Keywords
- Technical term