Q9NL38 · MA66_PINMA

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

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site154Zn2+ (UniProtKB | ChEBI); catalytic
Binding site156Zn2+ (UniProtKB | ChEBI); catalytic
Binding site179Zn2+ (UniProtKB | ChEBI); catalytic
Binding site506-507substrate

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncarbonate dehydratase activity
Molecular Functionzinc ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Organism names

Accessions

  • Primary accession
    Q9NL38

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-22
ChainPRO_000037979123-568N66 matrix protein
Glycosylation389N-linked (GlcNAc...) asparagine
Glycosylation511N-linked (GlcNAc...) asparagine

Keywords

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.

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain55-567Alpha-carbonic anhydrase
Compositional bias259-419Polar residues
Region259-421Disordered

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    568
  • Mass (Da)
    62,376
  • Last updated
    2000-10-01 v1
  • Checksum
    4AD9242A96EB642F
MWRMTTLLHLTALLVLIPLCHCASMHRHDHYMDMDQTYPNGLGYCEPSGESSCKAGFSYNRDICQGPYHWHTISSCYKACGHKRRQSPINIWSHKAVFLPYLPRLKFKPHMKSLDTDVTNHQNRAPEFEPEDGDKLHVKLKNLVDGHYKFHNLHIHNGKSRRKGSEHSVNRHFTPMEAHLVFHHDDKKEIKPPRVKLGGVYAGRNKFVVVGVFLEVGDEGYGDEPDDDECKRILKGHCENNGDNGNNCDNGNNGNNDNNGNNGNNGNGNNGYNGNNGDNGNNGNGNGNNGYNGNNGYNGNNGNNGNGNNDNNGNDNNGNNGGNGNNGNNGNGNNGNNGNGNNGNNGGNGNNGNNGNSNNGNNGNGNNGNNGGNGNNGNNGNGNNENNGNGSNGNNGGNGNNGNNGDNGNGDNGYNGDNGNSDGRLRRWDLANVRRMHAERYHFSGGCIVKKAKRLSRILECAYRHKKVREFKRNGEEKGLDVDITPEMVLPPMKYRHYYTYEGSLTTPPCNETVLWVVEKCHVQVSRRVLDALRNVEGYEDGTTLSKYGTRRPTQRNKHPLRVYKNSI

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict34-37in Ref. 1; AA sequence
Compositional bias259-419Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB032613
EMBL· GenBank· DDBJ
BAA90540.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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