Q90YC2 · MMP21_CYNPY

Function

function

May play a role in gastrulation-related cell movement (PubMed:11606053).
Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway (By similarity).

Cofactor

Protein has several cofactor binding sites:
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Features

Showing features for binding site, active site.

161650100150200250300350400450500550600
TypeIDPosition(s)Description
Binding site141Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site329Zn2+ (UniProtKB | ChEBI); catalytic
Active site330
Binding site333Zn2+ (UniProtKB | ChEBI); catalytic
Binding site339Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentextracellular matrix
Cellular Componentextracellular space
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processcollagen catabolic process
Biological Processdetermination of heart left/right asymmetry
Biological Processdetermination of left/right symmetry
Biological Processextracellular matrix organization
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Matrix metalloproteinase-21
  • EC number
  • Short names
    MMP-21

Gene names

    • Name
      MMP21

Organism names

Accessions

  • Primary accession
    Q90YC2

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, glycosylation, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-22
PropeptidePRO_000002884223-192
Glycosylation161N-linked (GlcNAc...) asparagine
Glycosylation172N-linked (GlcNAc...) asparagine
Glycosylation181N-linked (GlcNAc...) asparagine
ChainPRO_0000028843193-616Matrix metalloproteinase-21
Disulfide bond375↔606
Glycosylation418N-linked (GlcNAc...) asparagine
Glycosylation597N-linked (GlcNAc...) asparagine

Post-translational modification

The precursor is cleaved by a furin endopeptidase.

Keywords

PTM databases

Expression

Developmental stage

Detected during early embryogenesis, then, gradually decreased, but increased again starting in late gastrula. There are regional diiferences in the level of expression at late gastrula: the involved archenteron roof is the predominant site, while there is weak expression in the neuroectoderm and epidermal ectoderm.

Structure

Family & Domains

Features

Showing features for motif, region, repeat.

TypeIDPosition(s)Description
Motif139-146Cysteine switch
Region157-186Disordered
Repeat376-435Hemopexin 1
Repeat437-493Hemopexin 2
Repeat494-542Hemopexin 3
Repeat549-605Hemopexin 4

Domain

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    616
  • Mass (Da)
    70,428
  • Last updated
    2001-12-01 v1
  • Checksum
    ABFC72D8B13E5003
MPTAPALGALLLLLGALTPGHQEKLFHSRDHSDLQPSPQHQAELVTDLQSAQQFLSKYGWTEPVKWEGTSSKNAAELPRYGDADLMQEGASISRYGQEFPLEPTQAPAFVEALRKFQTLNGLPATGKLDDSTIAAMNKPRCGVPDNQIGKESAIVKSNSNNVTEKASGKSLNTTTNQNPENGTSTSKIRKKRFLQMLAAPVRYKDQANQGSTVRGAFSKKLLKWRLIGEGYSSQLSIDEQRYVFKTAFRMWSEVMPLDFEEDLTSPMSLIDVKLGFGRGRHLGCTRSFDGSGQEFAHAWFLGDIHFDDDEHFTAPSSDSGISLLKVAVHEIGHVLGLSHIYQTGSIMQPNYIPQEAGFELDWTDRKAIQMLYGTCEGSFDAVFDWIWKERNQYGELVLRYNTYFFRNAWYWLYENRKNRTRYGDPVTVSLGWHGIPAEGIDAFVHVWTWTEDATYFFKGTQYWRYDSENDQAYIKDAQGNQYPRLISEGFPKIPSPINTAFFDRRDQFIYFFKDAHVYAFDVKRNMVANHYPKRIIDVFPAVVRNNHPFGNIDAAYYAYTHNSIFLFKGKEYWKVVSDKDRQQNPKLPRNGLFLKKNISEQWTDICNVHSSMLKMR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB054185
EMBL· GenBank· DDBJ
BAB62075.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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