Q8TL28 · ULIL_METAC

Function

function

Metalloprotease which in vitro specifically cleaves IGFBP-2 to -6, insulin, and extracellular matrix proteins but not IGFBP-1 or IGF-II. Shows a preference for substrates with an arginine in the P1' position, the first position downstream of the scissile bond.

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 2 calcium ions per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Activity regulation

Inhibited by EDTA, excess zinc, and also significantly by batimastat in vitro. Is not inhibited by other metalloprotease inhibitors like phosphoramidon, captopril and galardine or those targeting other classes of proteases.

pH Dependence

Optimum pH is 7.5.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site188-189substrate
Binding site225substrate
Binding site228Zn2+ (UniProtKB | ChEBI); catalytic
Active site229Proton acceptor
Binding site232Zn2+ (UniProtKB | ChEBI); catalytic
Binding site238Zn2+ (UniProtKB | ChEBI); catalytic
Binding site240Ca2+ 1 (UniProtKB | ChEBI)
Binding site243Ca2+ 1 (UniProtKB | ChEBI)
Binding site249Ca2+ 1 (UniProtKB | ChEBI)
Binding site254Ca2+ 2 (UniProtKB | ChEBI)
Binding site256Ca2+ 2 (UniProtKB | ChEBI)
Binding site259Ca2+ 2 (UniProtKB | ChEBI)
Binding site262Ca2+ 1 (UniProtKB | ChEBI)
Binding site263Ca2+ 1 (UniProtKB | ChEBI)
Binding site295substrate

GO annotations

AspectTerm
Molecular Functionmetal ion binding
Molecular Functionmetallopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Ordered locus names
      MA_3214

Organism names

Accessions

  • Primary accession
    Q8TL28

Proteomes

PTM/Processing

Features

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

TypeIDPosition(s)Description
PropeptidePRO_0000280823?-60Removed in mature form
Signal1-?
ChainPRO_000028082461-322Ulilysin
Disulfide bond250↔277
Disulfide bond269↔297
PropeptidePRO_0000280825323-342Removed in mature form

Post-translational modification

The inactive zymogen pro-ulilysin undergoes calcium-mediated autolytic activation to the mature ulilysin. Autoproteolytic activation entails removal of the first 60 residues and of a highly charged 20-residue C-terminal tail.

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-20Disordered
Region323-342Disordered

Domain

Consists of two subdomains separated by an active site cleft containing the catalytic zinc ion.

Sequence similarities

Belongs to the peptidase M43B family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    342
  • Mass (Da)
    38,371
  • Last updated
    2002-06-01 v1
  • Checksum
    B2480CD7BB2B9574
MAEKFESRGIEEASSEVPTQRRCGAMEVHHRLLRSASYVRERDQIENLALKYKQGFRAISRMEIVKIPVVVHVVWNEEEENISDAQIQSQIDILNKDFRKLNSDVSQVPSVWSNLIADLGIEFFLATKDPNGNQTTGITRTQTSVTFFTTSDEVKFASSGGEDAWPADRYLNIWVCHVLKSEIGQDILGYAQFPGGPAETDGVVIVDAAFGTTGTALPPFDKGRTATHEIGHWLNLYHIWGDELRFEDPCSRSDEVDDTPNQADPNFGCPSYPHVSCSNGPNGDMFMNYMDYVDDKCMVMFTQGQATRVNACLDGPRSSFLARVEETEKKEAPSKREMPMPR

Mass Spectrometry

Molecular mass is 28,885 Da. Determined by Unknown.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE010299
EMBL· GenBank· DDBJ
AAM06585.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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