Q9PU71 · Q9PU71_XENLA

Function

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for binding site, active site.

169850100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site66Ca2+ 1 (UniProtKB | ChEBI)
Binding site74Ca2+ 1 (UniProtKB | ChEBI)
Binding site119Ca2+ 1 (UniProtKB | ChEBI)
Binding site121Ca2+ 1 (UniProtKB | ChEBI)
Binding site137Ca2+ 2 (UniProtKB | ChEBI)
Binding site140Ca2+ 2 (UniProtKB | ChEBI)
Binding site157Ca2+ 2 (UniProtKB | ChEBI)
Binding site158Ca2+ 2 (UniProtKB | ChEBI)
Binding site161Ca2+ 2 (UniProtKB | ChEBI)
Binding site233Ca2+ 3 (UniProtKB | ChEBI)
Binding site243Ca2+ 3 (UniProtKB | ChEBI)
Binding site282Ca2+ 3 (UniProtKB | ChEBI)
Active site489Charge relay system
Active site551Charge relay system
Active site645Charge relay system

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncalcium ion binding
Molecular Functionserine-type endopeptidase activity
Biological Processcomplement activation
Biological Processinnate immune response
Biological Processproteolysis

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Submitted names
    • Mannose-binding protein-associated serine protease (MASP)

Gene names

    • Name
      MASP

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus

Accessions

  • Primary accession
    Q9PU71

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, modified residue.

TypeIDPosition(s)Description
Signal1-17
ChainPRO_500433239918-698
Disulfide bond71↔89
Disulfide bond141↔155
Disulfide bond151↔164
Modified residue157(3R)-3-hydroxyasparagine
Disulfide bond166↔179
Disulfide bond183↔210
Modified residue196Phosphoserine; by CK2
Disulfide bond240↔258
Disulfide bond299↔347
Disulfide bond365↔412
Disulfide bond395↔430
Disulfide bond434↔571Interchain (between heavy and light chains)
Disulfide bond613↔630
Disulfide bond641↔671

Post-translational modification

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-136CUB
Domain183-295CUB
Domain297-362Sushi
Domain363-432Sushi
Domain447-695Peptidase S1

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    698
  • Mass (Da)
    79,415
  • Last updated
    2000-05-01 v1
  • Checksum
    79CE2FA4B774A6BE
MRIPLLFSICLWMLSEAEVIQLTDMFGEIRSLFFPDSYPSDSEVTWNITVPRGFSLKLYFMHFDLEPSYLCEYDYAKVESEDQVIANFCGKESTDTEQAPGRQIITSPSNFLSLTFRSDFSNEERFTGFDAHYSAIDIDECTEKSDEDLVCDHHCHNYIGGFYCSCRFGYLLHTDNRTCKVECSDNLFTQRSGLISSPDYPSPYAKSSDCRYRIELEEGFVINLHFDDNFDVEDHPEVKCPYDYLKIKTGKNEFGPLCGEKSPGRKETGSNTVQILFHRYNSGENGGWRLSYSVTGMPCPNLHPPMNGKLEPPQSEYTFKDQVVISCNQGYRVLKDNVEMESLQIECRKDGTWSNQIPPVQIVDCKKPKEIENGFITYSTAENRTTFQSSFNYSCREPYYMMVPNITLVYTCDASGEWTSQEIGAKIPTCQPVCGVPRFSRSALARIAGGKTAKRGISPWIAMFSDSQNNQPFCGGALISNKWIVTAAHCLHHELDTEDTDLNSLKWFELSSFKVILGKHRTLKKDDTEQTFQAKNLILHPNYKPKTFRFDIALVELSDKAFLNDYVMPICLPEKQVQQDEHVIVSGWGKHFLKRLPDSLMEVEIPVVGQTLCKTVYQTLELLVTDEMICAGFKEGGKDACSGDSGGPMVTKNELKKHWYLAGTVSWGVGCGKKIRYGMYSDVYKNLDWIKKKSGVQY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D83276
EMBL· GenBank· DDBJ
BAA86869.1
EMBL· GenBank· DDBJ
mRNA

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