Q9PU71 · Q9PU71_XENLA
- ProteinMannose-binding protein-associated serine protease (MASP)
- GeneMASP
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids698 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
Function
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 66 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 74 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 119 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 121 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 137 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 140 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 157 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 158 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 161 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 233 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 243 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 282 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 489 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 551 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 645 | Charge relay system | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | calcium ion binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | complement activation | |
Biological Process | innate immune response | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionQ9PU71
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MRIPLLFSICLWMLSEA | ||||||
Chain | PRO_5004332399 | 18-698 | ||||
Sequence: EVIQLTDMFGEIRSLFFPDSYPSDSEVTWNITVPRGFSLKLYFMHFDLEPSYLCEYDYAKVESEDQVIANFCGKESTDTEQAPGRQIITSPSNFLSLTFRSDFSNEERFTGFDAHYSAIDIDECTEKSDEDLVCDHHCHNYIGGFYCSCRFGYLLHTDNRTCKVECSDNLFTQRSGLISSPDYPSPYAKSSDCRYRIELEEGFVINLHFDDNFDVEDHPEVKCPYDYLKIKTGKNEFGPLCGEKSPGRKETGSNTVQILFHRYNSGENGGWRLSYSVTGMPCPNLHPPMNGKLEPPQSEYTFKDQVVISCNQGYRVLKDNVEMESLQIECRKDGTWSNQIPPVQIVDCKKPKEIENGFITYSTAENRTTFQSSFNYSCREPYYMMVPNITLVYTCDASGEWTSQEIGAKIPTCQPVCGVPRFSRSALARIAGGKTAKRGISPWIAMFSDSQNNQPFCGGALISNKWIVTAAHCLHHELDTEDTDLNSLKWFELSSFKVILGKHRTLKKDDTEQTFQAKNLILHPNYKPKTFRFDIALVELSDKAFLNDYVMPICLPEKQVQQDEHVIVSGWGKHFLKRLPDSLMEVEIPVVGQTLCKTVYQTLELLVTDEMICAGFKEGGKDACSGDSGGPMVTKNELKKHWYLAGTVSWGVGCGKKIRYGMYSDVYKNLDWIKKKSGVQY | ||||||
Disulfide bond | 71↔89 | |||||
Sequence: CEYDYAKVESEDQVIANFC | ||||||
Disulfide bond | 141↔155 | |||||
Sequence: CTEKSDEDLVCDHHC | ||||||
Disulfide bond | 151↔164 | |||||
Sequence: CDHHCHNYIGGFYC | ||||||
Modified residue | 157 | (3R)-3-hydroxyasparagine | ||||
Sequence: N | ||||||
Disulfide bond | 166↔179 | |||||
Sequence: CRFGYLLHTDNRTC | ||||||
Disulfide bond | 183↔210 | |||||
Sequence: CSDNLFTQRSGLISSPDYPSPYAKSSDC | ||||||
Modified residue | 196 | Phosphoserine; by CK2 | ||||
Sequence: S | ||||||
Disulfide bond | 240↔258 | |||||
Sequence: CPYDYLKIKTGKNEFGPLC | ||||||
Disulfide bond | 299↔347 | |||||
Sequence: CPNLHPPMNGKLEPPQSEYTFKDQVVISCNQGYRVLKDNVEMESLQIEC | ||||||
Disulfide bond | 365↔412 | |||||
Sequence: CKKPKEIENGFITYSTAENRTTFQSSFNYSCREPYYMMVPNITLVYTC | ||||||
Disulfide bond | 395↔430 | |||||
Sequence: CREPYYMMVPNITLVYTCDASGEWTSQEIGAKIPTC | ||||||
Disulfide bond | 434↔571 | Interchain (between heavy and light chains) | ||||
Sequence: CGVPRFSRSALARIAGGKTAKRGISPWIAMFSDSQNNQPFCGGALISNKWIVTAAHCLHHELDTEDTDLNSLKWFELSSFKVILGKHRTLKKDDTEQTFQAKNLILHPNYKPKTFRFDIALVELSDKAFLNDYVMPIC | ||||||
Disulfide bond | 613↔630 | |||||
Sequence: CKTVYQTLELLVTDEMIC | ||||||
Disulfide bond | 641↔671 | |||||
Sequence: CSGDSGGPMVTKNELKKHWYLAGTVSWGVGC |
Post-translational modification
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-136 | CUB | ||||
Sequence: CLWMLSEAEVIQLTDMFGEIRSLFFPDSYPSDSEVTWNITVPRGFSLKLYFMHFDLEPSYLCEYDYAKVESEDQVIANFCGKESTDTEQAPGRQIITSPSNFLSLTFRSDFSNEERFTGFDAHYSAI | ||||||
Domain | 183-295 | CUB | ||||
Sequence: CSDNLFTQRSGLISSPDYPSPYAKSSDCRYRIELEEGFVINLHFDDNFDVEDHPEVKCPYDYLKIKTGKNEFGPLCGEKSPGRKETGSNTVQILFHRYNSGENGGWRLSYSVT | ||||||
Domain | 297-362 | Sushi | ||||
Sequence: MPCPNLHPPMNGKLEPPQSEYTFKDQVVISCNQGYRVLKDNVEMESLQIECRKDGTWSNQIPPVQI | ||||||
Domain | 363-432 | Sushi | ||||
Sequence: VDCKKPKEIENGFITYSTAENRTTFQSSFNYSCREPYYMMVPNITLVYTCDASGEWTSQEIGAKIPTCQP | ||||||
Domain | 447-695 | Peptidase S1 | ||||
Sequence: IAGGKTAKRGISPWIAMFSDSQNNQPFCGGALISNKWIVTAAHCLHHELDTEDTDLNSLKWFELSSFKVILGKHRTLKKDDTEQTFQAKNLILHPNYKPKTFRFDIALVELSDKAFLNDYVMPICLPEKQVQQDEHVIVSGWGKHFLKRLPDSLMEVEIPVVGQTLCKTVYQTLELLVTDEMICAGFKEGGKDACSGDSGGPMVTKNELKKHWYLAGTVSWGVGCGKKIRYGMYSDVYKNLDWIKKKSG |
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length698
- Mass (Da)79,415
- Last updated2000-05-01 v1
- Checksum79CE2FA4B774A6BE