A0A4W4EEX1 · A0A4W4EEX1_ELEEL
- ProteinComplement component 1, s subcomponent.1
- Genec1s.2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids673 (go to sequence)
- Protein existencePredicted
- Annotation score2/5
Function
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 60 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 68 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 114 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 116 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 132 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 133 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 135 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 149 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 150 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 153 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 223 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 231 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Binding site | 268 | Ca2+ 3 (UniProtKB | ChEBI) | |||
Active site | 462 | Charge relay system | |||
Active site | 515 | Charge relay system | |||
Active site | 616 | Charge relay system | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | blood microparticle | |
Molecular Function | calcium ion binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | complement activation, classical pathway | |
Biological Process | innate immune response | |
Biological Process | zymogen activation |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Gymnotiformes > Gymnotoidei > Gymnotidae > Electrophorus
Accessions
- Primary accessionA0A4W4EEX1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-16 | ||||
Chain | PRO_5021212695 | 17-673 | |||
Disulfide bond | 65↔83 | ||||
Disulfide bond | 136↔147 | ||||
Disulfide bond | 143↔156 | ||||
Modified residue | 149 | (3R)-3-hydroxyasparagine | |||
Disulfide bond | 158↔171 | ||||
Disulfide bond | 175↔200 | ||||
Disulfide bond | 229↔246 | ||||
Disulfide bond | 287↔332 | ||||
Disulfide bond | 314↔344 | ||||
Disulfide bond | 349↔392 | ||||
Disulfide bond | 377↔409 | ||||
Disulfide bond | 413↔535 | Interchain (between heavy and light chains) | |||
Disulfide bond | 588↔601 | ||||
Disulfide bond | 612↔647 | ||||
Post-translational modification
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 7-131 | CUB | |||
Domain | 132-172 | EGF-like | |||
Domain | 171-283 | CUB | |||
Domain | 285-346 | Sushi | |||
Domain | 347-411 | Sushi | |||
Domain | 424-671 | Peptidase S1 | |||
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length673
- Mass (Da)73,906
- Last updated2019-09-18 v1
- MD5 Checksum3DEEFF30D6CB2233C175C02A7CA04057
Keywords
- Technical term