A0A2I6BQJ9 · A0A2I6BQJ9_SEBSC
- Proteincomplement subcomponent C1r
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids704 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.
Catalytic activity
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 69 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 77 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 122 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 142 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 145 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 165 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 291 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 496 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 549 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 654 | 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, classical pathway | |
Biological Process | innate immune response | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namecomplement subcomponent C1r
- EC number
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Perciformes > Scorpaenoidei > Sebastidae > Sebastinae > Sebastes
Accessions
- Primary accessionA0A2I6BQJ9
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MGWTSFIILFLCVSVSEC | ||||||
Chain | PRO_5014394670 | 19-704 | complement subcomponent C1r | |||
Sequence: WRLPDPEPLMHGAVQSPQYPEPYSPNLQEQWDLSVPEGYQIRLTFTHLDIEASAGCYYDVLTVLYDAKILGKFCGHENSADGHHPGNEPILSPGNRLTLTFQTDGNNPERHQNVGFSAQYQAIDMDECSAPEPEDGSGPLCSQICLNTLGSYLCSCHHGYELRPDQRSCVLSCGGGIFDEPEGHLFSPGYPNPPPHAVSCQYIISVESGFTVTLNFTDNFHIDSADTEQGPICLHHWLQVTIPDNEPMKLCGGKSPGLIVTNSNTVRLDYHIDDEGLSNGWSLDYSTYRVKCPFPGNVAKGRVTPILTEYLYRDYISARCDQGYKLMMDGQEVEGFSTMCQSNGQWHLPLPECHIIDCGEPEPLLNGGVTFMSGFQNQYRSVVQYHCNEPFYSLLGGINVVFTCESDRKWRSNNDIIFRPTCIPVCGKPTQLISTYQRIIGGSDAPDDTIPWQVMLSIDGGRGGGMVIGDRWIMTAAHNVMHDGNVVPNETVRIYMGLTNVNTLMNSPVYAASIHTHPLYNNPNLVDFNHDIALIKIQDPITFNSSVMPICLPAEGATYVTGTMGLVSGFGVTETDKRRILTNKMKYVQVPVVEQQACSDSITLLKKKKVLVPILTNNMFCAGVPEGGKDSCQGDSGGPYALRDDGRFWAAGIVSWGFDCGQRGTYGVYTRVINYIDWINKTMQEN | ||||||
Disulfide bond | 74↔92 | |||||
Sequence: CYYDVLTVLYDAKILGKFC | ||||||
Disulfide bond | 146↔163 | |||||
Sequence: CSAPEPEDGSGPLCSQIC | ||||||
Disulfide bond | 159↔172 | |||||
Sequence: CSQICLNTLGSYLC | ||||||
Modified residue | 165 | (3R)-3-hydroxyasparagine | ||||
Sequence: N | ||||||
Disulfide bond | 174↔187 | |||||
Sequence: CHHGYELRPDQRSC | ||||||
Disulfide bond | 191↔218 | |||||
Sequence: CGGGIFDEPEGHLFSPGYPNPPPHAVSC | ||||||
Disulfide bond | 251↔269 | |||||
Sequence: CLHHWLQVTIPDNEPMKLC | ||||||
Disulfide bond | 310↔358 | |||||
Sequence: CPFPGNVAKGRVTPILTEYLYRDYISARCDQGYKLMMDGQEVEGFSTMC | ||||||
Disulfide bond | 338↔371 | |||||
Sequence: CDQGYKLMMDGQEVEGFSTMCQSNGQWHLPLPEC | ||||||
Disulfide bond | 376↔422 | |||||
Sequence: CGEPEPLLNGGVTFMSGFQNQYRSVVQYHCNEPFYSLLGGINVVFTC | ||||||
Disulfide bond | 405↔440 | |||||
Sequence: CNEPFYSLLGGINVVFTCESDRKWRSNNDIIFRPTC | ||||||
Disulfide bond | 444↔569 | Interchain (between heavy and light chains) | ||||
Sequence: CGKPTQLISTYQRIIGGSDAPDDTIPWQVMLSIDGGRGGGMVIGDRWIMTAAHNVMHDGNVVPNETVRIYMGLTNVNTLMNSPVYAASIHTHPLYNNPNLVDFNHDIALIKIQDPITFNSSVMPIC | ||||||
Disulfide bond | 616↔639 | |||||
Sequence: CSDSITLLKKKKVLVPILTNNMFC | ||||||
Disulfide bond | 650↔678 | |||||
Sequence: CQGDSGGPYALRDDGRFWAAGIVSWGFDC |
Post-translational modification
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Keywords
- PTM
Interaction
Subunit
C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. C1r is a dimer of identical chains, each of which is activated by cleavage into two chains, A and B, connected by disulfide bonds.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-141 | CUB | ||||
Sequence: CWRLPDPEPLMHGAVQSPQYPEPYSPNLQEQWDLSVPEGYQIRLTFTHLDIEASAGCYYDVLTVLYDAKILGKFCGHENSADGHHPGNEPILSPGNRLTLTFQTDGNNPERHQNVGFSAQYQAI | ||||||
Domain | 191-306 | CUB | ||||
Sequence: CGGGIFDEPEGHLFSPGYPNPPPHAVSCQYIISVESGFTVTLNFTDNFHIDSADTEQGPICLHHWLQVTIPDNEPMKLCGGKSPGLIVTNSNTVRLDYHIDDEGLSNGWSLDYSTY | ||||||
Domain | 308-373 | Sushi | ||||
Sequence: VKCPFPGNVAKGRVTPILTEYLYRDYISARCDQGYKLMMDGQEVEGFSTMCQSNGQWHLPLPECHI | ||||||
Domain | 374-442 | Sushi | ||||
Sequence: IDCGEPEPLLNGGVTFMSGFQNQYRSVVQYHCNEPFYSLLGGINVVFTCESDRKWRSNNDIIFRPTCIP | ||||||
Domain | 457-702 | Peptidase S1 | ||||
Sequence: IIGGSDAPDDTIPWQVMLSIDGGRGGGMVIGDRWIMTAAHNVMHDGNVVPNETVRIYMGLTNVNTLMNSPVYAASIHTHPLYNNPNLVDFNHDIALIKIQDPITFNSSVMPICLPAEGATYVTGTMGLVSGFGVTETDKRRILTNKMKYVQVPVVEQQACSDSITLLKKKKVLVPILTNNMFCAGVPEGGKDSCQGDSGGPYALRDDGRFWAAGIVSWGFDCGQRGTYGVYTRVINYIDWINKTMQ |
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length704
- Mass (Da)77,957
- Last updated2018-03-28 v1
- ChecksumC908CCC2CB0AE26C