A0A2I6BQJ9 · A0A2I6BQJ9_SEBSC

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.

Caution

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

Catalytic activity

  • Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form the active form of C1s (EC 3.4.21.42).
    EC:3.4.21.41 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site, active site.

170450100150200250300350400450500550600650700
TypeIDPosition(s)Description
Binding site69Ca2+ 1 (UniProtKB | ChEBI)
Binding site77Ca2+ 1 (UniProtKB | ChEBI)
Binding site122Ca2+ 1 (UniProtKB | ChEBI)
Binding site142Ca2+ 2 (UniProtKB | ChEBI)
Binding site145Ca2+ 2 (UniProtKB | ChEBI)
Binding site165Ca2+ 2 (UniProtKB | ChEBI)
Binding site291Ca2+ 3 (UniProtKB | ChEBI)
Active site496Charge relay system
Active site549Charge relay system
Active site654Charge relay system

GO annotations

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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    complement subcomponent C1r
  • EC number

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Perciformes > Scorpaenoidei > Sebastidae > Sebastinae > Sebastes

Accessions

  • Primary accession
    A0A2I6BQJ9

Subcellular Location

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-18
ChainPRO_501439467019-704complement subcomponent C1r
Disulfide bond74↔92
Disulfide bond146↔163
Disulfide bond159↔172
Modified residue165(3R)-3-hydroxyasparagine
Disulfide bond174↔187
Disulfide bond191↔218
Disulfide bond251↔269
Disulfide bond310↔358
Disulfide bond338↔371
Disulfide bond376↔422
Disulfide bond405↔440
Disulfide bond444↔569Interchain (between heavy and light chains)
Disulfide bond616↔639
Disulfide bond650↔678

Post-translational modification

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

Keywords

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.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain18-141CUB
Domain191-306CUB
Domain308-373Sushi
Domain374-442Sushi
Domain457-702Peptidase S1

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    704
  • Mass (Da)
    77,957
  • Last updated
    2018-03-28 v1
  • Checksum
    C908CCC2CB0AE26C
MGWTSFIILFLCVSVSECWRLPDPEPLMHGAVQSPQYPEPYSPNLQEQWDLSVPEGYQIRLTFTHLDIEASAGCYYDVLTVLYDAKILGKFCGHENSADGHHPGNEPILSPGNRLTLTFQTDGNNPERHQNVGFSAQYQAIDMDECSAPEPEDGSGPLCSQICLNTLGSYLCSCHHGYELRPDQRSCVLSCGGGIFDEPEGHLFSPGYPNPPPHAVSCQYIISVESGFTVTLNFTDNFHIDSADTEQGPICLHHWLQVTIPDNEPMKLCGGKSPGLIVTNSNTVRLDYHIDDEGLSNGWSLDYSTYRVKCPFPGNVAKGRVTPILTEYLYRDYISARCDQGYKLMMDGQEVEGFSTMCQSNGQWHLPLPECHIIDCGEPEPLLNGGVTFMSGFQNQYRSVVQYHCNEPFYSLLGGINVVFTCESDRKWRSNNDIIFRPTCIPVCGKPTQLISTYQRIIGGSDAPDDTIPWQVMLSIDGGRGGGMVIGDRWIMTAAHNVMHDGNVVPNETVRIYMGLTNVNTLMNSPVYAASIHTHPLYNNPNLVDFNHDIALIKIQDPITFNSSVMPICLPAEGATYVTGTMGLVSGFGVTETDKRRILTNKMKYVQVPVVEQQACSDSITLLKKKKVLVPILTNNMFCAGVPEGGKDSCQGDSGGPYALRDDGRFWAAGIVSWGFDCGQRGTYGVYTRVINYIDWINKTMQEN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MF787223
EMBL· GenBank· DDBJ
AUI80561.1
EMBL· GenBank· DDBJ
mRNA

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