Search
complement C2; contains: complement C2b fragment; complement C2a fragment (C2)
Function:
- part of the complement classical pathway
- cleaved by activated factor C1 into 2 fragments: C2b & C2a
Structure:
- belongs to the peptidase S1 family
- contains 1 peptidase S1 domain
- contains 3 Sushi (CCP/SCR) domains
- contains 1 VWFA domain
Compartment: secreted
Alternative splicing: named isoforms=2
Polymorphism:
- the C2 variant Asp-318 is associated with a reduced risk of age-related macular degeneration
Pathology:
- defects in complement C2 are the cause of complement C2 deficiency
Notes:
- complement C2 is an MHC class 3 protein
Interactions
molecular events
Related
complement cascade
Specific
complement C2a; C3/C5 convertase
complement C2b
General
complement
human longevity protein
Properties
SIZE: entity length = 752 aa
MW = 83 kD
COMPARTMENT: plasma
MOTIF: signal sequence {1-20}
Sushi domain {22-86}
MOTIF: cysteine residue {C24}
MODIFICATION: cysteine residue {C64}
N-glycosylation site {N29}
cysteine residue {C51}
MODIFICATION: cysteine residue {C84}
cysteine residue {C64}
MODIFICATION: cysteine residue {C24}
cysteine residue {C84}
MODIFICATION: cysteine residue {C51}
Sushi domain {87-146}
MOTIF: cysteine residue {C89}
MODIFICATION: cysteine residue {C131}
N-glycosylation site {N112}
cysteine residue {C117}
MODIFICATION: cysteine residue {C144}
cysteine residue {C131}
MODIFICATION: cysteine residue {C89}
cysteine residue {C144}
MODIFICATION: cysteine residue {C117}
Sushi domain {149-206}
MOTIF: cysteine residue {C151}
MODIFICATION: cysteine residue {C191}
cysteine residue {C177}
MODIFICATION: cysteine residue {C204}
cysteine residue {C191}
MODIFICATION: cysteine residue {C151}
cysteine residue {C204}
MODIFICATION: cysteine residue {C177}
VWFA domain {254-452}
MOTIF: N-glycosylation site {N290}
N-glycosylation site {N333}
S1 domain {464-744}
MOTIF: N-glycosylation site {N467}
N-glycosylation site {N471}
cysteine residue {C492}
MODIFICATION: cysteine residue {C508}
histidine residue {H507}
cysteine residue {C508}
MODIFICATION: cysteine residue {C492}
aspartate residue {D561}
N-glycosylation site {N621}
N-glycosylation site {N651}
cysteine residue {C675}
MODIFICATION: cysteine residue {C705}
serine residue {S679}
cysteine residue {C705}
MODIFICATION: cysteine residue {C675}
Database Correlations
OMIM correlations
MORBIDMAP 613927
UniProt P06681
PFAM correlations
Entrez Gene 717
KEGG correlations
ENZYME 3.4.21.43
References
- UniProt :accession P06681
- C2base; Note: C2 mutation db
http://bioinf.uta.fi/C2base/
- SeattleSNPs
http://pga.gs.washington.edu/data/c2/
- Baron M, Norman DG, Campbell ID.
Protein modules.
Trends Biochem Sci. 1991 Jan;16(1):13-7. Review.
PMID: 2053133