C1QC
entrez
714
canonical
uniprot
P02747
canonical
ensembl
ENSG00000159189
resolver
ensp
ENSP00000363768
resolver
ensp
ENSP00000363770
resolver
ensp
ENSP00000363771
resolver
ensp
ENSP00000512142
resolver
ensp
ENSP00000512144
resolver
ensp
ENSP00000512146
resolver
ensp
ENSP00000537723
resolver
ensp
ENSP00000537724
resolver
ensp
ENSP00000638907
resolver
enst
ENST00000374637
resolver
enst
ENST00000374639
resolver
enst
ENST00000374640
resolver
enst
ENST00000695749
resolver
enst
ENST00000695751
resolver
enst
ENST00000695753
resolver
enst
ENST00000867664
resolver
enst
ENST00000867665
resolver
enst
ENST00000968848
resolver
genesymbol
C1QC
resolver
genesymbol_syn
C1QG
resolver
hgnc
HGNC:1245
resolver
uniprot
A0A8Q3SIZ0
resolver
uniprot
Q7Z502
resolver
uniprot
Q96DL2
resolver
uniprot
Q96H05
resolver
uniprot_entry
A0A8Q3SIZ0_HUMAN
resolver
uniprot_entry
C1QC_HUMAN
resolver
uniprot_sec
Q7Z502
resolver
uniprot_sec
Q96DL2
resolver
uniprot_sec
Q96H05
resolver
activity_regulation
ACTIVITY REGULATION: The C1Q subcomplex is inhibited by sulfated molecules, such as triterpenoid sulfates, heparan sulfate, or chondroitin sulfates. {ECO:0000269|PubMed:20548024, ECO:0000269|PubMed:6218163}.
uniprot
proteins
amino_acid_sequence
MDVGPSSLPHLGLKLLLLLLLLPLRGQANTGCYGIPGMPGLPGAPGKDGYDGLPGPKGEPGIPAIPGIRGPKGQKGEPGLPGHPGKNGPMGPPGMPGVPGPMGIPGEPGEEGRYKQKFQSVFTVTRQTHQPPAPNSLIRFNAVLTNPQGDYDTSTGKFTCKVPGLYYFVYHASHTANLCVLLYRSGVKVVTFCGHTSKTNQVNSGGVLLRLQVGEEVWLAVNDYYDMVGIQGSDSVFSGFLLFPD
uniprot
proteins
disease_involvement
DISEASE: C1q deficiency 3 (C1QD3) [MIM:620322]: An autosomal recessive disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease characterized by recurrent skin lesions, chronic infections, an increased risk of systemic lupus erythematosus, and glomerulonephritis. {ECO:0000269|PubMed:8630118}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Core component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:12847249, PubMed:19006321, PubMed:24626930, PubMed:29449492, PubMed:3258649, PubMed:34155115, PubMed:6249812, PubMed:6776418). The classical complement pathway is initiated by the C1Q subcomplex of the C1 complex, which specifically binds IgG or IgM immunoglobulins complexed with antigens, forming antigen-antibody complexes on the surface of pathogens: C1QA, together with C1QB and C1QC, specifically recognizes and binds the Fc regions of IgG or IgM via its C1q domain (PubMed:12847249, PubMed:19006321, PubMed:24626930, PubMed:29449492, PubMed:3258649, PubMed:6776418). Immunoglobulin-binding activates the proenzyme C1R, which cleaves C1S, initiating the proteolytic cascade of the complement system (PubMed:29449492). The C1Q subcomplex is activated by a hexamer of IgG complexed with antigens, while it is activated by a pentameric IgM (PubMed:19706439, PubMed:24626930, PubMed:29449492). The C1Q subcomplex also recognizes and binds phosphatidylserine exposed on the surface of cells undergoing programmed cell death, possibly promoting activation of the complement system (PubMed:18250442). {ECO:0000269|PubMed:12847249, ECO:0000269|PubMed:18250442, ECO:0000269|PubMed:19006321, ECO:0000269|PubMed:19706439, ECO:0000269|PubMed:24626930, ECO:0000269|PubMed:29449492, ECO:0000269|PubMed:3258649, ECO:0000269|PubMed:34155115, ECO:0000269|PubMed:6249812, ECO:0000269|PubMed:6776418}.
uniprot
proteins
mass_dalton
25774
uniprot
proteins
mutagenesis
MUTAGEN 86; /note="K->A: In LysC58; impaired ability to associate with C1R and C1S."; /evidence="ECO:0000269|PubMed:23650384"; MUTAGEN 129; /note="H->A: Has no effect on binding to IgM."; /evidence="ECO:0000269|PubMed:19006321"; MUTAGEN 198; /note="K->E: Decreases binding to IgM."; /evidence="ECO:0000269|PubMed:19006321
uniprot
proteins
post_translational_modification
PTM: O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. {ECO:0000269|PubMed:486087}.
uniprot
proteins
pubmed
12847249
uniprot
proteins
pubmed
12960167
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
1706597
uniprot
proteins
pubmed
18250442
uniprot
proteins
pubmed
19006321
uniprot
proteins
pubmed
19706439
uniprot
proteins
pubmed
20548024
uniprot
proteins
pubmed
23650384
uniprot
proteins
pubmed
24626930
uniprot
proteins
pubmed
29449492
uniprot
proteins
pubmed
2988513
uniprot
proteins
pubmed
3258649
uniprot
proteins
pubmed
34155115
uniprot
proteins
pubmed
486087
uniprot
proteins
pubmed
6218163
uniprot
proteins
pubmed
6249812
uniprot
proteins
pubmed
6776418
uniprot
proteins
pubmed
6952210
uniprot
proteins
pubmed
708376
uniprot
proteins
pubmed
8630118
uniprot
proteins
pubmed
9777412
uniprot
proteins
sequence_length
245
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18250442, ECO:0000269|PubMed:29449492, ECO:0000269|PubMed:486087}. Cell surface {ECO:0000269|PubMed:34155115}. Note=Specifically binds IgG or IgM immunoglobulins complexed with antigens, forming antigen-antibody complexes on the surface of pathogens. {ECO:0000269|PubMed:34155115}.
uniprot
proteins