C1R
entrez
715
canonical
uniprot
P00736
canonical
ensembl
ENSG00000159403
resolver
ensembl
ENSG00000288512
resolver
ensp
ENSP00000444271
resolver
ensp
ENSP00000497341
resolver
ensp
ENSP00000499988
resolver
ensp
ENSP00000500036
resolver
enst
ENST00000536053
resolver
enst
ENST00000647956
resolver
enst
ENST00000671968
resolver
enst
ENST00000673372
resolver
genesymbol
C1R
resolver
hgnc
HGNC:1246
resolver
uniprot
A0A3B3ISR2
resolver
uniprot
A0ACM8QGB8
resolver
uniprot
A6NJQ8
resolver
uniprot
B4DPQ0
resolver
uniprot
F5GZR1
resolver
uniprot
Q68D77
resolver
uniprot
Q8J012
resolver
uniprot_entry
A0A3B3ISR2_HUMAN
resolver
uniprot_entry
A0ACM8QGB8_HUMAN
resolver
uniprot_entry
B4DPQ0_HUMAN
resolver
uniprot_entry
C1R_HUMAN
resolver
uniprot_sec
A6NJQ8
resolver
uniprot_sec
F5GZR1
resolver
uniprot_sec
Q68D77
resolver
uniprot_sec
Q8J012
resolver
activity_regulation
ACTIVITY REGULATION: Activated by the C1Q subcomplex of the C1 complex following C1Q binding to immunoglobulins (IgG or IgM) complexed with antigens to form antigen-antibody complexes on the surface of pathogens (PubMed:17996945, PubMed:20178990, PubMed:6254570). Immunoglobulin-binding promotes autoactivation of C1R, which results in the cleavage of the Arg-Ile bond in the catalytic domain (PubMed:17996945, PubMed:20178990). {ECO:0000269|PubMed:17996945, ECO:0000269|PubMed:20178990, ECO:0000269|PubMed:6254570}.
uniprot
proteins
amino_acid_sequence
MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVFQQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDTHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQDDGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVFTNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAVRDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED
uniprot
proteins
disease_involvement
DISEASE: Ehlers-Danlos syndrome, periodontal type, 1 (EDSPD1) [MIM:130080]: A form of Ehlers-Danlos syndrome, a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDSPD1 is characterized by the association of typical features of Ehlers-Danlos syndrome with gingival recession and severe early-onset periodontal disease, leading to premature loss of permanent teeth. EDSPD1 inheritance is autosomal dominant. {ECO:0000269|PubMed:27745832}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.41
uniprot
proteins
function
FUNCTION: Serine protease 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:17996945, PubMed:19473974, PubMed:29449492). C1R catalyzes the first enzymatic step in the classical complement pathway: it is activated by the C1Q subcomplex of the C1 complex, which associates with IgG or IgM immunoglobulins complexed with antigens to form antigen-antibody complexes on the surface of pathogens (PubMed:29449492, PubMed:34155115). Immunoglobulin-binding promotes the autocatalytic cleavage and activation of C1R (PubMed:11445589, PubMed:11673533, PubMed:17996945, PubMed:20178990, PubMed:6254570, PubMed:6271784). Activated C1R then cleaves and activates C1S, the second protease of the classical complement pathway (PubMed:11445589, PubMed:11673533, PubMed:6271784). It is unclear if C1R activates C1S within single, strained C1 complexes or between neighboring C1 complexes on surfaces (PubMed:28104818, PubMed:29311313, PubMed:29449492). {ECO:0000269|PubMed:11445589, ECO:0000269|PubMed:11673533, ECO:0000269|PubMed:17996945, ECO:0000269|PubMed:19473974, ECO:0000269|PubMed:20178990, ECO:0000269|PubMed:28104818, ECO:0000269|PubMed:29311313, ECO:0000269|PubMed:29449492, ECO:0000269|PubMed:34155115, ECO:0000269|PubMed:6254570, ECO:0000269|PubMed:6271784}.
uniprot
proteins
mass_dalton
80119
uniprot
proteins
mutagenesis
MUTAGEN 66; /note="E->A: Abolished association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 73; /note="Y->A: Abolished association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 81; /note="D->N: Does not affect association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 144; /note="D->N: Does not affect association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 154; /note="E->A: Does not affect association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 155; /note="E->A: Does not affect association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 156; /note="D->A: Does not affect association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 290; /note="D->A: Decreased association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 463; /note="R->Q: Abolished autoprocessing, but promotes extrinsic cleavage by thermolysin."; /evidence="ECO:0000269|PubMed:11445589, ECO:0000269|PubMed:11673533"; MUTAGEN 654; /note="S->A: Abolished protease activity."; /evidence="ECO:0000269|PubMed:11445589, ECO:0000269|PubMed:11673533, ECO:0000269|PubMed:19473974
uniprot
proteins
post_translational_modification
PTM: Cleaved and activated by autocatalytic processing to generate Complement C1r subcomponent heavy and light chains that are connected by disulfide bonds. {ECO:0000269|PubMed:11445589, ECO:0000269|PubMed:11673533, ECO:0000269|PubMed:17996945, ECO:0000269|PubMed:20178990, ECO:0000269|PubMed:6254570, ECO:0000269|PubMed:869924}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:2820791}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
11445589
uniprot
proteins
pubmed
11673533
uniprot
proteins
pubmed
11823416
uniprot
proteins
pubmed
12429092
uniprot
proteins
pubmed
12914573
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
17996945
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19473974
uniprot
proteins
pubmed
20178990
uniprot
proteins
pubmed
22028381
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27745832
uniprot
proteins
pubmed
28104818
uniprot
proteins
pubmed
2820791
uniprot
proteins
pubmed
2831944
uniprot
proteins
pubmed
29311313
uniprot
proteins
pubmed
29449492
uniprot
proteins
pubmed
2988513
uniprot
proteins
pubmed
2989825
uniprot
proteins
pubmed
3021205
uniprot
proteins
pubmed
3030286
uniprot
proteins
pubmed
3036070
uniprot
proteins
pubmed
34155115
uniprot
proteins
pubmed
6254570
uniprot
proteins
pubmed
6271784
uniprot
proteins
pubmed
6303394
uniprot
proteins
pubmed
6952210
uniprot
proteins
pubmed
8162045
uniprot
proteins
pubmed
8635594
uniprot
proteins
pubmed
869924
uniprot
proteins
pubmed
9477945
uniprot
proteins
sequence_length
705
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27745832}. Cell surface {ECO:0000269|PubMed:34155115}. Note=Recruited to the surface of pathogens by the C1Q subcomplex. {ECO:0000269|PubMed:34155115}.
uniprot
proteins