CD46
entrez
4179
canonical
uniprot
P15529
canonical
ensembl
ENSG00000117335
resolver
ensp
ENSP00000313875
resolver
ensp
ENSP00000314664
resolver
ensp
ENSP00000346912
resolver
ensp
ENSP00000350346
resolver
ensp
ENSP00000350893
resolver
ensp
ENSP00000353342
resolver
ensp
ENSP00000356008
resolver
ensp
ENSP00000356009
resolver
ensp
ENSP00000418471
resolver
ensp
ENSP00000512167
resolver
ensp
ENSP00000557112
resolver
ensp
ENSP00000557114
resolver
ensp
ENSP00000640431
resolver
ensp
ENSP00000640436
resolver
ensp
ENSP00000684078
resolver
ensp
ENSP00000798824
resolver
enst
ENST00000695777
resolver
genesymbol
CD46
resolver
genesymbol_syn
MCP
resolver
genesymbol_syn
MIC10
resolver
hgnc
HGNC:6953
resolver
uniprot
A0A8Q3WLA6
resolver
uniprot
A0T1T0
resolver
uniprot
A0T1T1
resolver
uniprot
A0T1T2
resolver
uniprot
Q15429
resolver
uniprot
Q53GV9
resolver
uniprot
Q5HY94
resolver
uniprot
Q5VWS6
resolver
uniprot
Q5VWS7
resolver
uniprot
Q5VWS8
resolver
uniprot
Q5VWS9
resolver
uniprot
Q5VWT0
resolver
uniprot
Q5VWT1
resolver
uniprot
Q5VWT2
resolver
uniprot
Q6N0A1
resolver
uniprot
Q7Z3R5
resolver
uniprot
Q9NNW2
resolver
uniprot
Q9NNW3
resolver
uniprot
Q9NNW4
resolver
uniprot
Q9UCJ4
resolver
uniprot_entry
A0A8Q3WLA6_HUMAN
resolver
uniprot_entry
MCP_HUMAN
resolver
uniprot_sec
A0T1T0
resolver
uniprot_sec
A0T1T1
resolver
uniprot_sec
A0T1T2
resolver
uniprot_sec
Q15429
resolver
uniprot_sec
Q53GV9
resolver
uniprot_sec
Q5HY94
resolver
uniprot_sec
Q5VWS6
resolver
uniprot_sec
Q5VWS7
resolver
uniprot_sec
Q5VWS8
resolver
uniprot_sec
Q5VWS9
resolver
uniprot_sec
Q5VWT0
resolver
uniprot_sec
Q5VWT1
resolver
uniprot_sec
Q5VWT2
resolver
uniprot_sec
Q6N0A1
resolver
uniprot_sec
Q7Z3R5
resolver
uniprot_sec
Q9NNW2
resolver
uniprot_sec
Q9NNW3
resolver
uniprot_sec
Q9NNW4
resolver
uniprot_sec
Q9UCJ4
resolver
amino_acid_sequence
MEPPGRRECPFPSWRFPGLLLAAMVLLLYSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPTYKPPVSNYPGYPKPEEGILDSLDVWVIAVIVIAIVVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL
uniprot
proteins
disease_involvement
DISEASE: Hemolytic uremic syndrome, atypical, 2 (AHUS2) [MIM:612922]: An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. {ECO:0000269|PubMed:14566051, ECO:0000269|PubMed:16386793, ECO:0000269|PubMed:16621965, ECO:0000269|PubMed:20513133}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Other genes may play a role in modifying the phenotype. Patients with CD46 mutations seem to have an overall better prognosis compared to patients carrying CFH mutations.
uniprot
proteins
function
FUNCTION: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity. {ECO:0000269|PubMed:10843656, ECO:0000269|PubMed:12540904}.; FUNCTION: (Microbial infection) A number of viral and bacterial pathogens seem to bind MCP in order to exploit its immune regulation property and directly induce an immunosuppressive phenotype in T-cells.; FUNCTION: (Microbial infection) Acts as a receptor for Adenovirus subgroup B2 and Ad3. {ECO:0000269|PubMed:12915534, ECO:0000269|PubMed:14566335, ECO:0000269|PubMed:15047806, ECO:0000269|PubMed:15078926, ECO:0000269|PubMed:15919905, ECO:0000269|PubMed:16254377}.; FUNCTION: (Microbial infection) Acts as a receptor for cultured Measles virus. {ECO:0000269|PubMed:10972291, ECO:0000269|PubMed:20010840, ECO:0000269|PubMed:7534417, ECO:0000269|PubMed:8371352, ECO:0000269|PubMed:8402913}.; FUNCTION: (Microbial infection) Acts as a receptor for Herpesvirus 6/HHV-6. {ECO:0000269|PubMed:12663806, ECO:0000269|PubMed:12724329}.; FUNCTION: (Microbial infection) May act as a receptor for pathogenic bacteria Neisseria and Streptococcus pyogenes (PubMed:11260136, PubMed:11971006, PubMed:7708671, PubMed:9379894).; FUNCTION: (Microbial infection) Plays a minor role in fiber protein-mediated human adenovirus 55 infection; via its interaction with fiber protein (PubMed:32581096). Plays a minor role in fiber protein-mediated human adenovirus 14a infection (PubMed:32581096). {ECO:0000269|PubMed:32581096}.
uniprot
proteins
mass_dalton
43747
uniprot
proteins
mutagenesis
MUTAGEN 83; /note="N->Q: No effect on cytoprotective function. No effect on Neisseria binding. No effect on Measles virus binding."; /evidence="ECO:0000269|PubMed:11260136, ECO:0000269|PubMed:8764003, ECO:0000269|PubMed:9759896"; MUTAGEN 114; /note="N->Q: Strongly decreases cytoprotective function. Decreases Neisseria binding. Abolishes Measles virus binding."; /evidence="ECO:0000269|PubMed:11260136, ECO:0000269|PubMed:8764003, ECO:0000269|PubMed:9759896"; MUTAGEN 273; /note="N->Q: Strongly decreases cytoprotective function. Abolishes Neisseria binding. No effect on Measles virus binding."; /evidence="ECO:0000269|PubMed:11260136, ECO:0000269|PubMed:8764003, ECO:0000269|PubMed:9759896
uniprot
proteins
post_translational_modification
PTM: N-glycosylated on Asn-83; Asn-114 and Asn-273 in most tissues, but probably less N-glycosylated in testis. N-glycosylation on Asn-114 and Asn-273 is required for cytoprotective function. N-glycosylation on Asn-114 is required for Measles virus binding. N-glycosylation on Asn-273 is required for Neisseria binding. N-glycosylation is not required for human adenovirus binding.; PTM: Extensively O-glycosylated in the Ser/Thr-rich domain. O-glycosylation is required for Neisseria binding but not for Measles virus or human adenovirus binding.; PTM: In epithelial cells, isoforms B/D/F/H/J/L/3 are phosphorylated by YES1 in response to infection by Neisseria gonorrhoeae; which promotes infectivity. In T-cells, these isoforms may be phosphorylated by LCK.
uniprot
proteins
pubmed
10357804
uniprot
proteins
pubmed
10619434
uniprot
proteins
pubmed
10657632
uniprot
proteins
pubmed
10751138
uniprot
proteins
pubmed
10843656
uniprot
proteins
pubmed
10972291
uniprot
proteins
pubmed
11260136
uniprot
proteins
pubmed
11901164
uniprot
proteins
pubmed
11971006
uniprot
proteins
pubmed
12112588
uniprot
proteins
pubmed
12171934
uniprot
proteins
pubmed
12540904
uniprot
proteins
pubmed
12663806
uniprot
proteins
pubmed
12724329
uniprot
proteins
pubmed
12915534
uniprot
proteins
pubmed
14566051
uniprot
proteins
pubmed
14566335
uniprot
proteins
pubmed
14597734
uniprot
proteins
pubmed
14615110
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1479546
uniprot
proteins
pubmed
15047806
uniprot
proteins
pubmed
15078926
uniprot
proteins
pubmed
15307194
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15919905
uniprot
proteins
pubmed
1601037
uniprot
proteins
pubmed
16254377
uniprot
proteins
pubmed
16386793
uniprot
proteins
pubmed
16621965
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
1711570
uniprot
proteins
pubmed
1717583
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
20010840
uniprot
proteins
pubmed
2050389
uniprot
proteins
pubmed
20513133
uniprot
proteins
pubmed
2298462
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
32581096
uniprot
proteins
pubmed
3260937
uniprot
proteins
pubmed
7534417
uniprot
proteins
pubmed
7691939
uniprot
proteins
pubmed
7708671
uniprot
proteins
pubmed
7884872
uniprot
proteins
pubmed
8371352
uniprot
proteins
pubmed
8402913
uniprot
proteins
pubmed
8418811
uniprot
proteins
pubmed
8764003
uniprot
proteins
pubmed
9379894
uniprot
proteins
pubmed
9659228
uniprot
proteins
pubmed
9759896
uniprot
proteins
sequence_length
392
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000269|PubMed:12112588, ECO:0000269|PubMed:14597734, ECO:0000269|PubMed:15307194}; Single-pass type I membrane protein {ECO:0000269|PubMed:12112588, ECO:0000269|PubMed:14597734, ECO:0000269|PubMed:15307194}. Note=Inner acrosomal membrane of spermatozoa. Internalized upon binding of Measles virus, Herpesvirus 6 or Neisseria gonorrhoeae, which results in an increased susceptibility of infected cells to complement-mediated injury. In cancer cells or cells infected by Neisseria, shedding leads to a soluble peptide.
uniprot
proteins
transmembrane_region
TRANSMEM 344..366; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins