IED ID | IndEnz0002015634 |
Enzyme Type ID | protease015634 |
Protein Name |
Membrane cofactor protein TLX Trophoblast leukocyte common antigen CD antigen CD46 |
Gene Name | CD46 MCP MIC10 |
Organism | Homo sapiens (Human) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MEPPGRRECPFPSWRFPGLLLAAMVLLLYSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPTYKPPVSNYPGYPKPEEGILDSLDVWVIAVIVIAIVVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL |
Enzyme Length | 392 |
Uniprot Accession Number | P15529 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme 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}.; 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:7708671, PubMed:9379894, PubMed:11260136, PubMed:11971006). |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Alternative sequence (11); Beta strand (27); Chain (1); Compositional bias (1); Disulfide bond (8); Domain (4); Glycosylation (21); Helix (2); Modified residue (7); Mutagenesis (3); Natural variant (13); Region (1); Sequence conflict (4); Signal peptide (1); Topological domain (2); Transmembrane (1) |
Keywords | 3D-structure;Alternative splicing;Complement pathway;Cytoplasmic vesicle;Direct protein sequencing;Disease variant;Disulfide bond;Fertilization;Glycoprotein;Hemolytic uremic syndrome;Host cell receptor for virus entry;Host-virus interaction;Immunity;Innate immunity;Membrane;Phosphoprotein;Receptor;Reference proteome;Repeat;Signal;Sushi;Transmembrane;Transmembrane helix |
Interact With | P01024; P78504; Q8TD06; Q86W74-2; O60883; Q12837; Q9UEU0 |
Induction | |
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. |
Modified Residue | MOD_RES P15529-2:384; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:10657632; MOD_RES P15529-3:369; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:10657632; MOD_RES P15529-4:354; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:10657632; MOD_RES P15529-5:370; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:10657632; MOD_RES P15529-6:355; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:10657632; MOD_RES P15529-7:340; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:10657632; MOD_RES P15529-16:321; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:10657632 |
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. |
Signal Peptide | SIGNAL 1..34; /evidence="ECO:0000269|PubMed:1479546, ECO:0000269|PubMed:2298462, ECO:0000269|PubMed:3260937, ECO:0000269|PubMed:8371352" |
Structure 3D | X-ray crystallography (6) |
Cross Reference PDB | 1CKL; 2O39; 3INB; 3L89; 3O8E; 5FO8; |
Mapped Pubmed ID | 12055245; 1386357; 17220899; 17446270; 19367725; 19396169; 20010840; 20071571; 20534589; 20694009; 20711500; 20941397; 23086448; 2481448; 27013439; 6214588; 7391570; |
Motif | |
Gene Encoded By | |
Mass | 43,747 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |