GENTAUR Molecular Products.

 MCP_HUMAN               Reviewed;         392 AA.
 P15529; A0T1T0; A0T1T1; A0T1T2; Q15429; Q53GV9; Q5HY94; Q5VWS6;
 Q5VWS7; Q5VWS8; Q5VWS9; Q5VWT0; Q5VWT1; Q5VWT2; Q6N0A1; Q7Z3R5;
 Q9NNW2; Q9NNW3; Q9NNW4; Q9UCJ4;
 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
 16-JAN-2004, sequence version 3.
 28-MAR-2018, entry version 206.
 RecName: Full=Membrane cofactor protein;
 AltName: Full=TLX;
 AltName: Full=Trophoblast leukocyte common antigen;
 AltName: CD_antigen=CD46;
 Flags: Precursor;
 Name=CD46; Synonyms=MCP, MIC10;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), PROTEIN SEQUENCE OF 35-58, AND
 INTERACTION WITH C3B.
 PubMed=3260937; DOI=10.1084/jem.168.1.181;
 Lublin D.M., Liszewski M.K., Post T.W., Arce M.A., le Beau M.M.,
 Rebentisch M.B., Lemons R.S., Seya T., Atkinson J.P.;
 "Molecular cloning and chromosomal localization of human membrane
 cofactor protein (MCP). Evidence for inclusion in the multigene family
 of complement-regulatory proteins.";
 J. Exp. Med. 168:181-194(1988).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), AND ALTERNATIVE SPLICING.
 PubMed=2050389; DOI=10.1007/BF00216692;
 Purcell D.F., Russell S.M., Deacon N.J., Brown M.A., Hooker D.J.,
 McKenzie I.F.;
 "Alternatively spliced RNAs encode several isoforms of CD46 (MCP), a
 regulator of complement activation.";
 Immunogenetics 33:335-344(1991).
 [3]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D; E AND F).
 PubMed=1711570; DOI=10.1084/jem.174.1.93;
 Post T.W., Liszewski M.K., Adams E.M., Tedja I., Miller E.A.,
 Atkinson J.P.;
 "Membrane cofactor protein of the complement system: alternative
 splicing of serine/threonine/proline-rich exons and cytoplasmic tails
 produces multiple isoforms that correlate with protein phenotype.";
 J. Exp. Med. 174:93-102(1991).
 [4]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F).
 TISSUE=Testis;
 PubMed=8418811; DOI=10.1002/mrd.1080340117;
 Cervoni F., Fenichel P., Akhoundi C., Hsi B.L., Rossi B.;
 "Characterization of a cDNA clone coding for human testis membrane
 cofactor protein (MCP, CD46).";
 Mol. Reprod. Dev. 34:107-113(1993).
 [5]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N).
 TISSUE=Testis;
 PubMed=9659228; DOI=10.1046/j.1365-2567.1998.00455.x;
 Hara T., Suzuki Y., Nakazawa T., Nishimura H., Nagasawa S.,
 Nishiguchi M., Matsumoto M., Hatanaka M., Kitamura M., Seya T.;
 "Post-translational modification and intracellular localization of a
 splice product of CD46 cloned from human testis: role of the
 intracellular domains in O-glycosylation.";
 Immunology 93:546-555(1998).
 [6]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS D; F AND L).
 Xue Z.T., Widegren B., Salford L.;
 "Molecular cloning of human CD46 (membrane cofactor protein) CDS from
 cancer cell lines in a retroviral vector system.";
 Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
 [7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
 TISSUE=Teratocarcinoma;
 PubMed=14702039; DOI=10.1038/ng1285;
 Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
 Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
 Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
 Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
 Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
 Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
 Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
 Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
 Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
 Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
 Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
 Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
 Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
 Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
 Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
 Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
 Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
 Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
 Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
 Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
 Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
 Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
 Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
 Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
 Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
 Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
 Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
 Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
 "Complete sequencing and characterization of 21,243 full-length human
 cDNAs.";
 Nat. Genet. 36:40-45(2004).
 [8]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS D AND E).
 TISSUE=Fetal kidney, Liver, and Salivary gland;
 PubMed=17974005; DOI=10.1186/1471-2164-8-399;
 Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
 Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
 Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
 Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
 "The full-ORF clone resource of the German cDNA consortium.";
 BMC Genomics 8:399-399(2007).
 [9]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND VARIANT
 PHE-13.
 TISSUE=Liver;
 Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
 Tanaka A., Yokoyama S.;
 Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
 [10]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-266; LEU-324;
 VAL-353 AND GLY-355.
 SeattleSNPs variation discovery resource;
 Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
 [11]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=16710414; DOI=10.1038/nature04727;
 Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
 Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
 Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
 McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
 Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
 Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
 Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
 Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
 Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
 Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
 Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
 Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
 Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
 Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
 Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
 Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
 Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
 Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
 Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
 Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
 Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
 Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
 Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
 Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
 Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
 Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
 Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
 Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
 Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
 Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
 Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
 Beck S., Rogers J., Bentley D.R.;
 "The DNA sequence and biological annotation of human chromosome 1.";
 Nature 441:315-321(2006).
 [12]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
 Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
 Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
 Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
 Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
 Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
 Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
 Venter J.C.;
 Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
 [13]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
 TISSUE=Testis;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [14]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1-158, AND VARIANTS PHE-13 AND GLN-59.
 PubMed=10751138; DOI=10.1086/315386;
 Kusuhara K., Sasaki Y., Nakao F., Ihara K., Hattori H., Yamashita S.,
 Nihei K., Koide N., Aiba H., Takeshita K., Hara T.;
 "Analysis of measles virus binding sites of the CD46 gene in patients
 with subacute sclerosing panencephalitis.";
 J. Infect. Dis. 181:1447-1449(2000).
 [15]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
 PubMed=7691939;
 Cui W., Hourcade D., Post T.W., Greenlund A.C., Atkinson J.P.,
 Kumar V.;
 "Characterization of the promoter region of the membrane cofactor
 protein (CD46) gene of the human complement system and comparison to a
 membrane cofactor protein-like genetic element.";
 J. Immunol. 151:4137-4146(1993).
 [16]
 PROTEIN SEQUENCE OF 35-60.
 TISSUE=Sperm;
 PubMed=1479546; DOI=10.1248/bpb1978.15.455;
 Okabe M., Ying X., Nagira M., Ikawa M., Kohama Y., Mimura T.,
 Tanaka K.;
 "Homology of an acrosome-reacted sperm-specific antigen to CD46.";
 J. Pharmacobio-Dyn. 15:455-459(1992).
 [17]
 PROTEIN SEQUENCE OF 35-58.
 PubMed=2298462; DOI=10.1007/BF00702485;
 Purcell D.F., Deacon N.J., Andrew S.M., McKenzie I.F.;
 "Human non-lineage antigen, CD46 (HuLy-m5): purification and partial
 sequencing demonstrates structural homology with complement-regulating
 glycoproteins.";
 Immunogenetics 31:21-28(1990).
 [18]
 PROTEIN SEQUENCE OF 35-49, AND BINDING TO MEASLES VIRUS.
 PubMed=8371352;
 Naniche D., Varior-Krishnan G., Cervoni F., Wild T.F., Rossi B.,
 Rabourdin-Combe C., Gerlier D.;
 "Human membrane cofactor protein (CD46) acts as a cellular receptor
 for measles virus.";
 J. Virol. 67:6025-6032(1993).
 [19]
 INTERACTION WITH C3B AND C4B.
 PubMed=1717583;
 Adams E.M., Brown M.C., Nunge M., Krych M., Atkinson J.P.;
 "Contribution of the repeating domains of membrane cofactor protein
 (CD46) of the complement system to ligand binding and cofactor
 activity.";
 J. Immunol. 147:3005-3011(1991).
 [20]
 ALTERNATIVE SPLICING.
 PubMed=1601037; DOI=10.1002/eji.1830220625;
 Russell S.M., Sparrow R.L., McKenzie I.F.C., Purcell D.F.J.;
 "Tissue-specific and allelic expression of the complement regulator
 CD46 is controlled by alternative splicing.";
 Eur. J. Immunol. 22:1513-1518(1992).
 [21]
 BINDING TO MEASLES VIRUS.
 PubMed=8402913; DOI=10.1016/0092-8674(93)80071-L;
 Doerig R.E., Marcil A., Chopra A., Richardson C.D.;
 "The human CD46 molecule is a receptor for measles virus (Edmonston
 strain).";
 Cell 75:295-305(1993).
 [22]
 BINDING TO MEASLES VIRUS.
 PubMed=7534417; DOI=10.1073/pnas.92.6.2303;
 Manchester M., Valsamakis A., Kaufman R., Liszewski M.K., Alvarez J.,
 Atkinson J.P., Lublin D.M., Oldstone M.B.;
 "Measles virus and C3 binding sites are distinct on membrane cofactor
 protein (CD46).";
 Proc. Natl. Acad. Sci. U.S.A. 92:2303-2307(1995).
 [23]
 FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH STREPTOCOCCUS
 PYOGENES M PROTEIN.
 PubMed=7708671; DOI=10.1073/pnas.92.7.2489;
 Okada N., Liszewski M.K., Atkinson J.P., Caparon M.;
 "Membrane cofactor protein (CD46) is a keratinocyte receptor for the M
 protein of the group A streptococcus.";
 Proc. Natl. Acad. Sci. U.S.A. 92:2489-2493(1995).
 [24]
 MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
 PubMed=8764003;
 Maisner A., Alvarez J., Liszewski M.K., Atkinson D.J., Atkinson J.P.,
 Herrler G.;
 "The N-glycan of the SCR 2 region is essential for membrane cofactor
 protein (CD46) to function as a measles virus receptor.";
 J. Virol. 70:4973-4977(1996).
 [25]
 FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH NEISSERIA TYPE IV
 PILI.
 PubMed=9379894; DOI=10.1046/j.1365-2958.1997.4841857.x;
 Kaellstroem H., Liszewski M.K., Atkinson J.P., Jonsson A.-B.;
 "Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor
 for pathogenic Neisseria.";
 Mol. Microbiol. 25:639-647(1997).
 [26]
 MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
 PubMed=9759896;
 Liszewski M.K., Leung M.K., Atkinson J.P.;
 "Membrane cofactor protein: importance of N- and O-glycosylation for
 complement regulatory function.";
 J. Immunol. 161:3711-3718(1998).
 [27]
 BINDING OF HUMAN HERPESVIRUS 6.
 PubMed=10619434; DOI=10.1016/S0092-8674(00)81678-5;
 Santoro F., Kennedy P.E., Locatelli G., Malnati M.S., Berger E.A.,
 Lusso P.;
 "CD46 is a cellular receptor for human herpesvirus 6.";
 Cell 99:817-827(1999).
 [28]
 PHOSPHORYLATION AT TYR-384 (ISOFORM B), PHOSPHORYLATION AT TYR-369
 (ISOFORM D), PHOSPHORYLATION AT TYR-354 (ISOFORM F), PHOSPHORYLATION
 AT TYR-370 (ISOFORM H), PHOSPHORYLATION AT TYR-355 (ISOFORM J),
 PHOSPHORYLATION AT TYR-340 (ISOFORM L), AND PHOSPHORYLATION AT TYR-321
 (ISOFORM 3).
 PubMed=10657632; DOI=10.4049/jimmunol.164.4.1839;
 Wang G., Liszewski M.K., Chan A.C., Atkinson J.P.;
 "Membrane cofactor protein (MCP; CD46): isoform-specific tyrosine
 phosphorylation.";
 J. Immunol. 164:1839-1846(2000).
 [29]
 FUNCTION.
 PubMed=10843656; DOI=10.4049/jimmunol.164.12.6091;
 Astier A., Trescol-Biemont M.-C., Azocar O., Lamouille B.,
 Rabourdin-Combe C.;
 "CD46, a new costimulatory molecule for T cells, that induces p120CBL
 and LAT phosphorylation.";
 J. Immunol. 164:6091-6095(2000).
 [30]
 FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MEASLES VIRUS H
 PROTEIN.
 PubMed=10972291; DOI=10.1038/35022579;
 Tatsuo H., Ono N., Tanaka K., Yanagi Y.;
 "SLAM (CDw150) is a cellular receptor for measles virus.";
 Nature 406:893-897(2000).
 [31]
 FUNCTION (MICROBIAL INFECTION), INTERACTION WITH NEISSERIA TYPE IV
 PILI, AND MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
 PubMed=11260136; DOI=10.1046/j.1462-5822.2001.00095.x;
 Kaellstroem H., Blackmer Gill D., Albiger B., Liszewski M.K.,
 Atkinson J.P., Jonsson A.-B.;
 "Attachment of Neisseria gonorrhoeae to the cellular pilus receptor
 CD46: identification of domains important for bacterial adherence.";
 Cell. Microbiol. 3:133-143(2001).
 [32]
 BINDING OF HUMAN HERPESVIRUS 6.
 PubMed=12171934; DOI=10.1074/jbc.M206488200;
 Greenstone H.L., Santoro F., Lusso P., Berger E.A.;
 "Human Herpesvirus 6 and Measles Virus employ distinct CD46 domains
 for receptor function.";
 J. Biol. Chem. 277:39112-39118(2002).
 [33]
 PHOSPHORYLATION (ISOFORMS B/D/F/H/J/L/3).
 PubMed=11901164; DOI=10.1083/jcb.200109005;
 Lee S.W., Bonnah R.A., Higashi D.L., Atkinson J.P., Milgram S.L.,
 So M.;
 "CD46 is phosphorylated at tyrosine 354 upon infection of epithelial
 cells by Neisseria gonorrhoeae.";
 J. Cell Biol. 156:951-957(2002).
 [34]
 FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH STREPTOCOCCUS
 PYOGENES M PROTEIN.
 PubMed=11971006; DOI=10.4049/jimmunol.168.9.4585;
 Giannakis E., Jokiranta T.S., Ormsby R.J., Duthy T.G., Male D.A.,
 Christiansen D., Fischetti V.A., Bagley C., Loveland B.E.,
 Gordon D.L.;
 "Identification of the streptococcal M protein binding site on
 membrane cofactor protein (CD46).";
 J. Immunol. 168:4585-4592(2002).
 [35]
 SUBCELLULAR LOCATION, AND GLYCOSYLATION.
 PubMed=12112588; DOI=10.1002/mrd.10144;
 Riley R.C., Kemper C., Leung M., Atkinson J.P.;
 "Characterization of human membrane cofactor protein (MCP; CD46) on
 spermatozoa.";
 Mol. Reprod. Dev. 62:534-546(2002).
 [36]
 FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN HERPESVIRUS
 6 GH PROTEIN.
 PubMed=12724329; DOI=10.1074/jbc.M302373200;
 Santoro F., Greenstone H.L., Insinga A., Liszewski M.K.,
 Atkinson J.P., Lusso P., Berger E.A.;
 "Interaction of glycoprotein H of human herpesvirus 6 with the
 cellular receptor CD46.";
 J. Biol. Chem. 278:25964-25969(2003).
 [37]
 SUBCELLULAR LOCATION.
 PubMed=14597734; DOI=10.1084/jem.20031159;
 Gill D.B., Koomey M., Cannon J.G., Atkinson J.P.;
 "Down-regulation of CD46 by piliated Neisseria gonorrhoeae.";
 J. Exp. Med. 198:1313-1322(2003).
 [38]
 FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN HERPESVIRUS
 6 GH PROTEIN.
 PubMed=12663806; DOI=10.1128/JVI.77.8.4992-4999.2003;
 Mori Y., Yang X., Akkapaiboon P., Okuno T., Yamanishi K.;
 "Human herpesvirus 6 variant A glycoprotein H-glycoprotein L-
 glycoprotein Q complex associates with human CD46.";
 J. Virol. 77:4992-4999(2003).
 [39]
 FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ADENOVIRUS
 B FIBER PROTEIN.
 PubMed=12915534; DOI=10.1128/JVI.77.17.9183-9191.2003;
 Segerman A., Atkinson J.P., Marttila M., Dennerquist V., Wadell G.,
 Arnberg N.;
 "Adenovirus type 11 uses CD46 as a cellular receptor.";
 J. Virol. 77:9183-9191(2003).
 [40]
 DISEASE.
 PubMed=14615110; DOI=10.1016/S0140-6736(03)14742-3;
 Noris M., Brioschi S., Caprioli J., Todeschini M., Bresin E.,
 Porrati F., Gamba S., Remuzzi G.;
 "Familial haemolytic uraemic syndrome and an MCP mutation.";
 Lancet 362:1542-1547(2003).
 [41]
 FUNCTION.
 PubMed=12540904; DOI=10.1038/nature01315;
 Kemper C., Chan A.C., Green J.M., Brett K.A., Murphy K.M.,
 Atkinson J.P.;
 "Activation of human CD4+ cells with CD3 and CD46 induces a T-
 regulatory cell 1 phenotype.";
 Nature 421:388-392(2003).
 [42]
 FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HUMAN ADENOVIRUS B
 FIBER PROTEIN, AND IDENTIFICATION BY MASS SPECTROMETRY.
 PubMed=14566335; DOI=10.1038/nm952;
 Gaggar A., Shayakhmetov D.M., Lieber A.;
 "CD46 is a cellular receptor for group B adenoviruses.";
 Nat. Med. 9:1408-1412(2003).
 [43]
 GLYCOSYLATION, AND SUBCELLULAR LOCATION.
 PubMed=15307194; DOI=10.1002/eji.200424969;
 Hakulinen J., Junnikkala S., Sorsa T., Meri S.;
 "Complement inhibitor membrane cofactor protein (MCP; CD46) is
 constitutively shed from cancer cell membranes in vesicles and
 converted by a metalloproteinase to a functionally active soluble
 form.";
 Eur. J. Immunol. 34:2620-2629(2004).
 [44]
 FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HUMAN ADENOVIRUS D
 TYPE 37 PIV/FIBER PROTEIN, AND IDENTIFICATION BY MASS SPECTROMETRY.
 PubMed=15047806; DOI=10.1128/JVI.78.8.3897-3905.2004;
 Wu E., Trauger S.A., Pache L., Mullen T.-M., von Seggern D.J.,
 Siuzdak G., Nemerow G.R.;
 "Membrane cofactor protein is a receptor for adenoviruses associated
 with epidemic keratoconjunctivitis.";
 J. Virol. 78:3897-3905(2004).
 [45]
 FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ADENOVIRUS
 B TYPE 3 FIBER PROTEIN.
 PubMed=15078926; DOI=10.1128/JVI.78.9.4454-4462.2004;
 Sirena D., Lilienfeld B., Eisenhut M., Kaelin S., Boucke K.,
 Beerli R.R., Vogt L., Ruedl C., Bachmann M.F., Greber U.F., Hemmi S.;
 "The human membrane cofactor CD46 is a receptor for species B
 adenovirus serotype 3.";
 J. Virol. 78:4454-4462(2004).
 [46]
 FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ADENOVIRUS
 B TYPE 35 FIBER PROTEIN.
 PubMed=15919905; DOI=10.1128/JVI.79.12.7503-7513.2005;
 Gaggar A., Shayakhmetov D.M., Liszewski M.K., Atkinson J.P.,
 Lieber A.;
 "Localization of regions in CD46 that interact with adenovirus.";
 J. Virol. 79:7503-7513(2005).
 [47]
 FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ADENOVIRUS
 B FIBER PROTEIN.
 PubMed=16254377; DOI=10.1128/JVI.79.22.14429-14436.2005;
 Marttila M., Persson D., Gustafsson D., Liszewski M.K., Atkinson J.P.,
 Wadell G., Arnberg N.;
 "CD46 is a cellular receptor for all species B adenoviruses except
 types 3 and 7.";
 J. Virol. 79:14429-14436(2005).
 [48]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Liver;
 PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
 Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
 Wang L., Ye M., Zou H.;
 "An enzyme assisted RP-RPLC approach for in-depth analysis of human
 liver phosphoproteome.";
 J. Proteomics 96:253-262(2014).
 [49]
 X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 35-160.
 PubMed=10357804; DOI=10.1093/emboj/18.11.2911;
 Casasnovas J.M., Larvie M., Stehle T.;
 "Crystal structure of two CD46 domains reveals an extended measles
 virus-binding surface.";
 EMBO J. 18:2911-2922(1999).
 [50]
 CHARACTERIZATION OF VARIANTS AHUS2 PRO-240 AND 271-ASP-SER-272 DEL.
 PubMed=14566051; DOI=10.1073/pnas.2135497100;
 Richards A., Kemp E.J., Liszewski M.K., Goodship J.A., Lampe A.K.,
 Decorte R., Muesluemanoglu M.H., Kavukcu S., Filler G., Pirson Y.,
 Wen L.S., Atkinson J.P., Goodship T.H.J.;
 "Mutations in human complement regulator, membrane cofactor protein
 (CD46), predispose to development of familial hemolytic uremic
 syndrome.";
 Proc. Natl. Acad. Sci. U.S.A. 100:12966-12971(2003).
 [51]
 VARIANT AHUS2 TYR-35.
 PubMed=16621965; DOI=10.1182/blood-2005-10-007252;
 The international registry of recurrent and familial HUS/TTP;
 Caprioli J., Noris M., Brioschi S., Pianetti G., Castelletti F.,
 Bettinaglio P., Mele C., Bresin E., Cassis L., Gamba S., Porrati F.,
 Bucchioni S., Monteferrante G., Fang C.J., Liszewski M.K.,
 Kavanagh D., Atkinson J.P., Remuzzi G.;
 "Genetics of HUS: the impact of MCP, CFH, and IF mutations on clinical
 presentation, response to treatment, and outcome.";
 Blood 108:1267-1279(2006).
 [52]
 VARIANT AHUS2 SER-165.
 PubMed=16386793; DOI=10.1016/j.molimm.2005.11.008;
 Esparza-Gordillo J., Jorge E.G., Garrido C.A., Carreras L.,
 Lopez-Trascasa M., Sanchez-Corral P., de Cordoba S.R.;
 "Insights into hemolytic uremic syndrome: segregation of three
 independent predisposition factors in a large, multiple affected
 pedigree.";
 Mol. Immunol. 43:1769-1775(2006).
 [53]
 VARIANTS [LARGE SCALE ANALYSIS] TYR-228 AND VAL-353.
 PubMed=16959974; DOI=10.1126/science.1133427;
 Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
 Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
 Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
 Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
 Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
 Vogelstein B., Kinzler K.W., Velculescu V.E.;
 "The consensus coding sequences of human breast and colorectal
 cancers.";
 Science 314:268-274(2006).
 [54]
 VARIANTS AHUS2 CYS-216 AND ARG-231.
 PubMed=20513133; DOI=10.1002/humu.21256;
 Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.;
 "Mutations in alternative pathway complement proteins in American
 patients with atypical hemolytic uremic syndrome.";
 Hum. Mutat. 31:E1445-E1460(2010).
 -!- 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).
 -!- SUBUNIT: Interacts with C3b (PubMed:1717583, PubMed:3260937).
     Interacts with C4b (PubMed:1717583). {ECO:0000269|PubMed:1717583,
     ECO:0000269|PubMed:3260937}.
 -!- SUBUNIT: (Microbial infection) Interacts with measles virus H
     protein. {ECO:0000269|PubMed:10972291}.
 -!- SUBUNIT: (Microbial infection) Interacts with human herpesvirus 6
     GH protein (PubMed:12663806, PubMed:12724329).
     {ECO:0000269|PubMed:12663806, ECO:0000269|PubMed:12724329}.
 -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus B/D
     fiber protein (PubMed:12915534, PubMed:14566335, PubMed:15047806,
     PubMed:15078926, PubMed:15919905, PubMed:16254377).
     {ECO:0000269|PubMed:12915534, ECO:0000269|PubMed:14566335,
     ECO:0000269|PubMed:15047806, ECO:0000269|PubMed:15078926,
     ECO:0000269|PubMed:15919905, ECO:0000269|PubMed:16254377}.
 -!- SUBUNIT: (Microbial infection) Binds to Streptococcus pyogenes M
     protein and to type IV pili from Neisseria (PubMed:7708671,
     PubMed:9379894, PubMed:11260136, PubMed:11971006).
     {ECO:0000269|PubMed:11260136, ECO:0000269|PubMed:11971006,
     ECO:0000269|PubMed:7708671, ECO:0000269|PubMed:9379894}.
 -!- INTERACTION:
     P78504:JAG1; NbExp=5; IntAct=EBI-2623451, EBI-2847071;
 -!- 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.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=16;
       Comment=Additional isoforms seem to exist. The complete
       sequences of the isoforms are not known. Isoforms are classified
       as alpha (isoform C and isoform D), beta (isoform E and isoform
       F), gamma (isoform A and isoform B) and delta (isoform N).
       Isoforms gamma are preferentially expressed in EBV-B cells and
       leukemic cells. Isoforms alpha (66 kDa) and isoforms beta (56
       kDa) are found in all tissues except sperm. Isoform delta is
       expressed in spermatozoa. The exon 9 is specifically deleted in
       some placentae isoforms. All tissues differentially splice exon
       13.;
     Name=A; Synonyms=no del, ABC1;
       IsoId=P15529-1; Sequence=Displayed;
     Name=B; Synonyms=del 13, ABC2;
       IsoId=P15529-2; Sequence=VSP_001204;
       Note=Contains a phosphotyrosine at position 384.
       {ECO:0000269|PubMed:10657632};
     Name=C; Synonyms=del 7, BC1;
       IsoId=P15529-11; Sequence=VSP_009174;
     Name=D; Synonyms=del 7-13, BC2;
       IsoId=P15529-3; Sequence=VSP_009174, VSP_001204;
       Note=Contains a phosphotyrosine at position 369.
       {ECO:0000269|PubMed:10657632};
     Name=E; Synonyms=del 7-8, C1;
       IsoId=P15529-12; Sequence=VSP_009175;
     Name=F; Synonyms=del 7-8-13, C2;
       IsoId=P15529-4; Sequence=VSP_009175, VSP_001204;
       Note=Contains a phosphotyrosine at position 354.
       {ECO:0000269|PubMed:10657632};
     Name=G; Synonyms=del 9;
       IsoId=P15529-13; Sequence=VSP_009177;
     Name=H; Synonyms=del 9-13;
       IsoId=P15529-5; Sequence=VSP_009177, VSP_001204;
       Note=Contains a phosphotyrosine at position 370.
       {ECO:0000269|PubMed:10657632};
     Name=I; Synonyms=del 7-9;
       IsoId=P15529-14; Sequence=VSP_009174, VSP_009177;
     Name=J; Synonyms=del 7-9-13;
       IsoId=P15529-6; Sequence=VSP_009174, VSP_009177, VSP_001204;
       Note=Contains a phosphotyrosine at position 355.
       {ECO:0000269|PubMed:10657632};
     Name=K; Synonyms=del 7-8-9;
       IsoId=P15529-15; Sequence=VSP_009176;
     Name=L; Synonyms=del 7-8-9-13;
       IsoId=P15529-7; Sequence=VSP_009176, VSP_001204;
       Note=Contains a phosphotyrosine at position 340.
       {ECO:0000269|PubMed:10657632};
     Name=M; Synonyms=del 7-12a-13;
       IsoId=P15529-8; Sequence=VSP_009174, VSP_001202, VSP_001203;
     Name=N; Synonyms=del 7-8-12-13;
       IsoId=P15529-9; Sequence=VSP_009175, VSP_009178;
       Note=No experimental confirmation available.;
     Name=2;
       IsoId=P15529-10; Sequence=VSP_001201;
     Name=3;
       IsoId=P15529-16; Sequence=VSP_019005, VSP_019006, VSP_001204;
       Note=Contains a phosphotyrosine at position 321.
       {ECO:0000269|PubMed:10657632};
 -!- TISSUE SPECIFICITY: Expressed by all cells except erythrocytes.
 -!- DOMAIN: Sushi domains 1 and 2 are required for interaction with
     human adenovirus B PIV/FIBER protein and with Measles virus H
     protein. Sushi domains 2 and 3 are required for Herpesvirus 6
     binding. Sushi domain 3 is required for Neisseria binding. Sushi
     domains 3 and 4 are required for interaction with Streptococcus
     pyogenes M protein and are the most important for interaction with
     C3b and C4b.
 -!- 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.
 -!- 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 variations 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.
 -!- WEB RESOURCE: Name=SeattleSNPs;
     URL="http://pga.gs.washington.edu/data/mcp/";
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution-NoDerivs License
 -----------------------------------------------------------------------
 EMBL; Y00651; CAA68675.1; -; mRNA.
 EMBL; M58050; AAA62833.1; -; mRNA.
 EMBL; X59405; -; NOT_ANNOTATED_CDS; mRNA.
 EMBL; X59406; -; NOT_ANNOTATED_CDS; mRNA.
 EMBL; X59407; -; NOT_ANNOTATED_CDS; mRNA.
 EMBL; X59408; -; NOT_ANNOTATED_CDS; mRNA.
 EMBL; X59409; -; NOT_ANNOTATED_CDS; mRNA.
 EMBL; X59410; -; NOT_ANNOTATED_CDS; mRNA.
 EMBL; S51940; AAB24802.1; -; mRNA.
 EMBL; D84105; BAA12224.1; -; mRNA.
 EMBL; EF076055; ABK81635.1; -; mRNA.
 EMBL; EF076056; ABK81636.1; -; mRNA.
 EMBL; EF076057; ABK81637.1; -; mRNA.
 EMBL; EF076058; ABK81638.1; -; mRNA.
 EMBL; AK291227; BAF83916.1; -; mRNA.
 EMBL; BX537451; CAD97694.1; -; mRNA.
 EMBL; BX640613; CAE45719.1; -; mRNA.
 EMBL; BX649050; CAI45983.1; -; mRNA.
 EMBL; AK222822; BAD96542.1; -; mRNA.
 EMBL; AY916779; AAW82433.1; -; Genomic_DNA.
 EMBL; AL365178; CAH73947.1; -; Genomic_DNA.
 EMBL; AL035209; CAH73947.1; JOINED; Genomic_DNA.
 EMBL; AL365178; CAH73948.1; -; Genomic_DNA.
 EMBL; AL035209; CAH73948.1; JOINED; Genomic_DNA.
 EMBL; AL365178; CAH73949.1; -; Genomic_DNA.
 EMBL; AL035209; CAH73949.1; JOINED; Genomic_DNA.
 EMBL; AL365178; CAH73950.1; -; Genomic_DNA.
 EMBL; AL035209; CAH73950.1; JOINED; Genomic_DNA.
 EMBL; AL365178; CAH73951.1; -; Genomic_DNA.
 EMBL; AL035209; CAH73951.1; JOINED; Genomic_DNA.
 EMBL; AL365178; CAH73952.1; -; Genomic_DNA.
 EMBL; AL035209; CAH73952.1; JOINED; Genomic_DNA.
 EMBL; AL365178; CAH73953.1; -; Genomic_DNA.
 EMBL; AL035209; CAH73953.1; JOINED; Genomic_DNA.
 EMBL; AL365178; CAH73954.1; -; Genomic_DNA.
 EMBL; AL035209; CAH73954.1; JOINED; Genomic_DNA.
 EMBL; AL035209; CAI18804.1; -; Genomic_DNA.
 EMBL; AL365178; CAI18804.1; JOINED; Genomic_DNA.
 EMBL; AL035209; CAI18805.1; -; Genomic_DNA.
 EMBL; AL365178; CAI18805.1; JOINED; Genomic_DNA.
 EMBL; AL035209; CAI18806.1; -; Genomic_DNA.
 EMBL; AL365178; CAI18806.1; JOINED; Genomic_DNA.
 EMBL; AL035209; CAI18807.1; -; Genomic_DNA.
 EMBL; AL365178; CAI18807.1; JOINED; Genomic_DNA.
 EMBL; AL035209; CAI18808.1; -; Genomic_DNA.
 EMBL; AL365178; CAI18808.1; JOINED; Genomic_DNA.
 EMBL; AL035209; CAI18809.1; -; Genomic_DNA.
 EMBL; AL365178; CAI18809.1; JOINED; Genomic_DNA.
 EMBL; AL035209; CAI18810.1; -; Genomic_DNA.
 EMBL; AL365178; CAI18810.1; JOINED; Genomic_DNA.
 EMBL; AL035209; CAI18811.1; -; Genomic_DNA.
 EMBL; AL365178; CAI18811.1; JOINED; Genomic_DNA.
 EMBL; CH471100; EAW93465.1; -; Genomic_DNA.
 EMBL; CH471100; EAW93470.1; -; Genomic_DNA.
 EMBL; CH471100; EAW93476.1; -; Genomic_DNA.
 EMBL; BC030594; AAH30594.1; -; mRNA.
 EMBL; AF209712; AAF73844.1; -; mRNA.
 EMBL; AF209713; AAF73845.1; -; mRNA.
 EMBL; AF209714; AAF73846.1; -; mRNA.
 EMBL; S65879; AAD13968.1; -; Genomic_DNA.
 CCDS; CCDS1479.1; -. [P15529-9]
 CCDS; CCDS1480.1; -. [P15529-3]
 CCDS; CCDS1481.1; -. [P15529-4]
 CCDS; CCDS1482.1; -. [P15529-2]
 CCDS; CCDS1484.1; -. [P15529-7]
 CCDS; CCDS1485.1; -. [P15529-1]
 CCDS; CCDS31008.1; -. [P15529-11]
 CCDS; CCDS31009.1; -. [P15529-12]
 PIR; G02913; G02913.
 PIR; I54479; I54479.
 PIR; I57998; I57998.
 PIR; S01896; S01896.
 RefSeq; NP_002380.3; NM_002389.4. [P15529-1]
 RefSeq; NP_722548.1; NM_153826.3. [P15529-3]
 RefSeq; NP_758860.1; NM_172350.2. [P15529-9]
 RefSeq; NP_758861.1; NM_172351.2. [P15529-11]
 RefSeq; NP_758862.1; NM_172352.2. [P15529-12]
 RefSeq; NP_758863.1; NM_172353.2. [P15529-4]
 RefSeq; NP_758869.1; NM_172359.2. [P15529-2]
 RefSeq; NP_758871.1; NM_172361.2. [P15529-7]
 RefSeq; XP_011507865.1; XM_011509563.1. [P15529-5]
 RefSeq; XP_011507866.1; XM_011509564.1. [P15529-6]
 RefSeq; XP_016856797.1; XM_017001308.1. [P15529-13]
 RefSeq; XP_016856798.1; XM_017001309.1. [P15529-14]
 RefSeq; XP_016856799.1; XM_017001310.1. [P15529-15]
 UniGene; Hs.510402; -.
 PDB; 1CKL; X-ray; 3.10 A; A/B/C/D/E/F=35-160.
 PDB; 1HR4; Model; -; A=159-284.
 PDB; 2O39; X-ray; 2.85 A; C/D=35-160.
 PDB; 3INB; X-ray; 3.10 A; C/D=35-160.
 PDB; 3L89; X-ray; 3.50 A; M/N/O/P/Q/R/S/T/U/V/W/X=35-160.
 PDB; 3O8E; X-ray; 2.84 A; B/D=35-286.
 PDB; 5FO8; X-ray; 2.40 A; C=35-286.
 PDBsum; 1CKL; -.
 PDBsum; 1HR4; -.
 PDBsum; 2O39; -.
 PDBsum; 3INB; -.
 PDBsum; 3L89; -.
 PDBsum; 3O8E; -.
 PDBsum; 5FO8; -.
 ProteinModelPortal; P15529; -.
 SMR; P15529; -.
 BioGrid; 110346; 11.
 DIP; DIP-41232N; -.
 IntAct; P15529; 9.
 STRING; 9606.ENSP00000313875; -.
 iPTMnet; P15529; -.
 PhosphoSitePlus; P15529; -.
 SwissPalm; P15529; -.
 BioMuta; CD46; -.
 DMDM; 41019474; -.
 EPD; P15529; -.
 MaxQB; P15529; -.
 PaxDb; P15529; -.
 PeptideAtlas; P15529; -.
 PRIDE; P15529; -.
 TopDownProteomics; P15529-4; -. [P15529-4]
 Ensembl; ENST00000322875; ENSP00000313875; ENSG00000117335. [P15529-2]
 Ensembl; ENST00000322918; ENSP00000314664; ENSG00000117335. [P15529-9]
 Ensembl; ENST00000354848; ENSP00000346912; ENSG00000117335. [P15529-3]
 Ensembl; ENST00000357714; ENSP00000350346; ENSG00000117335. [P15529-4]
 Ensembl; ENST00000358170; ENSP00000350893; ENSG00000117335. [P15529-1]
 Ensembl; ENST00000360212; ENSP00000353342; ENSG00000117335. [P15529-7]
 Ensembl; ENST00000367041; ENSP00000356008; ENSG00000117335. [P15529-12]
 Ensembl; ENST00000367042; ENSP00000356009; ENSG00000117335. [P15529-11]
 Ensembl; ENST00000367047; ENSP00000356014; ENSG00000117335. [P15529-16]
 Ensembl; ENST00000480003; ENSP00000418471; ENSG00000117335. [P15529-6]
 GeneID; 4179; -.
 KEGG; hsa:4179; -.
 UCSC; uc001hgc.4; human. [P15529-1]
 CTD; 4179; -.
 DisGeNET; 4179; -.
 EuPathDB; HostDB:ENSG00000117335.18; -.
 GeneCards; CD46; -.
 GeneReviews; CD46; -.
 HGNC; HGNC:6953; CD46.
 HPA; CAB010401; -.
 HPA; HPA016903; -.
 MalaCards; CD46; -.
 MIM; 120920; gene+phenotype.
 MIM; 612922; phenotype.
 neXtProt; NX_P15529; -.
 OpenTargets; ENSG00000117335; -.
 Orphanet; 93576; Atypical hemolytic-uremic syndrome with MCP/CD46 anomaly.
 Orphanet; 244242; HELLP syndrome.
 PharmGKB; PA30700; -.
 eggNOG; ENOG410IY7G; Eukaryota.
 eggNOG; ENOG4111CPD; LUCA.
 GeneTree; ENSGT00910000143999; -.
 HOVERGEN; HBG006335; -.
 InParanoid; P15529; -.
 KO; K04007; -.
 OMA; TYSCDPA; -.
 OrthoDB; EOG091G0DWA; -.
 PhylomeDB; P15529; -.
 TreeFam; TF334137; -.
 Reactome; R-HSA-977606; Regulation of Complement cascade.
 SIGNOR; P15529; -.
 ChiTaRS; CD46; human.
 EvolutionaryTrace; P15529; -.
 GeneWiki; CD46; -.
 GenomeRNAi; 4179; -.
 PMAP-CutDB; P15529; -.
 PRO; PR:P15529; -.
 Proteomes; UP000005640; Chromosome 1.
 Bgee; ENSG00000117335; -.
 ExpressionAtlas; P15529; baseline and differential.
 Genevisible; P15529; HS.
 GO; GO:0009986; C:cell surface; IDA:UniProtKB.
 GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
 GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
 GO; GO:0002079; C:inner acrosomal membrane; IEA:UniProtKB-SubCell.
 GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
 GO; GO:0005886; C:plasma membrane; IDA:AgBase.
 GO; GO:0045296; F:cadherin binding; IPI:UniProtKB.
 GO; GO:0004872; F:receptor activity; TAS:ProtInc.
 GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
 GO; GO:0002250; P:adaptive immune response; IC:UniProtKB.
 GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
 GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
 GO; GO:0032613; P:interleukin-10 production; IDA:UniProtKB.
 GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
 GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
 GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
 GO; GO:0043382; P:positive regulation of memory T cell differentiation; IDA:UniProtKB.
 GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IDA:UniProtKB.
 GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
 GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IDA:UniProtKB.
 GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
 GO; GO:0008593; P:regulation of Notch signaling pathway; IDA:UniProtKB.
 GO; GO:0035581; P:sequestering of extracellular ligand from receptor; IDA:UniProtKB.
 GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
 GO; GO:0002456; P:T cell mediated immunity; IMP:UniProtKB.
 CDD; cd00033; CCP; 4.
 InterPro; IPR017341; CD46.
 InterPro; IPR035976; Sushi/SCR/CCP_sf.
 InterPro; IPR000436; Sushi_SCR_CCP_dom.
 Pfam; PF00084; Sushi; 4.
 PIRSF; PIRSF037971; TLX_CD46; 1.
 SMART; SM00032; CCP; 4.
 SUPFAM; SSF57535; SSF57535; 4.
 PROSITE; PS50923; SUSHI; 4.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Complement pathway;
 Complete proteome; Cytoplasmic vesicle; Direct protein sequencing;
 Disease mutation; Disulfide bond; Fertilization; Glycoprotein;
 Hemolytic uremic syndrome; Host cell receptor for virus entry;
 Host-virus interaction; Immunity; Innate immunity; Membrane;
 Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
 Signal; Sushi; Transmembrane; Transmembrane helix.
 SIGNAL        1     34       {ECO:0000269|PubMed:1479546,
                              ECO:0000269|PubMed:2298462,
                              ECO:0000269|PubMed:3260937,
                              ECO:0000269|PubMed:8371352}.
 CHAIN        35    392       Membrane cofactor protein.
                              /FTId=PRO_0000006008.
 TOPO_DOM     35    343       Extracellular. {ECO:0000255}.
 TRANSMEM    344    366       Helical. {ECO:0000255}.
 TOPO_DOM    367    392       Cytoplasmic. {ECO:0000255}.
 DOMAIN       35     96       Sushi 1. {ECO:0000255|PROSITE-
                              ProRule:PRU00302}.
 DOMAIN       97    159       Sushi 2. {ECO:0000255|PROSITE-
                              ProRule:PRU00302}.
 DOMAIN      160    225       Sushi 3. {ECO:0000255|PROSITE-
                              ProRule:PRU00302}.
 DOMAIN      226    285       Sushi 4. {ECO:0000255|PROSITE-
                              ProRule:PRU00302}.
 COMPBIAS    302    326       Ser/Thr-rich.
 CARBOHYD     83     83       N-linked (GlcNAc...) asparagine.
 CARBOHYD    114    114       N-linked (GlcNAc...) asparagine.
 CARBOHYD    163    163       O-linked (GalNAc...) threonine.
                              {ECO:0000255}.
 CARBOHYD    273    273       N-linked (GlcNAc...) asparagine.
 CARBOHYD    290    290       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 CARBOHYD    291    291       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 CARBOHYD    292    292       O-linked (GalNAc...) threonine.
                              {ECO:0000255}.
 CARBOHYD    298    298       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 CARBOHYD    300    300       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 CARBOHYD    302    302       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 CARBOHYD    303    303       O-linked (GalNAc...) threonine.
                              {ECO:0000255}.
 CARBOHYD    304    304       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 CARBOHYD    305    305       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 CARBOHYD    306    306       O-linked (GalNAc...) threonine.
                              {ECO:0000255}.
 CARBOHYD    307    307       O-linked (GalNAc...) threonine.
                              {ECO:0000255}.
 CARBOHYD    309    309       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 CARBOHYD    312    312       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 CARBOHYD    313    313       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 CARBOHYD    315    315       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 CARBOHYD    320    320       O-linked (GalNAc...) threonine.
                              {ECO:0000255}.
 CARBOHYD    326    326       O-linked (GalNAc...) serine.
                              {ECO:0000255}.
 DISULFID     35     80       {ECO:0000255|PROSITE-ProRule:PRU00302}.
 DISULFID     64     94       {ECO:0000255|PROSITE-ProRule:PRU00302}.
 DISULFID     99    141       {ECO:0000255|PROSITE-ProRule:PRU00302}.
 DISULFID    127    157       {ECO:0000255|PROSITE-ProRule:PRU00302}.
 DISULFID    162    210       {ECO:0000255|PROSITE-ProRule:PRU00302}.
 DISULFID    191    223       {ECO:0000255|PROSITE-ProRule:PRU00302}.
 DISULFID    228    270       {ECO:0000255|PROSITE-ProRule:PRU00302}.
 DISULFID    256    283       {ECO:0000255|PROSITE-ProRule:PRU00302}.
 VAR_SEQ      33     33       D -> G (in isoform 3). {ECO:0000305}.
                              /FTId=VSP_019005.
 VAR_SEQ      34     96       Missing (in isoform 3). {ECO:0000305}.
                              /FTId=VSP_019006.
 VAR_SEQ     286    329       Missing (in isoform K and isoform L).
                              {ECO:0000303|Ref.6}.
                              /FTId=VSP_009176.
 VAR_SEQ     286    315       Missing (in isoform E, isoform F and
                              isoform N). {ECO:0000303|PubMed:1711570,
                              ECO:0000303|PubMed:17974005,
                              ECO:0000303|PubMed:8418811,
                              ECO:0000303|PubMed:9659228,
                              ECO:0000303|Ref.6}.
                              /FTId=VSP_009175.
 VAR_SEQ     286    300       Missing (in isoform C, isoform D, isoform
                              I, isoform J and isoform M).
                              {ECO:0000303|PubMed:14702039,
                              ECO:0000303|PubMed:15489334,
                              ECO:0000303|PubMed:1711570,
                              ECO:0000303|PubMed:17974005,
                              ECO:0000303|PubMed:2050389,
                              ECO:0000303|PubMed:3260937,
                              ECO:0000303|Ref.6}.
                              /FTId=VSP_009174.
 VAR_SEQ     301    305       Missing (in isoform 2). {ECO:0000305}.
                              /FTId=VSP_001201.
 VAR_SEQ     316    329       Missing (in isoform G, isoform H, isoform
                              I and isoform J). {ECO:0000305}.
                              /FTId=VSP_009177.
 VAR_SEQ     355    392       VVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL ->
                              GKQMVELNMPLTRLNQPLQQSREAE (in isoform N).
                              {ECO:0000303|PubMed:9659228}.
                              /FTId=VSP_009178.
 VAR_SEQ     355    367       Missing (in isoform M). {ECO:0000305}.
                              /FTId=VSP_001202.
 VAR_SEQ     368    392       YLQRRKKKGTYLTDETHREVKFTSL -> GKQMVELNMPLT
                              RLNQPLQQSREAE (in isoform M).
                              {ECO:0000305}.
                              /FTId=VSP_001203.
 VAR_SEQ     377    392       TYLTDETHREVKFTSL -> KADGGAEYATYQTKSTTPAEQ
                              RG (in isoform B, isoform D, isoform F,
                              isoform H, isoform J, isoform L and
                              isoform 3). {ECO:0000303|PubMed:14702039,
                              ECO:0000303|PubMed:15489334,
                              ECO:0000303|PubMed:1711570,
                              ECO:0000303|PubMed:17974005,
                              ECO:0000303|PubMed:3260937,
                              ECO:0000303|PubMed:8418811,
                              ECO:0000303|Ref.6, ECO:0000303|Ref.9}.
                              /FTId=VSP_001204.
 VARIANT      13     13       S -> F (in dbSNP:rs138843816).
                              {ECO:0000269|PubMed:10751138,
                              ECO:0000269|Ref.9}.
                              /FTId=VAR_026567.
 VARIANT      35     35       C -> Y (in AHUS2; dbSNP:rs121909591).
                              {ECO:0000269|PubMed:16621965}.
                              /FTId=VAR_063656.
 VARIANT      59     59       R -> Q (in dbSNP:rs780693519).
                              {ECO:0000269|PubMed:10751138}.
                              /FTId=VAR_026568.
 VARIANT     165    165       P -> S (in AHUS2; reduced cell surface
                              expression; dbSNP:rs759136081).
                              {ECO:0000269|PubMed:16386793}.
                              /FTId=VAR_026569.
 VARIANT     216    216       W -> C (in AHUS2).
                              {ECO:0000269|PubMed:20513133}.
                              /FTId=VAR_063657.
 VARIANT     228    228       C -> Y (in a colorectal cancer sample;
                              somatic mutation).
                              {ECO:0000269|PubMed:16959974}.
                              /FTId=VAR_035828.
 VARIANT     231    231       P -> R (in AHUS2).
                              {ECO:0000269|PubMed:20513133}.
                              /FTId=VAR_063658.
 VARIANT     240    240       S -> P (in AHUS2; no change in cell
                              surface expression but reduced activity;
                              dbSNP:rs121909589).
                              {ECO:0000269|PubMed:14566051}.
                              /FTId=VAR_026570.
 VARIANT     266    266       D -> N (in dbSNP:rs17006830).
                              {ECO:0000269|Ref.10}.
                              /FTId=VAR_022262.
 VARIANT     271    272       Missing (in AHUS2; no cell surface
                              expression).
                              {ECO:0000269|PubMed:14566051}.
                              /FTId=VAR_026571.
 VARIANT     324    324       P -> L (in dbSNP:rs41317833).
                              {ECO:0000269|Ref.10}.
                              /FTId=VAR_022263.
 VARIANT     353    353       A -> V (in dbSNP:rs35366573).
                              {ECO:0000269|PubMed:16959974,
                              ECO:0000269|Ref.10}.
                              /FTId=VAR_022264.
 VARIANT     355    355       V -> G. {ECO:0000269|Ref.10}.
                              /FTId=VAR_022265.
 MUTAGEN      83     83       N->Q: No effect on cytoprotective
                              function. No effect on Neisseria binding.
                              No effect on Measles virus binding.
                              {ECO:0000269|PubMed:11260136,
                              ECO:0000269|PubMed:8764003,
                              ECO:0000269|PubMed:9759896}.
 MUTAGEN     114    114       N->Q: Strongly decreases cytoprotective
                              function. Decreases Neisseria binding.
                              Abolishes Measles virus binding.
                              {ECO:0000269|PubMed:11260136,
                              ECO:0000269|PubMed:8764003,
                              ECO:0000269|PubMed:9759896}.
 MUTAGEN     273    273       N->Q: Strongly decreases cytoprotective
                              function. Abolishes Neisseria binding. No
                              effect on Measles virus binding.
                              {ECO:0000269|PubMed:11260136,
                              ECO:0000269|PubMed:8764003,
                              ECO:0000269|PubMed:9759896}.
 CONFLICT     25     25       V -> A (in Ref. 8; CAE45719).
                              {ECO:0000305}.
 CONFLICT    108    108       G -> S (in Ref. 8; CAD97694).
                              {ECO:0000305}.
 CONFLICT    159    159       K -> S (in Ref. 8; CAD97694).
                              {ECO:0000305}.
 CONFLICT    162    162       C -> R (in Ref. 8; CAI45983).
                              {ECO:0000305}.
 STRAND       42     48       {ECO:0000244|PDB:3O8E}.
 STRAND       59     64       {ECO:0000244|PDB:3O8E}.
 STRAND       68     70       {ECO:0000244|PDB:3O8E}.
 STRAND       72     74       {ECO:0000244|PDB:3O8E}.
 STRAND       77     80       {ECO:0000244|PDB:3O8E}.
 STRAND       84     86       {ECO:0000244|PDB:3O8E}.
 HELIX        91     93       {ECO:0000244|PDB:3L89}.
 STRAND       94     96       {ECO:0000244|PDB:3O8E}.
 STRAND      108    112       {ECO:0000244|PDB:3O8E}.
 STRAND      115    118       {ECO:0000244|PDB:3O8E}.
 STRAND      122    127       {ECO:0000244|PDB:3O8E}.
 STRAND      131    135       {ECO:0000244|PDB:3O8E}.
 STRAND      137    146       {ECO:0000244|PDB:3O8E}.
 STRAND      148    152       {ECO:0000244|PDB:3O8E}.
 STRAND      156    159       {ECO:0000244|PDB:3O8E}.
 STRAND      171    174       {ECO:0000244|PDB:5FO8}.
 STRAND      183    191       {ECO:0000244|PDB:5FO8}.
 STRAND      195    198       {ECO:0000244|PDB:5FO8}.
 STRAND      201    204       {ECO:0000244|PDB:5FO8}.
 STRAND      206    210       {ECO:0000244|PDB:5FO8}.
 HELIX       212    214       {ECO:0000244|PDB:5FO8}.
 STRAND      215    218       {ECO:0000244|PDB:5FO8}.
 STRAND      222    224       {ECO:0000244|PDB:5FO8}.
 STRAND      236    240       {ECO:0000244|PDB:5FO8}.
 STRAND      251    256       {ECO:0000244|PDB:5FO8}.
 STRAND      260    264       {ECO:0000244|PDB:5FO8}.
 STRAND      266    270       {ECO:0000244|PDB:5FO8}.
 STRAND      276    278       {ECO:0000244|PDB:5FO8}.
 STRAND      282    285       {ECO:0000244|PDB:5FO8}.
 SEQUENCE   392 AA;  43747 MW;  85FE0CF100EA703E CRC64;
 MEPPGRRECP FPSWRFPGLL LAAMVLLLYS FSDACEEPPT FEAMELIGKP KPYYEIGERV
 DYKCKKGYFY IPPLATHTIC DRNHTWLPVS DDACYRETCP YIRDPLNGQA VPANGTYEFG
 YQMHFICNEG YYLIGEEILY CELKGSVAIW SGKPPICEKV LCTPPPKIKN GKHTFSEVEV
 FEYLDAVTYS CDPAPGPDPF SLIGESTIYC GDNSVWSRAA PECKVVKCRF PVVENGKQIS
 GFGKKFYYKA TVMFECDKGF YLDGSDTIVC DSNSTWDPPV PKCLKVLPPS STKPPALSHS
 VSTSSTTKSP ASSASGPRPT YKPPVSNYPG YPKPEEGILD SLDVWVIAVI VIAIVVGVAV
 ICVVPYRYLQ RRKKKGTYLT DETHREVKFT SL

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