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Membrane cofactor protein (TLX) (Trophoblast leukocyte common antigen) (CD antigen CD46)

 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.
20-JUN-2018, entry version 208.
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/";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
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; AL035209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL365178; -; NOT_ANNOTATED_CDS; 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; -.
ProteomicsDB; 53167; -.
ProteomicsDB; 53168; -. [P15529-10]
ProteomicsDB; 53169; -. [P15529-11]
ProteomicsDB; 53170; -. [P15529-12]
ProteomicsDB; 53171; -. [P15529-13]
ProteomicsDB; 53172; -. [P15529-14]
ProteomicsDB; 53173; -. [P15529-15]
ProteomicsDB; 53174; -. [P15529-16]
ProteomicsDB; 53175; -. [P15529-2]
ProteomicsDB; 53176; -. [P15529-3]
ProteomicsDB; 53177; -. [P15529-4]
ProteomicsDB; 53178; -. [P15529-5]
ProteomicsDB; 53179; -. [P15529-6]
ProteomicsDB; 53180; -. [P15529-7]
ProteomicsDB; 53181; -. [P15529-8]
ProteomicsDB; 53182; -. [P15529-9]
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:0038023; F:signaling 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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