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Database: UniProt
Entry: P15529
LinkDB: P15529
Original site: P15529 
ID   MCP_HUMAN               Reviewed;         392 AA.
AC   P15529; A0T1T0; A0T1T1; A0T1T2; Q15429; Q53GV9; Q5HY94; Q5VWS6; Q5VWS7;
AC   Q5VWS8; Q5VWS9; Q5VWT0; Q5VWT1; Q5VWT2; Q6N0A1; Q7Z3R5; Q9NNW2; Q9NNW3;
AC   Q9NNW4; Q9UCJ4;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 3.
DT   02-JUN-2021, entry version 229.
DE   RecName: Full=Membrane cofactor protein;
DE   AltName: Full=TLX;
DE   AltName: Full=Trophoblast leukocyte common antigen;
DE   AltName: CD_antigen=CD46;
DE   Flags: Precursor;
GN   Name=CD46; Synonyms=MCP, MIC10;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), PROTEIN SEQUENCE OF 35-58, AND
RP   INTERACTION WITH C3B.
RX   PubMed=3260937; DOI=10.1084/jem.168.1.181;
RA   Lublin D.M., Liszewski M.K., Post T.W., Arce M.A., le Beau M.M.,
RA   Rebentisch M.B., Lemons R.S., Seya T., Atkinson J.P.;
RT   "Molecular cloning and chromosomal localization of human membrane cofactor
RT   protein (MCP). Evidence for inclusion in the multigene family of
RT   complement-regulatory proteins.";
RL   J. Exp. Med. 168:181-194(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), AND ALTERNATIVE SPLICING.
RX   PubMed=2050389; DOI=10.1007/bf00216692;
RA   Purcell D.F., Russell S.M., Deacon N.J., Brown M.A., Hooker D.J.,
RA   McKenzie I.F.;
RT   "Alternatively spliced RNAs encode several isoforms of CD46 (MCP), a
RT   regulator of complement activation.";
RL   Immunogenetics 33:335-344(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D; E AND F).
RX   PubMed=1711570; DOI=10.1084/jem.174.1.93;
RA   Post T.W., Liszewski M.K., Adams E.M., Tedja I., Miller E.A.,
RA   Atkinson J.P.;
RT   "Membrane cofactor protein of the complement system: alternative splicing
RT   of serine/threonine/proline-rich exons and cytoplasmic tails produces
RT   multiple isoforms that correlate with protein phenotype.";
RL   J. Exp. Med. 174:93-102(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F).
RC   TISSUE=Testis;
RX   PubMed=8418811; DOI=10.1002/mrd.1080340117;
RA   Cervoni F., Fenichel P., Akhoundi C., Hsi B.L., Rossi B.;
RT   "Characterization of a cDNA clone coding for human testis membrane cofactor
RT   protein (MCP, CD46).";
RL   Mol. Reprod. Dev. 34:107-113(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N).
RC   TISSUE=Testis;
RX   PubMed=9659228; DOI=10.1046/j.1365-2567.1998.00455.x;
RA   Hara T., Suzuki Y., Nakazawa T., Nishimura H., Nagasawa S., Nishiguchi M.,
RA   Matsumoto M., Hatanaka M., Kitamura M., Seya T.;
RT   "Post-translational modification and intracellular localization of a splice
RT   product of CD46 cloned from human testis: role of the intracellular domains
RT   in O-glycosylation.";
RL   Immunology 93:546-555(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS D; F AND L).
RA   Xue Z.T., Widegren B., Salford L.;
RT   "Molecular cloning of human CD46 (membrane cofactor protein) CDS from
RT   cancer cell lines in a retroviral vector system.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC   TISSUE=Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS D AND E).
RC   TISSUE=Fetal kidney, Liver, and Salivary gland;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND VARIANT PHE-13.
RC   TISSUE=Liver;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-266; LEU-324; VAL-353
RP   AND GLY-355.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-158, AND VARIANTS PHE-13 AND GLN-59.
RX   PubMed=10751138; DOI=10.1086/315386;
RA   Kusuhara K., Sasaki Y., Nakao F., Ihara K., Hattori H., Yamashita S.,
RA   Nihei K., Koide N., Aiba H., Takeshita K., Hara T.;
RT   "Analysis of measles virus binding sites of the CD46 gene in patients with
RT   subacute sclerosing panencephalitis.";
RL   J. Infect. Dis. 181:1447-1449(2000).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RX   PubMed=7691939;
RA   Cui W., Hourcade D., Post T.W., Greenlund A.C., Atkinson J.P., Kumar V.;
RT   "Characterization of the promoter region of the membrane cofactor protein
RT   (CD46) gene of the human complement system and comparison to a membrane
RT   cofactor protein-like genetic element.";
RL   J. Immunol. 151:4137-4146(1993).
RN   [16]
RP   PROTEIN SEQUENCE OF 35-60.
RC   TISSUE=Sperm;
RX   PubMed=1479546; DOI=10.1248/bpb1978.15.455;
RA   Okabe M., Ying X., Nagira M., Ikawa M., Kohama Y., Mimura T., Tanaka K.;
RT   "Homology of an acrosome-reacted sperm-specific antigen to CD46.";
RL   J. Pharmacobio-Dyn. 15:455-459(1992).
RN   [17]
RP   PROTEIN SEQUENCE OF 35-58.
RX   PubMed=2298462; DOI=10.1007/bf00702485;
RA   Purcell D.F., Deacon N.J., Andrew S.M., McKenzie I.F.;
RT   "Human non-lineage antigen, CD46 (HuLy-m5): purification and partial
RT   sequencing demonstrates structural homology with complement-regulating
RT   glycoproteins.";
RL   Immunogenetics 31:21-28(1990).
RN   [18]
RP   PROTEIN SEQUENCE OF 35-49, AND BINDING TO MEASLES VIRUS.
RX   PubMed=8371352; DOI=10.1128/jvi.67.10.6025-6032.1993;
RA   Naniche D., Varior-Krishnan G., Cervoni F., Wild T.F., Rossi B.,
RA   Rabourdin-Combe C., Gerlier D.;
RT   "Human membrane cofactor protein (CD46) acts as a cellular receptor for
RT   measles virus.";
RL   J. Virol. 67:6025-6032(1993).
RN   [19]
RP   INTERACTION WITH C3B AND C4B.
RX   PubMed=1717583;
RA   Adams E.M., Brown M.C., Nunge M., Krych M., Atkinson J.P.;
RT   "Contribution of the repeating domains of membrane cofactor protein (CD46)
RT   of the complement system to ligand binding and cofactor activity.";
RL   J. Immunol. 147:3005-3011(1991).
RN   [20]
RP   ALTERNATIVE SPLICING.
RX   PubMed=1601037; DOI=10.1002/eji.1830220625;
RA   Russell S.M., Sparrow R.L., McKenzie I.F.C., Purcell D.F.J.;
RT   "Tissue-specific and allelic expression of the complement regulator CD46 is
RT   controlled by alternative splicing.";
RL   Eur. J. Immunol. 22:1513-1518(1992).
RN   [21]
RP   BINDING TO MEASLES VIRUS.
RX   PubMed=8402913; DOI=10.1016/0092-8674(93)80071-l;
RA   Doerig R.E., Marcil A., Chopra A., Richardson C.D.;
RT   "The human CD46 molecule is a receptor for measles virus (Edmonston
RT   strain).";
RL   Cell 75:295-305(1993).
RN   [22]
RP   BINDING TO MEASLES VIRUS.
RX   PubMed=7534417; DOI=10.1073/pnas.92.6.2303;
RA   Manchester M., Valsamakis A., Kaufman R., Liszewski M.K., Alvarez J.,
RA   Atkinson J.P., Lublin D.M., Oldstone M.B.;
RT   "Measles virus and C3 binding sites are distinct on membrane cofactor
RT   protein (CD46).";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:2303-2307(1995).
RN   [23]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH STREPTOCOCCUS PYOGENES
RP   M PROTEIN.
RX   PubMed=7708671; DOI=10.1073/pnas.92.7.2489;
RA   Okada N., Liszewski M.K., Atkinson J.P., Caparon M.;
RT   "Membrane cofactor protein (CD46) is a keratinocyte receptor for the M
RT   protein of the group A streptococcus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:2489-2493(1995).
RN   [24]
RP   INTERACTION WITH MSN.
RX   PubMed=7884872; DOI=10.1128/jvi.69.4.2248-2256.1995;
RA   Schneider-Schaulies J., Dunster L.M., Schwartz-Albiez R., Krohne G.,
RA   ter Meulen V.;
RT   "Physical association of moesin and CD46 as a receptor complex for measles
RT   virus.";
RL   J. Virol. 69:2248-2256(1995).
RN   [25]
RP   MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
RX   PubMed=8764003; DOI=10.1128/jvi.70.8.4973-4977.1996;
RA   Maisner A., Alvarez J., Liszewski M.K., Atkinson D.J., Atkinson J.P.,
RA   Herrler G.;
RT   "The N-glycan of the SCR 2 region is essential for membrane cofactor
RT   protein (CD46) to function as a measles virus receptor.";
RL   J. Virol. 70:4973-4977(1996).
RN   [26]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH NEISSERIA TYPE IV
RP   PILI.
RX   PubMed=9379894; DOI=10.1046/j.1365-2958.1997.4841857.x;
RA   Kaellstroem H., Liszewski M.K., Atkinson J.P., Jonsson A.-B.;
RT   "Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for
RT   pathogenic Neisseria.";
RL   Mol. Microbiol. 25:639-647(1997).
RN   [27]
RP   MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
RX   PubMed=9759896;
RA   Liszewski M.K., Leung M.K., Atkinson J.P.;
RT   "Membrane cofactor protein: importance of N- and O-glycosylation for
RT   complement regulatory function.";
RL   J. Immunol. 161:3711-3718(1998).
RN   [28]
RP   BINDING OF HUMAN HERPESVIRUS 6.
RX   PubMed=10619434; DOI=10.1016/s0092-8674(00)81678-5;
RA   Santoro F., Kennedy P.E., Locatelli G., Malnati M.S., Berger E.A.,
RA   Lusso P.;
RT   "CD46 is a cellular receptor for human herpesvirus 6.";
RL   Cell 99:817-827(1999).
RN   [29]
RP   PHOSPHORYLATION AT TYR-384 (ISOFORM B), PHOSPHORYLATION AT TYR-369 (ISOFORM
RP   D), PHOSPHORYLATION AT TYR-354 (ISOFORM F), PHOSPHORYLATION AT TYR-370
RP   (ISOFORM H), PHOSPHORYLATION AT TYR-355 (ISOFORM J), PHOSPHORYLATION AT
RP   TYR-340 (ISOFORM L), AND PHOSPHORYLATION AT TYR-321 (ISOFORM 3).
RX   PubMed=10657632; DOI=10.4049/jimmunol.164.4.1839;
RA   Wang G., Liszewski M.K., Chan A.C., Atkinson J.P.;
RT   "Membrane cofactor protein (MCP; CD46): isoform-specific tyrosine
RT   phosphorylation.";
RL   J. Immunol. 164:1839-1846(2000).
RN   [30]
RP   FUNCTION.
RX   PubMed=10843656; DOI=10.4049/jimmunol.164.12.6091;
RA   Astier A., Trescol-Biemont M.-C., Azocar O., Lamouille B.,
RA   Rabourdin-Combe C.;
RT   "CD46, a new costimulatory molecule for T cells, that induces p120CBL and
RT   LAT phosphorylation.";
RL   J. Immunol. 164:6091-6095(2000).
RN   [31]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MEASLES VIRUS H
RP   PROTEIN.
RX   PubMed=10972291; DOI=10.1038/35022579;
RA   Tatsuo H., Ono N., Tanaka K., Yanagi Y.;
RT   "SLAM (CDw150) is a cellular receptor for measles virus.";
RL   Nature 406:893-897(2000).
RN   [32]
RP   FUNCTION (MICROBIAL INFECTION), INTERACTION WITH NEISSERIA TYPE IV PILI,
RP   AND MUTAGENESIS OF ASN-83; ASN-114 AND ASN-273.
RX   PubMed=11260136; DOI=10.1046/j.1462-5822.2001.00095.x;
RA   Kaellstroem H., Blackmer Gill D., Albiger B., Liszewski M.K.,
RA   Atkinson J.P., Jonsson A.-B.;
RT   "Attachment of Neisseria gonorrhoeae to the cellular pilus receptor CD46:
RT   identification of domains important for bacterial adherence.";
RL   Cell. Microbiol. 3:133-143(2001).
RN   [33]
RP   BINDING OF HUMAN HERPESVIRUS 6.
RX   PubMed=12171934; DOI=10.1074/jbc.m206488200;
RA   Greenstone H.L., Santoro F., Lusso P., Berger E.A.;
RT   "Human Herpesvirus 6 and Measles Virus employ distinct CD46 domains for
RT   receptor function.";
RL   J. Biol. Chem. 277:39112-39118(2002).
RN   [34]
RP   PHOSPHORYLATION (ISOFORMS B/D/F/H/J/L/3).
RX   PubMed=11901164; DOI=10.1083/jcb.200109005;
RA   Lee S.W., Bonnah R.A., Higashi D.L., Atkinson J.P., Milgram S.L., So M.;
RT   "CD46 is phosphorylated at tyrosine 354 upon infection of epithelial cells
RT   by Neisseria gonorrhoeae.";
RL   J. Cell Biol. 156:951-957(2002).
RN   [35]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH STREPTOCOCCUS PYOGENES
RP   M PROTEIN.
RX   PubMed=11971006; DOI=10.4049/jimmunol.168.9.4585;
RA   Giannakis E., Jokiranta T.S., Ormsby R.J., Duthy T.G., Male D.A.,
RA   Christiansen D., Fischetti V.A., Bagley C., Loveland B.E., Gordon D.L.;
RT   "Identification of the streptococcal M protein binding site on membrane
RT   cofactor protein (CD46).";
RL   J. Immunol. 168:4585-4592(2002).
RN   [36]
RP   SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX   PubMed=12112588; DOI=10.1002/mrd.10144;
RA   Riley R.C., Kemper C., Leung M., Atkinson J.P.;
RT   "Characterization of human membrane cofactor protein (MCP; CD46) on
RT   spermatozoa.";
RL   Mol. Reprod. Dev. 62:534-546(2002).
RN   [37]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN HERPESVIRUS 6 GH
RP   PROTEIN.
RX   PubMed=12724329; DOI=10.1074/jbc.m302373200;
RA   Santoro F., Greenstone H.L., Insinga A., Liszewski M.K., Atkinson J.P.,
RA   Lusso P., Berger E.A.;
RT   "Interaction of glycoprotein H of human herpesvirus 6 with the cellular
RT   receptor CD46.";
RL   J. Biol. Chem. 278:25964-25969(2003).
RN   [38]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14597734; DOI=10.1084/jem.20031159;
RA   Gill D.B., Koomey M., Cannon J.G., Atkinson J.P.;
RT   "Down-regulation of CD46 by piliated Neisseria gonorrhoeae.";
RL   J. Exp. Med. 198:1313-1322(2003).
RN   [39]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN HERPESVIRUS 6 GH
RP   PROTEIN.
RX   PubMed=12663806; DOI=10.1128/jvi.77.8.4992-4999.2003;
RA   Mori Y., Yang X., Akkapaiboon P., Okuno T., Yamanishi K.;
RT   "Human herpesvirus 6 variant A glycoprotein H-glycoprotein L-glycoprotein Q
RT   complex associates with human CD46.";
RL   J. Virol. 77:4992-4999(2003).
RN   [40]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ADENOVIRUS B
RP   FIBER PROTEIN.
RX   PubMed=12915534; DOI=10.1128/jvi.77.17.9183-9191.2003;
RA   Segerman A., Atkinson J.P., Marttila M., Dennerquist V., Wadell G.,
RA   Arnberg N.;
RT   "Adenovirus type 11 uses CD46 as a cellular receptor.";
RL   J. Virol. 77:9183-9191(2003).
RN   [41]
RP   DISEASE.
RX   PubMed=14615110; DOI=10.1016/s0140-6736(03)14742-3;
RA   Noris M., Brioschi S., Caprioli J., Todeschini M., Bresin E., Porrati F.,
RA   Gamba S., Remuzzi G.;
RT   "Familial haemolytic uraemic syndrome and an MCP mutation.";
RL   Lancet 362:1542-1547(2003).
RN   [42]
RP   FUNCTION.
RX   PubMed=12540904; DOI=10.1038/nature01315;
RA   Kemper C., Chan A.C., Green J.M., Brett K.A., Murphy K.M., Atkinson J.P.;
RT   "Activation of human CD4+ cells with CD3 and CD46 induces a T-regulatory
RT   cell 1 phenotype.";
RL   Nature 421:388-392(2003).
RN   [43]
RP   FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HUMAN ADENOVIRUS B FIBER
RP   PROTEIN, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14566335; DOI=10.1038/nm952;
RA   Gaggar A., Shayakhmetov D.M., Lieber A.;
RT   "CD46 is a cellular receptor for group B adenoviruses.";
RL   Nat. Med. 9:1408-1412(2003).
RN   [44]
RP   GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=15307194; DOI=10.1002/eji.200424969;
RA   Hakulinen J., Junnikkala S., Sorsa T., Meri S.;
RT   "Complement inhibitor membrane cofactor protein (MCP; CD46) is
RT   constitutively shed from cancer cell membranes in vesicles and converted by
RT   a metalloproteinase to a functionally active soluble form.";
RL   Eur. J. Immunol. 34:2620-2629(2004).
RN   [45]
RP   FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HUMAN ADENOVIRUS D TYPE 37
RP   PIV/FIBER PROTEIN, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15047806; DOI=10.1128/jvi.78.8.3897-3905.2004;
RA   Wu E., Trauger S.A., Pache L., Mullen T.-M., von Seggern D.J., Siuzdak G.,
RA   Nemerow G.R.;
RT   "Membrane cofactor protein is a receptor for adenoviruses associated with
RT   epidemic keratoconjunctivitis.";
RL   J. Virol. 78:3897-3905(2004).
RN   [46]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ADENOVIRUS B
RP   TYPE 3 FIBER PROTEIN.
RX   PubMed=15078926; DOI=10.1128/jvi.78.9.4454-4462.2004;
RA   Sirena D., Lilienfeld B., Eisenhut M., Kaelin S., Boucke K., Beerli R.R.,
RA   Vogt L., Ruedl C., Bachmann M.F., Greber U.F., Hemmi S.;
RT   "The human membrane cofactor CD46 is a receptor for species B adenovirus
RT   serotype 3.";
RL   J. Virol. 78:4454-4462(2004).
RN   [47]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ADENOVIRUS B
RP   TYPE 35 FIBER PROTEIN.
RX   PubMed=15919905; DOI=10.1128/jvi.79.12.7503-7513.2005;
RA   Gaggar A., Shayakhmetov D.M., Liszewski M.K., Atkinson J.P., Lieber A.;
RT   "Localization of regions in CD46 that interact with adenovirus.";
RL   J. Virol. 79:7503-7513(2005).
RN   [48]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN ADENOVIRUS B
RP   FIBER PROTEIN.
RX   PubMed=16254377; DOI=10.1128/jvi.79.22.14429-14436.2005;
RA   Marttila M., Persson D., Gustafsson D., Liszewski M.K., Atkinson J.P.,
RA   Wadell G., Arnberg N.;
RT   "CD46 is a cellular receptor for all species B adenoviruses except types 3
RT   and 7.";
RL   J. Virol. 79:14429-14436(2005).
RN   [49]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [50]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 35-160.
RX   PubMed=10357804; DOI=10.1093/emboj/18.11.2911;
RA   Casasnovas J.M., Larvie M., Stehle T.;
RT   "Crystal structure of two CD46 domains reveals an extended measles virus-
RT   binding surface.";
RL   EMBO J. 18:2911-2922(1999).
RN   [51]
RP   CHARACTERIZATION OF VARIANTS AHUS2 PRO-240 AND 271-ASP-SER-272 DEL.
RX   PubMed=14566051; DOI=10.1073/pnas.2135497100;
RA   Richards A., Kemp E.J., Liszewski M.K., Goodship J.A., Lampe A.K.,
RA   Decorte R., Muesluemanoglu M.H., Kavukcu S., Filler G., Pirson Y.,
RA   Wen L.S., Atkinson J.P., Goodship T.H.J.;
RT   "Mutations in human complement regulator, membrane cofactor protein (CD46),
RT   predispose to development of familial hemolytic uremic syndrome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12966-12971(2003).
RN   [52]
RP   VARIANT AHUS2 TYR-35.
RX   PubMed=16621965; DOI=10.1182/blood-2005-10-007252;
RG   The international registry of recurrent and familial HUS/TTP;
RA   Caprioli J., Noris M., Brioschi S., Pianetti G., Castelletti F.,
RA   Bettinaglio P., Mele C., Bresin E., Cassis L., Gamba S., Porrati F.,
RA   Bucchioni S., Monteferrante G., Fang C.J., Liszewski M.K., Kavanagh D.,
RA   Atkinson J.P., Remuzzi G.;
RT   "Genetics of HUS: the impact of MCP, CFH, and IF mutations on clinical
RT   presentation, response to treatment, and outcome.";
RL   Blood 108:1267-1279(2006).
RN   [53]
RP   VARIANT AHUS2 SER-165.
RX   PubMed=16386793; DOI=10.1016/j.molimm.2005.11.008;
RA   Esparza-Gordillo J., Jorge E.G., Garrido C.A., Carreras L.,
RA   Lopez-Trascasa M., Sanchez-Corral P., de Cordoba S.R.;
RT   "Insights into hemolytic uremic syndrome: segregation of three independent
RT   predisposition factors in a large, multiple affected pedigree.";
RL   Mol. Immunol. 43:1769-1775(2006).
RN   [54]
RP   VARIANTS [LARGE SCALE ANALYSIS] TYR-228 AND VAL-353.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [55]
RP   VARIANTS AHUS2 CYS-216 AND ARG-231.
RX   PubMed=20513133; DOI=10.1002/humu.21256;
RA   Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.;
RT   "Mutations in alternative pathway complement proteins in American patients
RT   with atypical hemolytic uremic syndrome.";
RL   Hum. Mutat. 31:E1445-E1460(2010).
CC   -!- FUNCTION: Acts as a cofactor for complement factor I, a serine protease
CC       which protects autologous cells against complement-mediated injury by
CC       cleaving C3b and C4b deposited on host tissue. May be involved in the
CC       fusion of the spermatozoa with the oocyte during fertilization. Also
CC       acts as a costimulatory factor for T-cells which induces the
CC       differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells
CC       suppress immune responses by secreting interleukin-10, and therefore
CC       are thought to prevent autoimmunity. {ECO:0000269|PubMed:10843656,
CC       ECO:0000269|PubMed:12540904}.
CC   -!- FUNCTION: (Microbial infection) A number of viral and bacterial
CC       pathogens seem to bind MCP in order to exploit its immune regulation
CC       property and directly induce an immunosuppressive phenotype in T-cells.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for Adenovirus
CC       subgroup B2 and Ad3. {ECO:0000269|PubMed:12915534,
CC       ECO:0000269|PubMed:14566335, ECO:0000269|PubMed:15047806,
CC       ECO:0000269|PubMed:15078926, ECO:0000269|PubMed:15919905,
CC       ECO:0000269|PubMed:16254377}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for cultured Measles
CC       virus. {ECO:0000269|PubMed:10972291}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for Herpesvirus
CC       6/HHV-6. {ECO:0000269|PubMed:12663806, ECO:0000269|PubMed:12724329}.
CC   -!- FUNCTION: (Microbial infection) May act as a receptor for pathogenic
CC       bacteria Neisseria and Streptococcus pyogenes (PubMed:7708671,
CC       PubMed:9379894, PubMed:11260136, PubMed:11971006).
CC   -!- SUBUNIT: Interacts with C3b (PubMed:3260937, PubMed:1717583). Interacts
CC       with C4b (PubMed:1717583). Interacts with moesin/MSN (PubMed:7884872).
CC       {ECO:0000269|PubMed:1717583, ECO:0000269|PubMed:3260937,
CC       ECO:0000269|PubMed:7884872}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with measles virus H protein.
CC       {ECO:0000269|PubMed:10972291}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human herpesvirus 6 GH
CC       protein (PubMed:12663806, PubMed:12724329).
CC       {ECO:0000269|PubMed:12663806, ECO:0000269|PubMed:12724329}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus B/D
CC       fiber protein (PubMed:12915534, PubMed:14566335, PubMed:15047806,
CC       PubMed:15078926, PubMed:15919905, PubMed:16254377).
CC       {ECO:0000269|PubMed:12915534, ECO:0000269|PubMed:14566335,
CC       ECO:0000269|PubMed:15047806, ECO:0000269|PubMed:15078926,
CC       ECO:0000269|PubMed:15919905, ECO:0000269|PubMed:16254377}.
CC   -!- SUBUNIT: (Microbial infection) Binds to Streptococcus pyogenes M
CC       protein and to type IV pili from Neisseria (PubMed:7708671,
CC       PubMed:9379894, PubMed:11260136, PubMed:11971006).
CC       {ECO:0000269|PubMed:11260136, ECO:0000269|PubMed:11971006,
CC       ECO:0000269|PubMed:7708671, ECO:0000269|PubMed:9379894}.
CC   -!- INTERACTION:
CC       P15529; P01024: C3; NbExp=2; IntAct=EBI-2623451, EBI-905851;
CC       P15529; P78504: JAG1; NbExp=5; IntAct=EBI-2623451, EBI-2847071;
CC       P15529-3; Q8TD06: AGR3; NbExp=3; IntAct=EBI-13046140, EBI-3925742;
CC       P15529-3; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-13046140, EBI-12109402;
CC       P15529-3; O60883: GPR37L1; NbExp=3; IntAct=EBI-13046140, EBI-2927498;
CC       P15529-3; Q12837: POU4F2; NbExp=3; IntAct=EBI-13046140, EBI-17236143;
CC       P15529-3; Q9UEU0: VTI1B; NbExp=3; IntAct=EBI-13046140, EBI-723716;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC       inner membrane {ECO:0000269|PubMed:12112588,
CC       ECO:0000269|PubMed:14597734, ECO:0000269|PubMed:15307194}; Single-pass
CC       type I membrane protein {ECO:0000269|PubMed:12112588,
CC       ECO:0000269|PubMed:14597734, ECO:0000269|PubMed:15307194}. Note=Inner
CC       acrosomal membrane of spermatozoa. Internalized upon binding of Measles
CC       virus, Herpesvirus 6 or Neisseria gonorrhoeae, which results in an
CC       increased susceptibility of infected cells to complement-mediated
CC       injury. In cancer cells or cells infected by Neisseria, shedding leads
CC       to a soluble peptide.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=16;
CC         Comment=Additional isoforms seem to exist. The complete sequences of
CC         the isoforms are not known. Isoforms are classified as alpha (isoform
CC         C and isoform D), beta (isoform E and isoform F), gamma (isoform A
CC         and isoform B) and delta (isoform N). Isoforms gamma are
CC         preferentially expressed in EBV-B cells and leukemic cells. Isoforms
CC         alpha (66 kDa) and isoforms beta (56 kDa) are found in all tissues
CC         except sperm. Isoform delta is expressed in spermatozoa. The exon 9
CC         is specifically deleted in some placentae isoforms. All tissues
CC         differentially splice exon 13.;
CC       Name=A; Synonyms=no del, ABC1;
CC         IsoId=P15529-1; Sequence=Displayed;
CC       Name=B; Synonyms=del 13, ABC2;
CC         IsoId=P15529-2; Sequence=VSP_001204;
CC       Name=C; Synonyms=del 7, BC1;
CC         IsoId=P15529-11; Sequence=VSP_009174;
CC       Name=D; Synonyms=del 7-13, BC2;
CC         IsoId=P15529-3; Sequence=VSP_009174, VSP_001204;
CC       Name=E; Synonyms=del 7-8, C1;
CC         IsoId=P15529-12; Sequence=VSP_009175;
CC       Name=F; Synonyms=del 7-8-13, C2;
CC         IsoId=P15529-4; Sequence=VSP_009175, VSP_001204;
CC       Name=G; Synonyms=del 9;
CC         IsoId=P15529-13; Sequence=VSP_009177;
CC       Name=H; Synonyms=del 9-13;
CC         IsoId=P15529-5; Sequence=VSP_009177, VSP_001204;
CC       Name=I; Synonyms=del 7-9;
CC         IsoId=P15529-14; Sequence=VSP_009174, VSP_009177;
CC       Name=J; Synonyms=del 7-9-13;
CC         IsoId=P15529-6; Sequence=VSP_009174, VSP_009177, VSP_001204;
CC       Name=K; Synonyms=del 7-8-9;
CC         IsoId=P15529-15; Sequence=VSP_009176;
CC       Name=L; Synonyms=del 7-8-9-13;
CC         IsoId=P15529-7; Sequence=VSP_009176, VSP_001204;
CC       Name=M; Synonyms=del 7-12a-13;
CC         IsoId=P15529-8; Sequence=VSP_009174, VSP_001202, VSP_001203;
CC       Name=N; Synonyms=del 7-8-12-13;
CC         IsoId=P15529-9; Sequence=VSP_009175, VSP_009178;
CC       Name=2;
CC         IsoId=P15529-10; Sequence=VSP_001201;
CC       Name=3;
CC         IsoId=P15529-16; Sequence=VSP_019005, VSP_019006, VSP_001204;
CC   -!- TISSUE SPECIFICITY: Expressed by all cells except erythrocytes.
CC   -!- DOMAIN: Sushi domains 1 and 2 are required for interaction with human
CC       adenovirus B PIV/FIBER protein and with Measles virus H protein. Sushi
CC       domains 2 and 3 are required for Herpesvirus 6 binding. Sushi domain 3
CC       is required for Neisseria binding. Sushi domains 3 and 4 are required
CC       for interaction with Streptococcus pyogenes M protein and are the most
CC       important for interaction with C3b and C4b.
CC   -!- PTM: N-glycosylated on Asn-83; Asn-114 and Asn-273 in most tissues, but
CC       probably less N-glycosylated in testis. N-glycosylation on Asn-114 and
CC       Asn-273 is required for cytoprotective function. N-glycosylation on
CC       Asn-114 is required for Measles virus binding. N-glycosylation on Asn-
CC       273 is required for Neisseria binding. N-glycosylation is not required
CC       for human adenovirus binding.
CC   -!- PTM: Extensively O-glycosylated in the Ser/Thr-rich domain. O-
CC       glycosylation is required for Neisseria binding but not for Measles
CC       virus or human adenovirus binding.
CC   -!- PTM: In epithelial cells, isoforms B/D/F/H/J/L/3 are phosphorylated by
CC       YES1 in response to infection by Neisseria gonorrhoeae; which promotes
CC       infectivity. In T-cells, these isoforms may be phosphorylated by LCK.
CC   -!- DISEASE: Hemolytic uremic syndrome atypical 2 (AHUS2) [MIM:612922]: An
CC       atypical form of hemolytic uremic syndrome. It is a complex genetic
CC       disease characterized by microangiopathic hemolytic anemia,
CC       thrombocytopenia, renal failure and absence of episodes of
CC       enterocolitis and diarrhea. In contrast to typical hemolytic uremic
CC       syndrome, atypical forms have a poorer prognosis, with higher death
CC       rates and frequent progression to end-stage renal disease.
CC       {ECO:0000269|PubMed:14566051, ECO:0000269|PubMed:16386793,
CC       ECO:0000269|PubMed:16621965, ECO:0000269|PubMed:20513133}. Note=Disease
CC       susceptibility is associated with variants affecting the gene
CC       represented in this entry. Other genes may play a role in modifying the
CC       phenotype. Patients with CD46 mutations seem to have an overall better
CC       prognosis compared to patients carrying CFH mutations.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/mcp/";
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DR   EMBL; Y00651; CAA68675.1; -; mRNA.
DR   EMBL; M58050; AAA62833.1; -; mRNA.
DR   EMBL; X59405; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; X59406; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; X59407; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; X59408; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; X59409; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; X59410; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; S51940; AAB24802.1; -; mRNA.
DR   EMBL; D84105; BAA12224.1; -; mRNA.
DR   EMBL; EF076055; ABK81635.1; -; mRNA.
DR   EMBL; EF076056; ABK81636.1; -; mRNA.
DR   EMBL; EF076057; ABK81637.1; -; mRNA.
DR   EMBL; EF076058; ABK81638.1; -; mRNA.
DR   EMBL; AK291227; BAF83916.1; -; mRNA.
DR   EMBL; BX537451; CAD97694.1; -; mRNA.
DR   EMBL; BX640613; CAE45719.1; -; mRNA.
DR   EMBL; BX649050; CAI45983.1; -; mRNA.
DR   EMBL; AK222822; BAD96542.1; -; mRNA.
DR   EMBL; AY916779; AAW82433.1; -; Genomic_DNA.
DR   EMBL; AL035209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL365178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471100; EAW93465.1; -; Genomic_DNA.
DR   EMBL; CH471100; EAW93470.1; -; Genomic_DNA.
DR   EMBL; CH471100; EAW93476.1; -; Genomic_DNA.
DR   EMBL; BC030594; AAH30594.1; -; mRNA.
DR   EMBL; AF209712; AAF73844.1; -; mRNA.
DR   EMBL; AF209713; AAF73845.1; -; mRNA.
DR   EMBL; AF209714; AAF73846.1; -; mRNA.
DR   EMBL; S65879; AAD13968.1; -; Genomic_DNA.
DR   CCDS; CCDS1479.1; -. [P15529-9]
DR   CCDS; CCDS1480.1; -. [P15529-3]
DR   CCDS; CCDS1481.1; -. [P15529-4]
DR   CCDS; CCDS1482.1; -. [P15529-2]
DR   CCDS; CCDS1484.1; -. [P15529-7]
DR   CCDS; CCDS1485.1; -. [P15529-1]
DR   CCDS; CCDS31008.1; -. [P15529-11]
DR   CCDS; CCDS31009.1; -. [P15529-12]
DR   CCDS; CCDS86048.1; -. [P15529-6]
DR   PIR; G02913; G02913.
DR   PIR; I54479; I54479.
DR   PIR; I57998; I57998.
DR   PIR; S01896; S01896.
DR   RefSeq; NP_002380.3; NM_002389.4. [P15529-1]
DR   RefSeq; NP_722548.1; NM_153826.3. [P15529-3]
DR   RefSeq; NP_758860.1; NM_172350.2. [P15529-9]
DR   RefSeq; NP_758861.1; NM_172351.2. [P15529-11]
DR   RefSeq; NP_758862.1; NM_172352.2. [P15529-12]
DR   RefSeq; NP_758863.1; NM_172353.2. [P15529-4]
DR   RefSeq; NP_758869.1; NM_172359.2. [P15529-2]
DR   RefSeq; NP_758871.1; NM_172361.2. [P15529-7]
DR   RefSeq; XP_011507865.1; XM_011509563.1. [P15529-5]
DR   RefSeq; XP_011507866.1; XM_011509564.1.
DR   RefSeq; XP_016856797.1; XM_017001308.1. [P15529-13]
DR   RefSeq; XP_016856798.1; XM_017001309.1.
DR   RefSeq; XP_016856799.1; XM_017001310.1.
DR   PDB; 1CKL; X-ray; 3.10 A; A/B/C/D/E/F=35-160.
DR   PDB; 1HR4; Model; -; A=159-284.
DR   PDB; 2O39; X-ray; 2.85 A; C/D=35-160.
DR   PDB; 3INB; X-ray; 3.10 A; C/D=35-160.
DR   PDB; 3L89; X-ray; 3.50 A; M/N/O/P/Q/R/S/T/U/V/W/X=35-160.
DR   PDB; 3O8E; X-ray; 2.84 A; B/D=35-286.
DR   PDB; 5FO8; X-ray; 2.40 A; C=35-286.
DR   PDBsum; 1CKL; -.
DR   PDBsum; 1HR4; -.
DR   PDBsum; 2O39; -.
DR   PDBsum; 3INB; -.
DR   PDBsum; 3L89; -.
DR   PDBsum; 3O8E; -.
DR   PDBsum; 5FO8; -.
DR   SMR; P15529; -.
DR   BioGRID; 110346; 22.
DR   DIP; DIP-41232N; -.
DR   IntAct; P15529; 18.
DR   STRING; 9606.ENSP00000313875; -.
DR   GlyConnect; 1501; 8 N-Linked glycans (2 sites).
DR   GlyGen; P15529; 21 sites.
DR   iPTMnet; P15529; -.
DR   PhosphoSitePlus; P15529; -.
DR   SwissPalm; P15529; -.
DR   BioMuta; CD46; -.
DR   DMDM; 41019474; -.
DR   EPD; P15529; -.
DR   jPOST; P15529; -.
DR   MassIVE; P15529; -.
DR   MaxQB; P15529; -.
DR   PaxDb; P15529; -.
DR   PeptideAtlas; P15529; -.
DR   PRIDE; P15529; -.
DR   ProteomicsDB; 53167; -. [P15529-1]
DR   ProteomicsDB; 53168; -. [P15529-10]
DR   ProteomicsDB; 53169; -. [P15529-11]
DR   ProteomicsDB; 53170; -. [P15529-12]
DR   ProteomicsDB; 53171; -. [P15529-13]
DR   ProteomicsDB; 53172; -. [P15529-14]
DR   ProteomicsDB; 53173; -. [P15529-15]
DR   ProteomicsDB; 53174; -. [P15529-16]
DR   ProteomicsDB; 53175; -. [P15529-2]
DR   ProteomicsDB; 53176; -. [P15529-3]
DR   ProteomicsDB; 53177; -. [P15529-4]
DR   ProteomicsDB; 53178; -. [P15529-5]
DR   ProteomicsDB; 53179; -. [P15529-6]
DR   ProteomicsDB; 53180; -. [P15529-7]
DR   ProteomicsDB; 53181; -. [P15529-8]
DR   ProteomicsDB; 53182; -. [P15529-9]
DR   TopDownProteomics; P15529-4; -. [P15529-4]
DR   ABCD; P15529; 8 sequenced antibodies.
DR   Antibodypedia; 2378; 1260 antibodies.
DR   DNASU; 4179; -.
DR   Ensembl; ENST00000322875; ENSP00000313875; ENSG00000117335. [P15529-2]
DR   Ensembl; ENST00000322918; ENSP00000314664; ENSG00000117335. [P15529-9]
DR   Ensembl; ENST00000354848; ENSP00000346912; ENSG00000117335. [P15529-3]
DR   Ensembl; ENST00000357714; ENSP00000350346; ENSG00000117335. [P15529-4]
DR   Ensembl; ENST00000358170; ENSP00000350893; ENSG00000117335. [P15529-1]
DR   Ensembl; ENST00000360212; ENSP00000353342; ENSG00000117335. [P15529-7]
DR   Ensembl; ENST00000367041; ENSP00000356008; ENSG00000117335. [P15529-12]
DR   Ensembl; ENST00000367042; ENSP00000356009; ENSG00000117335. [P15529-11]
DR   Ensembl; ENST00000367047; ENSP00000356014; ENSG00000117335. [P15529-16]
DR   Ensembl; ENST00000480003; ENSP00000418471; ENSG00000117335. [P15529-6]
DR   GeneID; 4179; -.
DR   KEGG; hsa:4179; -.
DR   UCSC; uc001hgc.4; human. [P15529-1]
DR   CTD; 4179; -.
DR   DisGeNET; 4179; -.
DR   GeneCards; CD46; -.
DR   GeneReviews; CD46; -.
DR   HGNC; HGNC:6953; CD46.
DR   HPA; ENSG00000117335; Low tissue specificity.
DR   MalaCards; CD46; -.
DR   MIM; 120920; gene+phenotype.
DR   MIM; 612922; phenotype.
DR   neXtProt; NX_P15529; -.
DR   OpenTargets; ENSG00000117335; -.
DR   Orphanet; 544472; Atypical hemolytic uremic syndrome with complement gene abnormality.
DR   Orphanet; 244242; HELLP syndrome.
DR   PharmGKB; PA30700; -.
DR   VEuPathDB; HostDB:ENSG00000117335.18; -.
DR   eggNOG; ENOG502QPUC; Eukaryota.
DR   GeneTree; ENSGT00940000161381; -.
DR   HOGENOM; CLU_020107_1_2_1; -.
DR   InParanoid; P15529; -.
DR   OMA; PPPFEAM; -.
DR   OrthoDB; 1239877at2759; -.
DR   PhylomeDB; P15529; -.
DR   TreeFam; TF334137; -.
DR   PathwayCommons; P15529; -.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   SIGNOR; P15529; -.
DR   BioGRID-ORCS; 4179; 26 hits in 997 CRISPR screens.
DR   ChiTaRS; CD46; human.
DR   EvolutionaryTrace; P15529; -.
DR   GeneWiki; CD46; -.
DR   GenomeRNAi; 4179; -.
DR   Pharos; P15529; Tbio.
DR   PRO; PR:P15529; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P15529; protein.
DR   Bgee; ENSG00000117335; Expressed in palpebral conjunctiva and 246 other tissues.
DR   ExpressionAtlas; P15529; baseline and differential.
DR   Genevisible; P15529; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0002079; C:inner acrosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR   GO; GO:0045296; F:cadherin binding; IPI:UniProtKB.
DR   GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0002250; P:adaptive immune response; IC:UniProtKB.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
DR   GO; GO:0043382; P:positive regulation of memory T cell differentiation; IDA:UniProtKB.
DR   GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IDA:UniProtKB.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
DR   GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IDA:UniProtKB.
DR   GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
DR   GO; GO:0008593; P:regulation of Notch signaling pathway; IDA:UniProtKB.
DR   GO; GO:0035581; P:sequestering of extracellular ligand from receptor; IDA:UniProtKB.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   GO; GO:0002456; P:T cell mediated immunity; IMP:UniProtKB.
DR   CDD; cd00033; CCP; 4.
DR   InterPro; IPR017341; CD46.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   Pfam; PF00084; Sushi; 4.
DR   PIRSF; PIRSF037971; TLX_CD46; 1.
DR   SMART; SM00032; CCP; 4.
DR   SUPFAM; SSF57535; SSF57535; 4.
DR   PROSITE; PS50923; SUSHI; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complement pathway;
KW   Cytoplasmic vesicle; Direct protein sequencing; Disease variant;
KW   Disulfide bond; Fertilization; Glycoprotein; Hemolytic uremic syndrome;
KW   Host cell receptor for virus entry; Host-virus interaction; Immunity;
KW   Innate immunity; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Sushi; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000269|PubMed:1479546,
FT                   ECO:0000269|PubMed:2298462, ECO:0000269|PubMed:3260937,
FT                   ECO:0000269|PubMed:8371352"
FT   CHAIN           35..392
FT                   /note="Membrane cofactor protein"
FT                   /id="PRO_0000006008"
FT   TOPO_DOM        35..343
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        367..392
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..96
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          97..159
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          160..225
FT                   /note="Sushi 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          226..285
FT                   /note="Sushi 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          291..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        163
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        290
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        298
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        300
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        64..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        99..141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        127..157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        162..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        191..223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        228..270
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        256..283
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   VAR_SEQ         33
FT                   /note="D -> G (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_019005"
FT   VAR_SEQ         34..96
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_019006"
FT   VAR_SEQ         286..329
FT                   /note="Missing (in isoform K and isoform L)"
FT                   /evidence="ECO:0000303|Ref.6"
FT                   /id="VSP_009176"
FT   VAR_SEQ         286..315
FT                   /note="Missing (in isoform E, isoform F and isoform N)"
FT                   /evidence="ECO:0000303|PubMed:1711570,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:8418811,
FT                   ECO:0000303|PubMed:9659228, ECO:0000303|Ref.6"
FT                   /id="VSP_009175"
FT   VAR_SEQ         286..300
FT                   /note="Missing (in isoform C, isoform D, isoform I, isoform
FT                   J and isoform M)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1711570,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:2050389,
FT                   ECO:0000303|PubMed:3260937, ECO:0000303|Ref.6"
FT                   /id="VSP_009174"
FT   VAR_SEQ         301..305
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001201"
FT   VAR_SEQ         316..329
FT                   /note="Missing (in isoform G, isoform H, isoform I and
FT                   isoform J)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_009177"
FT   VAR_SEQ         355..392
FT                   /note="VVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL -> GKQMVELNMP
FT                   LTRLNQPLQQSREAE (in isoform N)"
FT                   /evidence="ECO:0000303|PubMed:9659228"
FT                   /id="VSP_009178"
FT   VAR_SEQ         355..367
FT                   /note="Missing (in isoform M)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001202"
FT   VAR_SEQ         368..392
FT                   /note="YLQRRKKKGTYLTDETHREVKFTSL -> GKQMVELNMPLTRLNQPLQQSRE
FT                   AE (in isoform M)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001203"
FT   VAR_SEQ         377..392
FT                   /note="TYLTDETHREVKFTSL -> KADGGAEYATYQTKSTTPAEQRG (in
FT                   isoform B, isoform D, isoform F, isoform H, isoform J,
FT                   isoform L and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1711570,
FT                   ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:3260937,
FT                   ECO:0000303|PubMed:8418811, ECO:0000303|Ref.6,
FT                   ECO:0000303|Ref.9"
FT                   /id="VSP_001204"
FT   VARIANT         13
FT                   /note="S -> F (in dbSNP:rs138843816)"
FT                   /evidence="ECO:0000269|PubMed:10751138, ECO:0000269|Ref.9"
FT                   /id="VAR_026567"
FT   VARIANT         35
FT                   /note="C -> Y (in AHUS2; dbSNP:rs121909591)"
FT                   /evidence="ECO:0000269|PubMed:16621965"
FT                   /id="VAR_063656"
FT   VARIANT         59
FT                   /note="R -> Q (in dbSNP:rs780693519)"
FT                   /evidence="ECO:0000269|PubMed:10751138"
FT                   /id="VAR_026568"
FT   VARIANT         165
FT                   /note="P -> S (in AHUS2; reduced cell surface expression;
FT                   dbSNP:rs759136081)"
FT                   /evidence="ECO:0000269|PubMed:16386793"
FT                   /id="VAR_026569"
FT   VARIANT         216
FT                   /note="W -> C (in AHUS2)"
FT                   /evidence="ECO:0000269|PubMed:20513133"
FT                   /id="VAR_063657"
FT   VARIANT         228
FT                   /note="C -> Y (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035828"
FT   VARIANT         231
FT                   /note="P -> R (in AHUS2; dbSNP:rs1271761432)"
FT                   /evidence="ECO:0000269|PubMed:20513133"
FT                   /id="VAR_063658"
FT   VARIANT         240
FT                   /note="S -> P (in AHUS2; no change in cell surface
FT                   expression but reduced activity; dbSNP:rs121909589)"
FT                   /evidence="ECO:0000269|PubMed:14566051"
FT                   /id="VAR_026570"
FT   VARIANT         266
FT                   /note="D -> N (in dbSNP:rs17006830)"
FT                   /evidence="ECO:0000269|Ref.10"
FT                   /id="VAR_022262"
FT   VARIANT         271..272
FT                   /note="Missing (in AHUS2; no cell surface expression)"
FT                   /evidence="ECO:0000269|PubMed:14566051"
FT                   /id="VAR_026571"
FT   VARIANT         324
FT                   /note="P -> L (in dbSNP:rs41317833)"
FT                   /evidence="ECO:0000269|Ref.10"
FT                   /id="VAR_022263"
FT   VARIANT         353
FT                   /note="A -> V (in dbSNP:rs35366573)"
FT                   /evidence="ECO:0000269|PubMed:16959974, ECO:0000269|Ref.10"
FT                   /id="VAR_022264"
FT   VARIANT         355
FT                   /note="V -> G"
FT                   /evidence="ECO:0000269|Ref.10"
FT                   /id="VAR_022265"
FT   MUTAGEN         83
FT                   /note="N->Q: No effect on cytoprotective function. No
FT                   effect on Neisseria binding. No effect on Measles virus
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:11260136,
FT                   ECO:0000269|PubMed:8764003, ECO:0000269|PubMed:9759896"
FT   MUTAGEN         114
FT                   /note="N->Q: Strongly decreases cytoprotective function.
FT                   Decreases Neisseria binding. Abolishes Measles virus
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:11260136,
FT                   ECO:0000269|PubMed:8764003, ECO:0000269|PubMed:9759896"
FT   MUTAGEN         273
FT                   /note="N->Q: Strongly decreases cytoprotective function.
FT                   Abolishes Neisseria binding. No effect on Measles virus
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:11260136,
FT                   ECO:0000269|PubMed:8764003, ECO:0000269|PubMed:9759896"
FT   CONFLICT        25
FT                   /note="V -> A (in Ref. 8; CAE45719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="G -> S (in Ref. 8; CAD97694)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="K -> S (in Ref. 8; CAD97694)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="C -> R (in Ref. 8; CAI45983)"
FT                   /evidence="ECO:0000305"
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:3L89"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          108..112
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          122..127
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          131..135
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          137..146
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          156..159
FT                   /evidence="ECO:0007829|PDB:3O8E"
FT   STRAND          171..174
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          183..191
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          195..198
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          201..204
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          206..210
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          215..218
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          222..224
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          236..240
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          251..256
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          260..264
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          266..270
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          276..278
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   STRAND          282..285
FT                   /evidence="ECO:0007829|PDB:5FO8"
FT   MOD_RES         P15529-2:384
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:10657632"
FT   MOD_RES         P15529-3:369
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:10657632"
FT   MOD_RES         P15529-4:354
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:10657632"
FT   MOD_RES         P15529-5:370
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:10657632"
FT   MOD_RES         P15529-6:355
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:10657632"
FT   MOD_RES         P15529-7:340
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:10657632"
FT   MOD_RES         P15529-16:321
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:10657632"
SQ   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
//
DBGET integrated database retrieval system