MCP_HUMAN
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 03-AUG-2022, entry version 233.
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/";
CC ---------------------------------------------------------------------------
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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; 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; 2O39; -.
DR PDBsum; 3INB; -.
DR PDBsum; 3L89; -.
DR PDBsum; 3O8E; -.
DR PDBsum; 5FO8; -.
DR AlphaFoldDB; P15529; -.
DR SMR; P15529; -.
DR BioGRID; 110346; 29.
DR DIP; DIP-41232N; -.
DR IntAct; P15529; 20.
DR MINT; P15529; -.
DR STRING; 9606.ENSP00000313875; -.
DR GlyConnect; 1501; 8 N-Linked glycans (2 sites).
DR GlyGen; P15529; 22 sites, 7 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
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; 10 sequenced antibodies.
DR Antibodypedia; 2378; 1246 antibodies from 45 providers.
DR DNASU; 4179; -.
DR Ensembl; ENST00000322875.8; ENSP00000313875.4; ENSG00000117335.20. [P15529-2]
DR Ensembl; ENST00000322918.9; ENSP00000314664.5; ENSG00000117335.20. [P15529-9]
DR Ensembl; ENST00000354848.5; ENSP00000346912.1; ENSG00000117335.20. [P15529-3]
DR Ensembl; ENST00000357714.5; ENSP00000350346.1; ENSG00000117335.20. [P15529-4]
DR Ensembl; ENST00000358170.6; ENSP00000350893.2; ENSG00000117335.20. [P15529-1]
DR Ensembl; ENST00000360212.6; ENSP00000353342.2; ENSG00000117335.20. [P15529-7]
DR Ensembl; ENST00000367041.5; ENSP00000356008.1; ENSG00000117335.20. [P15529-12]
DR Ensembl; ENST00000367042.6; ENSP00000356009.1; ENSG00000117335.20. [P15529-11]
DR Ensembl; ENST00000367047.5; ENSP00000356014.1; ENSG00000117335.20. [P15529-16]
DR Ensembl; ENST00000480003.5; ENSP00000418471.1; ENSG00000117335.20. [P15529-6]
DR GeneID; 4179; -.
DR KEGG; hsa:4179; -.
DR MANE-Select; ENST00000367042.6; ENSP00000356009.1; NM_172351.3; NP_758861.1. [P15529-11]
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; -.
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 SignaLink; P15529; -.
DR SIGNOR; P15529; -.
DR BioGRID-ORCS; 4179; 31 hits in 1084 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 211 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:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central.
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: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
