CD209_HUMAN
ID CD209_HUMAN Reviewed; 404 AA.
AC Q9NNX6; A8KAM4; A8MVQ9; G5E9C4; Q2TB19; Q96QP7; Q96QP8; Q96QP9; Q96QQ0;
AC Q96QQ1; Q96QQ2; Q96QQ3; Q96QQ4; Q96QQ5; Q96QQ6; Q96QQ7; Q96QQ8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=CD209 antigen;
DE AltName: Full=C-type lectin domain family 4 member L;
DE AltName: Full=Dendritic cell-specific ICAM-3-grabbing non-integrin 1;
DE Short=DC-SIGN;
DE Short=DC-SIGN1;
DE AltName: CD_antigen=CD209;
GN Name=CD209; Synonyms=CLEC4L;
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 1), SUBCELLULAR LOCATION, FUNCTION
RP (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 GP120 (MICROBIAL
RP INFECTION).
RC TISSUE=Placenta;
RX PubMed=1518869; DOI=10.1073/pnas.89.17.8356;
RA Curtis B.M., Scharnowske S., Watson A.J.;
RT "Sequence and expression of a membrane-associated C-type lectin that
RT exhibits CD4-independent binding of human immunodeficiency virus envelope
RT glycoprotein gp 120.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8356-8360(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=10975799; DOI=10.4049/jimmunol.165.6.2937;
RA Soilleux E.J., Barten R., Trowsdale J.;
RT "DC-SIGN, a related gene, DC-SIGNR, and CD23 form a cluster on 19p13.";
RL J. Immunol. 165:2937-2942(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11257134; DOI=10.1084/jem.193.6.671;
RA Bashirova A.A., Geijtenbeek T.B.H., van Duijnhoven G.C.F., van Vliet S.J.,
RA Eilering J.B.G., Martin M.P., Wu L., Martin T.D., Viebig N., Knolle P.A.,
RA Kewalramani V.N., van Kooyk Y., Carrington M.;
RT "A dendritic cell-specific intercellular adhesion molecule 3-grabbing
RT nonintegrin (DC-SIGN)-related protein is highly expressed on human liver
RT sinusoidal endothelial cells and promotes HIV-1 infection.";
RL J. Exp. Med. 193:671-678(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10; 11 AND
RP 12), ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=11337487; DOI=10.1074/jbc.m009807200;
RA Mummidi S., Catano G., Lam L., Hoefle A., Telles V., Begum K., Jimenez F.,
RA Ahuja S.S., Ahuja S.K.;
RT "Extensive repertoire of membrane-bound and soluble dendritic cell-specific
RT ICAM-3-grabbing nonintegrin 1 (DC-SIGN1) and DC-SIGN2 isoforms. Inter-
RT individual variation in expression of DC-SIGN transcripts.";
RL J. Biol. Chem. 276:33196-33212(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
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 [9]
RP FUNCTION, AND INTERACTION WITH ICAM3.
RX PubMed=10721995; DOI=10.1016/s0092-8674(00)80694-7;
RA Geijtenbeek T.B.H., Kwon D.S., Torensma R., van Vliet S.J.,
RA van Duijnhoven G.C.F., Middel J., Cornelissen I.L., Nottet H.S.,
RA Kewalramani V.N., Littman D.R., Figdor C.G., van Kooyk Y.;
RT "DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances
RT trans-infection of T cells.";
RL Cell 100:587-597(2000).
RN [10]
RP FUNCTION, AND INTERACTION WITH ICAM2.
RX PubMed=11017109; DOI=10.1038/79815;
RA Geijtenbeek T.B.H., Krooshoop D.J., Bleijs D.A., van Vliet S.J.,
RA van Duijnhoven G.C.F., Grabovsky V., Alon R., Figdor C.G., van Kooyk Y.;
RT "DC-SIGN-ICAM-2 interaction mediates dendritic cell trafficking.";
RL Nat. Immunol. 1:353-357(2000).
RN [11]
RP SUBUNIT, AND LIGAND-BINDING.
RX PubMed=11384997; DOI=10.1074/jbc.m104565200;
RA Mitchell D.A., Fadden A.J., Drickamer K.;
RT "A novel mechanism of carbohydrate recognition by the C-type lectins DC-
RT SIGN and DC-SIGNR. Subunit organization and binding to multivalent
RT ligands.";
RL J. Biol. Chem. 276:28939-28945(2001).
RN [12]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH CYTOMEGALOVIRUS
RP GLYCOPROTEIN B (GB) (MICROBIAL INFECTION).
RX PubMed=12433371; DOI=10.1016/s1074-7613(02)00447-8;
RA Halary F., Amara A., Lortat-Jacob H., Messerle M., Delaunay T., Houles C.,
RA Fieschi F., Arenzana-Seisdedos F., Moreau J.-F., Dechanet-Merville J.;
RT "Human cytomegalovirus binding to DC-SIGN is required for dendritic cell
RT infection and target cell trans-infection.";
RL Immunity 17:653-664(2002).
RN [13]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH ICAM 3 AND HIV-1 GP120
RP (MICROBIAL INFECTION), AND MUTAGENESIS OF ASP-320; GLU-324; GLU-347;
RP ASN-349; ASN-350; ASP-355; ASN-365 AND ASP-366.
RX PubMed=11799126; DOI=10.1074/jbc.m111532200;
RA Geijtenbeek T.B.H., van Duijnhoven G.C.F., van Vliet S.J., Krieger E.,
RA Vriend G., Figdor C.G., van Kooyk Y.;
RT "Identification of different binding sites in the dendritic cell-specific
RT receptor DC-SIGN for intercellular adhesion molecule 3 and HIV-1.";
RL J. Biol. Chem. 277:11314-11320(2002).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF 14-LEU-LEU-15.
RX PubMed=11859097; DOI=10.4049/jimmunol.168.5.2118;
RA Engering A., Geijtenbeek T.B.H., van Vliet S.J., Wijers M., van Liempt E.,
RA Demaurex N., Lanzavecchia A., Fransen J., Figdor C.G., Piguet V.,
RA van Kooyk Y.;
RT "The dendritic cell-specific adhesion receptor DC-SIGN internalizes antigen
RT for presentation to T cells.";
RL J. Immunol. 168:2118-2126(2002).
RN [15]
RP ROLE IN HIV-1 INFECTION (MICROBIAL INFECTION).
RX PubMed=11825572; DOI=10.1016/s1074-7613(02)00259-5;
RA Kwon D.S., Gregorio G., Bitton N., Hendrickson W.A., Littman D.R.;
RT "DC-SIGN-mediated internalization of HIV is required for trans-enhancement
RT of T cell infection.";
RL Immunity 16:135-144(2002).
RN [16]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 GP120; HIV-2
RP GP120; SIV GP120 AND EBOLA GLYCOPROTEINS (MICROBIAL INFECTION).
RX PubMed=12502850; DOI=10.1128/jvi.77.2.1337-1346.2003;
RA Lin G., Simmons G., Poehlmann S., Baribaud F., Ni H., Leslie G.J.,
RA Haggarty B.S., Bates P., Weissman D., Hoxie J.A., Doms R.W.;
RT "Differential N-linked glycosylation of human immunodeficiency virus and
RT Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and
RT DC-SIGNR.";
RL J. Virol. 77:1337-1346(2003).
RN [17]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH DENGUE VIRUS ENVELOPE
RP E PROTEIN (MICROBIAL INFECTION).
RX PubMed=12682107; DOI=10.1084/jem.20021840;
RA Tassaneetrithep B., Burgess T.H., Granelli-Piperno A., Trumpfheller C.,
RA Finke J., Sun W., Eller M.A., Pattanapanyasat K., Sarasombath S.,
RA Birx D.L., Steinman R.M., Schlesinger S., Marovich M.A.;
RT "DC-SIGN (CD209) mediates dengue virus infection of human dendritic
RT cells.";
RL J. Exp. Med. 197:823-829(2003).
RN [18]
RP FUNCTION (MICROBIAL INFECTION) IN HIV-1 INFECTION.
RX PubMed=12692233; DOI=10.1128/jvi.77.9.5313-5323.2003;
RA Nobile C., Moris A., Porrot F., Sol-Foulon N., Schwartz O.;
RT "Inhibition of human immunodeficiency virus type 1 Env-mediated fusion by
RT DC-SIGN.";
RL J. Virol. 77:5313-5323(2003).
RN [19]
RP FUNCTION.
RX PubMed=12574325; DOI=10.4049/jimmunol.170.4.1635;
RA Appelmelk B.J., van Die I., van Vliet S.J., Vandenbroucke-Grauls C.M.,
RA Geijtenbeek T.B.H., van Kooyk Y.;
RT "Carbohydrate profiling identifies new pathogens that interact with
RT dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells.";
RL J. Immunol. 170:1635-1639(2003).
RN [20]
RP REVIEW ON ROLE IN HIV-1 INFECTION AND ON PATHOGEN BINDING (MICROBIAL
RP INFECTION).
RX PubMed=12949494; DOI=10.1038/nri1182;
RA van Kooyk Y., Geijtenbeek T.B.H.;
RT "DC-SIGN: escape mechanism for pathogens.";
RL Nat. Rev. Immunol. 3:697-709(2003).
RN [21]
RP REVIEW ON ROLE IN HIV-1 INFECTION (MICROBIAL INFECTION).
RX PubMed=12960229; DOI=10.1189/jlb.0503208;
RA Turville S., Wilkinson J., Cameron P., Dable J., Cunningham A.L.;
RT "The role of dendritic cell C-type lectin receptors in HIV pathogenesis.";
RL J. Leukoc. Biol. 74:710-718(2003).
RN [22]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EBOLAVIRUS
RP GLYCOPROTEIN (MICROBIAL INFECTION).
RX PubMed=12504546; DOI=10.1006/viro.2002.1730;
RA Simmons G., Reeves J.D., Grogan C.C., Vandenberghe L.H., Baribaud F.,
RA Whitbeck J.C., Burke E., Buchmeier M.J., Soilleux E.J., Riley J.L.,
RA Doms R.W., Bates P., Poehlmann S.;
RT "DC-SIGN and DC-SIGNR bind ebola glycoproteins and enhance infection of
RT macrophages and endothelial cells.";
RL Virology 305:115-123(2003).
RN [23]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HCV E2 GLYCOPROTEIN
RP (MICROBIAL INFECTION).
RX PubMed=15371595; DOI=10.1073/pnas.0405695101;
RA Cormier E.G., Durso R.J., Tsamis F., Boussemart L., Manix C., Olson W.C.,
RA Gardner J.P., Dragic T.;
RT "L-SIGN (CD209L) and DC-SIGN (CD209) mediate transinfection of liver cells
RT by hepatitis C virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14067-14072(2004).
RN [24]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH SARS-COV SPIKE
RP GLYCOPROTEIN (MICROBIAL INFECTION)V.
RX PubMed=15140961; DOI=10.1128/jvi.78.11.5642-5650.2004;
RA Yang Z.Y., Huang Y., Ganesh L., Leung K., Kong W.P., Schwartz O.,
RA Subbarao K., Nabel G.J.;
RT "pH-dependent entry of severe acute respiratory syndrome coronavirus is
RT mediated by the spike glycoprotein and enhanced by dendritic cell transfer
RT through DC-SIGN.";
RL J. Virol. 78:5642-5650(2004).
RN [25]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MARBURG VIRUS
RP GLYCOPROTEIN (MICROBIAL INFECTION).
RX PubMed=15479853; DOI=10.1128/jvi.78.21.12090-12095.2004;
RA Marzi A., Gramberg T., Simmons G., Moeller P., Rennekamp A.J.,
RA Krumbiegel M., Geier M., Eisemann J., Turza N., Saunier B.,
RA Steinkasserer A., Becker S., Bates P., Hofmann H., Poehlmann S.;
RT "DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and
RT the S protein of severe acute respiratory syndrome coronavirus.";
RL J. Virol. 78:12090-12095(2004).
RN [26]
RP INTERACTION WITH CEACAM1.
RX PubMed=16246332; DOI=10.1016/j.febslet.2005.09.089;
RA van Gisbergen K.P., Ludwig I.S., Geijtenbeek T.B., van Kooyk Y.;
RT "Interactions of DC-SIGN with Mac-1 and CEACAM1 regulate contact between
RT dendritic cells and neutrophils.";
RL FEBS Lett. 579:6159-6168(2005).
RN [27]
RP POLYMORPHISM, AND INVOLVEMENT IN SUSCEPTIBILITY TO DENGUE VIRUS INFECTION
RP (MICROBIAL INFECTION).
RX PubMed=15838506; DOI=10.1038/ng1550;
RA Sakuntabhai A., Turbpaiboon C., Casademont I., Chuansumrit A., Lowhnoo T.,
RA Kajaste-Rudnitski A., Kalayanarooj S.M., Tangnararatchakit K.,
RA Tangthawornchaikul N., Vasanawathana S., Chaiyaratana W.,
RA Yenchitsomanus P.T., Suriyaphol P., Avirutnan P., Chokephaibulkit K.,
RA Matsuda F., Yoksan S., Jacob Y., Lathrop G.M., Malasit P., Despres P.,
RA Julier C.;
RT "A variant in the CD209 promoter is associated with severity of dengue
RT disease.";
RL Nat. Genet. 37:507-513(2005).
RN [28]
RP FUNCTION (MICROBIAL INFECTION) BY M.TUBERCULOSIS.
RX PubMed=16092920; DOI=10.1042/bj20050709;
RA Pitarque S., Herrmann J.L., Duteyrat J.L., Jackson M., Stewart G.R.,
RA Lecointe F., Payre B., Schwartz O., Young D.B., Marchal G., Lagrange P.H.,
RA Puzo G., Gicquel B., Nigou J., Neyrolles O.;
RT "Deciphering the molecular bases of Mycobacterium tuberculosis binding to
RT the lectin DC-SIGN reveals an underestimated complexity.";
RL Biochem. J. 392:615-624(2005).
RN [29]
RP FUNCTION (MICROBIAL INFECTION), AND INVOLVEMENT IN M.TUBERCULOSIS
RP SUSCEPTIBILITY (MICROBIAL INFECTION).
RX PubMed=16379498; DOI=10.1371/journal.pmed.0030020;
RA Barreiro L.B., Neyrolles O., Babb C.L., Tailleux L., Quach H.,
RA McElreavey K., Helden P.D., Hoal E.G., Gicquel B., Quintana-Murci L.;
RT "Promoter variation in the DC-SIGN-encoding gene CD209 is associated with
RT tuberculosis.";
RL PLoS Med. 3:230-235(2006).
RN [30]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MEASLES VIRUS
RP HEMAGGLUTININ (MICROBIAL INFECTION).
RX PubMed=16537615; DOI=10.1128/jvi.80.7.3477-3486.2006;
RA de Witte L., Abt M., Schneider-Schaulies S., van Kooyk Y.,
RA Geijtenbeek T.B.;
RT "Measles virus targets DC-SIGN to enhance dendritic cell infection.";
RL J. Virol. 80:3477-3486(2006).
RN [31]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH WEST-NILE VIRUS
RP ENVELOPE GLYCOPROTEIN (MICROBIAL INFECTION).
RX PubMed=16415006; DOI=10.1128/jvi.80.3.1290-1301.2006;
RA Davis C.W., Nguyen H.Y., Hanna S.L., Sanchez M.D., Doms R.W., Pierson T.C.;
RT "West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular
RT attachment and infection.";
RL J. Virol. 80:1290-1301(2006).
RN [32]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HEPATITIS C VIRUS E1
RP AND E2 PROTEINS (MICROBIAL INFECTION).
RX PubMed=16816373; DOI=10.2353/ajpath.2006.051191;
RA Lai W.K., Sun P.J., Zhang J., Jennings A., Lalor P.F., Hubscher S.,
RA McKeating J.A., Adams D.H.;
RT "Expression of DC-SIGN and DC-SIGNR on human sinusoidal endothelium: a role
RT for capturing hepatitis C virus particles.";
RL Am. J. Pathol. 169:200-208(2006).
RN [33]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH M.BOVIS PROTEINS
RP (MICROBIAL INFECTION).
RX PubMed=21203928; DOI=10.1007/s13238-010-0101-3;
RA Carroll M.V., Sim R.B., Bigi F., Jaekel A., Antrobus R., Mitchell D.A.;
RT "Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG.";
RL Protein Cell 1:859-870(2010).
RN [34]
RP INTERACTION WITH C1QBP.
RX PubMed=22700724; DOI=10.1182/blood-2011-07-369728;
RA Hosszu K.K., Valentino A., Vinayagasundaram U., Vinayagasundaram R.,
RA Joyce M.G., Ji Y., Peerschke E.I., Ghebrehiwet B.;
RT "DC-SIGN, C1q, and gC1qR form a trimolecular receptor complex on the
RT surface of monocyte-derived immature dendritic cells.";
RL Blood 120:1228-1236(2012).
RN [35]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HERPES SIMPLEX VIRUS
RP SURFACE PROTEINS (MICROBIAL INFECTION).
RX PubMed=18796707; DOI=10.1099/vir.0.2008/003129-0;
RA de Jong M.A., de Witte L., Bolmstedt A., van Kooyk Y., Geijtenbeek T.B.;
RT "Dendritic cells mediate herpes simplex virus infection and transmission
RT through the C-type lectin DC-SIGN.";
RL J. Gen. Virol. 89:2398-2409(2008).
RN [36]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH INFLUENZAVIRUS
RP HEMAGGLUTININ (MICROBIAL INFECTION).
RX PubMed=21191006; DOI=10.1128/jvi.01705-10;
RA Londrigan S.L., Turville S.G., Tate M.D., Deng Y.M., Brooks A.G.,
RA Reading P.C.;
RT "N-linked glycosylation facilitates sialic acid-independent attachment and
RT entry of influenza A viruses into cells expressing DC-SIGN or L-SIGN.";
RL J. Virol. 85:2990-3000(2011).
RN [37]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH RIFT FEVER VALLEY
RP VIRUS GLYCOPROTEIN G (MICROBIAL INFECTION).
RX PubMed=21767814; DOI=10.1016/j.chom.2011.06.007;
RA Lozach P.Y., Kuehbacher A., Meier R., Mancini R., Bitto D., Bouloy M.,
RA Helenius A.;
RT "DC-SIGN as a receptor for phleboviruses.";
RL Cell Host Microbe 10:75-88(2011).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 254-382 IN COMPLEX WITH
RP GLCNAC(2)-MAN(3) PENTASACCHARIDE.
RX PubMed=11739956; DOI=10.1126/science.1066371;
RA Feinberg H., Mitchell D.A., Drickamer K., Weis W.I.;
RT "Structural basis for selective recognition of oligosaccharides by DC-SIGN
RT and DC-SIGNR.";
RL Science 294:2163-2166(2001).
RN [39]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN CYTOMEGALOVIRUS
RP /HHV-5 SURFACE PROTEINS (MICROBIAL INFECTION).
RX PubMed=22496863; DOI=10.1371/journal.pone.0034795;
RA Haspot F., Lavault A., Sinzger C., Laib Sampaio K., Stierhof Y.D.,
RA Pilet P., Bressolette-Bodin C., Halary F.;
RT "Human cytomegalovirus entry into dendritic cells occurs via a
RT macropinocytosis-like pathway in a pH-independent and cholesterol-dependent
RT manner.";
RL PLoS ONE 7:E34795-E34795(2012).
RN [40]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH RESPIRATORY SYNCYTIAL
RP VIRUS GLYCOPROTEIN G (MICROBIAL INFECTION).
RX PubMed=22090124; DOI=10.1128/jvi.06096-11;
RA Johnson T.R., McLellan J.S., Graham B.S.;
RT "Respiratory syncytial virus glycoprotein G interacts with DC-SIGN and L-
RT SIGN to activate ERK1 and ERK2.";
RL J. Virol. 86:1339-1347(2012).
RN [41]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH JAPANESE ENCEPHALITIS
RP VIRUS E PROTEIN (MICROBIAL INFECTION).
RX PubMed=24623090; DOI=10.1007/s00705-014-2042-2;
RA Shimojima M., Takenouchi A., Shimoda H., Kimura N., Maeda K.;
RT "Distinct usage of three C-type lectins by Japanese encephalitis virus: DC-
RT SIGN, DC-SIGNR, and LSECtin.";
RL Arch. Virol. 159:2023-2031(2014).
RN [42]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH LASSA VIRUS
RP GLYCOPROTEIN (MICROBIAL INFECTION).
RX PubMed=23966408; DOI=10.1128/jvi.01893-13;
RA Goncalves A.R., Moraz M.L., Pasquato A., Helenius A., Lozach P.Y., Kunz S.;
RT "Role of DC-SIGN in Lassa virus entry into human dendritic cells.";
RL J. Virol. 87:11504-11515(2013).
RN [43]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=22440960; DOI=10.1016/j.coviro.2011.12.005;
RA Backovic M., Rey F.A.;
RT "Virus entry: old viruses, new receptors.";
RL Curr. Opin. Virol. 2:4-13(2012).
CC -!- FUNCTION: Pathogen-recognition receptor expressed on the surface of
CC immature dendritic cells (DCs) and involved in initiation of primary
CC immune response. Thought to mediate the endocytosis of pathogens which
CC are subsequently degraded in lysosomal compartments. The receptor
CC returns to the cell membrane surface and the pathogen-derived antigens
CC are presented to resting T-cells via MHC class II proteins to initiate
CC the adaptive immune response. {ECO:0000269|PubMed:11859097}.
CC -!- FUNCTION: On DCs it is a high affinity receptor for ICAM2 and ICAM3 by
CC binding to mannose-like carbohydrates. May act as a DC rolling receptor
CC that mediates transendothelial migration of DC presursors from blood to
CC tissues by binding endothelial ICAM2. Seems to regulate DC-induced T-
CC cell proliferation by binding to ICAM3 on T-cells in the immunological
CC synapse formed between DC and T-cells. {ECO:0000269|PubMed:10721995,
CC ECO:0000269|PubMed:11017109, ECO:0000269|PubMed:12574325}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for HIV-
CC 1 and HIV-2. {ECO:0000269|PubMed:11799126, ECO:0000269|PubMed:12502850,
CC ECO:0000269|PubMed:1518869}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
CC Ebolavirus. {ECO:0000269|PubMed:12502850, ECO:0000269|PubMed:12504546}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
CC Cytomegalovirus. {ECO:0000269|PubMed:12433371,
CC ECO:0000269|PubMed:22496863}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for HCV.
CC {ECO:0000269|PubMed:15371595, ECO:0000269|PubMed:16816373}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
CC Dengue virus. {ECO:0000269|PubMed:12682107}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
CC Measles virus. {ECO:0000269|PubMed:16537615}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
CC Herpes simplex virus 1. {ECO:0000269|PubMed:18796707}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
CC Influenzavirus A. {ECO:0000269|PubMed:21191006}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
CC SARS-CoV. {ECO:0000269|PubMed:15140961}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
CC Japanese encephalitis virus. {ECO:0000269|PubMed:24623090}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
CC Lassa virus (PubMed:23966408). Acts as an attachment receptor for
CC Marburg virusn. {ECO:0000269|PubMed:15479853}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
CC Respiratory syncytial virus. {ECO:0000269|PubMed:22090124}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for Rift
CC valley fever virus and uukuniemi virus. {ECO:0000269|PubMed:21767814}.
CC -!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
CC West-nile virus. {ECO:0000269|PubMed:16415006}.
CC -!- FUNCTION: (Microbial infection) Probably recognizes in a calcium-
CC dependent manner high mannose N-linked oligosaccharides in a variety of
CC bacterial pathogen antigens, including Leishmania pifanoi LPG, Lewis-x
CC antigen in Helicobacter pylori LPS, mannose in Klebsiella pneumonae
CC LPS, di-mannose and tri-mannose in Mycobacterium tuberculosis ManLAM
CC and Lewis-x antigen in Schistosoma mansoni SEA (PubMed:16379498).
CC Recognition of M.tuberculosis by dendritic cells occurs partially via
CC this molecule (PubMed:16092920, PubMed:21203928).
CC {ECO:0000269|PubMed:16092920, ECO:0000269|PubMed:16379498,
CC ECO:0000269|PubMed:21203928}.
CC -!- SUBUNIT: Homotetramer. Interacts with C1QBP; the interaction is
CC indicative for a C1q:C1QBP:CD209 signaling complex. Interacts with
CC ICAM2 and ICAM3 by binding to mannose-like carbohydrates. Interacts
CC (via C-type lectin domain) with CEACAM1 (via Lewis X moieties); this
CC interaction is regulated by the glycosylation pattern of CEACAM1 on
CC cell types and regulates contact between dendritic cells and
CC neutrophils (PubMed:16246332). {ECO:0000269|PubMed:10721995,
CC ECO:0000269|PubMed:11017109, ECO:0000269|PubMed:11384997,
CC ECO:0000269|PubMed:11739956, ECO:0000269|PubMed:16246332,
CC ECO:0000269|PubMed:22700724}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 and HIV-2 gp120
CC (PubMed:11799126, PubMed:12502850, PubMed:1518869).
CC {ECO:0000269|PubMed:11799126, ECO:0000269|PubMed:12502850,
CC ECO:0000269|PubMed:1518869}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus envelope
CC glycoproteins (PubMed:12502850, PubMed:12504546).
CC {ECO:0000269|PubMed:12502850, ECO:0000269|PubMed:12504546}.
CC -!- SUBUNIT: (Microbial infection) Interacts with cytomegalovirus gB
CC protein (PubMed:12433371, PubMed:22496863).
CC {ECO:0000269|PubMed:12433371, ECO:0000269|PubMed:22496863}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HCV E2 protein
CC (PubMed:15371595, PubMed:16816373). {ECO:0000269|PubMed:15371595,
CC ECO:0000269|PubMed:16816373}.
CC -!- SUBUNIT: (Microbial infection) Interacts with dengue virus major
CC envelope protein E. {ECO:0000269|PubMed:12682107}.
CC -!- SUBUNIT: (Microbial infection) Interacts with measles hemagglutinin.
CC {ECO:0000269|PubMed:16537615}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus 1
CC surface proteins. {ECO:0000269|PubMed:18796707}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Influenzavirus A
CC hemagglutinin. {ECO:0000269|PubMed:21191006}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV spike
CC glycoprotein. {ECO:0000269|PubMed:15140961}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Japanese encephalitis
CC virus E protein. {ECO:0000269|PubMed:24623090}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Lassa virus Glycoprotein.
CC {ECO:0000269|PubMed:23966408}.
CC -!- SUBUNIT: (Microbial infection) Interacts with marburg virus
CC glycoprotein. {ECO:0000269|PubMed:15479853}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Respiratory syncytial
CC virus glycoprotein G. {ECO:0000269|PubMed:22090124}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Rift valley fever virus
CC and uukuniemi virus envelope glycoprotein.
CC {ECO:0000269|PubMed:21767814}.
CC -!- SUBUNIT: (Microbial infection) Interacts with west-nile virus envelope
CC glycoprotein. {ECO:0000269|PubMed:16415006}.
CC -!- SUBUNIT: (Microbial infection) Interacts with whole M.bovis cells in a
CC Ca(2+)-dependent and independent manner; in vitro experiments suggest
CC it interacts with CH60.1 (groL1), DnaK, GADPH (gap) and LrpG
CC (PubMed:21203928). {ECO:0000269|PubMed:21203928}.
CC -!- INTERACTION:
CC Q9NNX6; Q08AM6: VAC14; NbExp=4; IntAct=EBI-9257341, EBI-2107455;
CC Q9NNX6; P0DTC2: S; Xeno; NbExp=12; IntAct=EBI-9257341, EBI-25474821;
CC Q9NNX6; PRO_0000278734 [Q03463]; Xeno; NbExp=2; IntAct=EBI-9257341, EBI-9257330;
CC Q9NNX6-10; Q86V38: ATN1; NbExp=3; IntAct=EBI-12300031, EBI-11954292;
CC Q9NNX6-10; P55212: CASP6; NbExp=3; IntAct=EBI-12300031, EBI-718729;
CC Q9NNX6-10; P02489: CRYAA; NbExp=3; IntAct=EBI-12300031, EBI-6875961;
CC Q9NNX6-10; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-12300031, EBI-12593112;
CC Q9NNX6-10; O14645: DNALI1; NbExp=3; IntAct=EBI-12300031, EBI-395638;
CC Q9NNX6-10; O75460-2: ERN1; NbExp=3; IntAct=EBI-12300031, EBI-25852368;
CC Q9NNX6-10; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-12300031, EBI-10226858;
CC Q9NNX6-10; P54652: HSPA2; NbExp=3; IntAct=EBI-12300031, EBI-356991;
CC Q9NNX6-10; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-12300031, EBI-9091197;
CC Q9NNX6-10; O14901: KLF11; NbExp=3; IntAct=EBI-12300031, EBI-948266;
CC Q9NNX6-10; P13473-2: LAMP2; NbExp=3; IntAct=EBI-12300031, EBI-21591415;
CC Q9NNX6-10; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-12300031, EBI-2811583;
CC Q9NNX6-10; D3DTS7: PMP22; NbExp=3; IntAct=EBI-12300031, EBI-25882629;
CC Q9NNX6-10; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-12300031, EBI-5280197;
CC Q9NNX6-10; P62826: RAN; NbExp=3; IntAct=EBI-12300031, EBI-286642;
CC Q9NNX6-10; P50502: ST13; NbExp=3; IntAct=EBI-12300031, EBI-357285;
CC Q9NNX6-10; Q8IYN2: TCEAL8; NbExp=3; IntAct=EBI-12300031, EBI-2116184;
CC Q9NNX6-10; Q08AM6: VAC14; NbExp=3; IntAct=EBI-12300031, EBI-2107455;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 9]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 10]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 11]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 12]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Comment=Additional isoforms seem to exist. Several splicing events
CC may be used independently in a modular way. Deletion of the
CC transmembrane domain encoding exon through alternative splicing
CC produces soluble isoforms. {ECO:0000269|PubMed:11337487};
CC Name=1; Synonyms=mDC-SIGN1A type I;
CC IsoId=Q9NNX6-1; Sequence=Displayed;
CC Name=2; Synonyms=mDC-SIGN1A type II;
CC IsoId=Q9NNX6-2; Sequence=VSP_010049;
CC Name=3; Synonyms=mDC-SIGN1A type III;
CC IsoId=Q9NNX6-3; Sequence=VSP_010044;
CC Name=4; Synonyms=mDC-SIGN1A type IV;
CC IsoId=Q9NNX6-4; Sequence=VSP_010042;
CC Name=5; Synonyms=mDC-SIGN1B type I;
CC IsoId=Q9NNX6-5; Sequence=VSP_010037;
CC Name=6; Synonyms=sDC-SIGN1A type I;
CC IsoId=Q9NNX6-6; Sequence=VSP_010041;
CC Name=7; Synonyms=sDC-SIGN1A type II;
CC IsoId=Q9NNX6-7; Sequence=VSP_010038;
CC Name=8; Synonyms=sDC-SIGN1A type III;
CC IsoId=Q9NNX6-8; Sequence=VSP_010038, VSP_010043;
CC Name=9; Synonyms=sDC-SIGN1A type IV;
CC IsoId=Q9NNX6-9; Sequence=VSP_010039, VSP_010040;
CC Name=10; Synonyms=sDC-SIGN1B type I;
CC IsoId=Q9NNX6-10; Sequence=VSP_010037, VSP_010041;
CC Name=11; Synonyms=sDC-SIGN1B type II;
CC IsoId=Q9NNX6-11; Sequence=VSP_010037, VSP_010041, VSP_010047;
CC Name=12; Synonyms=sDC-SIGN1B type III;
CC IsoId=Q9NNX6-12; Sequence=VSP_010037, VSP_010041, VSP_010048,
CC VSP_010050;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in dendritic cells and in
CC DC-residing tissues. Also found in placental macrophages, endothelial
CC cells of placental vascular channels, peripheral blood mononuclear
CC cells, and THP-1 monocytes. {ECO:0000269|PubMed:11257134,
CC ECO:0000269|PubMed:11337487}.
CC -!- DOMAIN: The tandem repeat domain, also called neck domain, mediates
CC oligomerization.
CC -!- POLYMORPHISM: Genetic variations in the CD209 promoter determine
CC M.tuberculosis susceptibility [MIM:607948] (PubMed:16379498).
CC {ECO:0000305|PubMed:16379498}.
CC -!- POLYMORPHISM: Genetic variations in CD209 may influence susceptibility
CC or resistance to dengue virus infection, as well as disease progression
CC and severity [MIM:614371]. A promoter polymorphism in the CD209 gene is
CC associated with protection from dengue fever, but not dengue
CC hemorrhagic fever.
CC -!- MISCELLANEOUS: In vitro, is a receptor for HIV-1 and transmits HIV-1
CC either in trans without DC infection, or in cis following a DC
CC infection to permissive T-cells to induce a robust infection. Bound
CC HIV-1 remains infectious over a prolonged period of time and it is
CC proposed that bound HIV-1 is not degraded but protected in non-
CC lysosomal acidic organelles within the DCs close to the cell membrane
CC thus contributing to the HIV-1 infectious potential during transport by
CC DCs from the periphery to lymphoid organs.
CC -!- MISCELLANEOUS: [Isoform 9]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK91858.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=DC-SIGN entry;
CC URL="https://en.wikipedia.org/wiki/DC-SIGN";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=DC-SIGN;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_00121";
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DR EMBL; M98457; AAF77072.1; -; mRNA.
DR EMBL; AF209479; AAG13814.1; -; Genomic_DNA.
DR EMBL; AF290886; AAK20997.1; -; mRNA.
DR EMBL; AY042221; AAK91846.1; -; mRNA.
DR EMBL; AY042222; AAK91847.1; -; mRNA.
DR EMBL; AY042223; AAK91848.1; -; mRNA.
DR EMBL; AY042224; AAK91849.1; -; mRNA.
DR EMBL; AY042225; AAK91850.1; -; mRNA.
DR EMBL; AY042226; AAK91851.1; -; mRNA.
DR EMBL; AY042227; AAK91852.1; -; mRNA.
DR EMBL; AY042228; AAK91853.1; -; mRNA.
DR EMBL; AY042229; AAK91854.1; -; mRNA.
DR EMBL; AY042230; AAK91855.1; -; mRNA.
DR EMBL; AY042231; AAK91856.1; -; mRNA.
DR EMBL; AY042232; AAK91857.1; -; mRNA.
DR EMBL; AY042233; AAK91858.1; ALT_SEQ; mRNA.
DR EMBL; AK293089; BAF85778.1; -; mRNA.
DR EMBL; AC008763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW68991.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW68993.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW68997.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW68998.1; -; Genomic_DNA.
DR EMBL; BC110615; AAI10616.1; -; mRNA.
DR CCDS; CCDS12186.1; -. [Q9NNX6-1]
DR CCDS; CCDS45949.1; -. [Q9NNX6-7]
DR CCDS; CCDS45950.1; -. [Q9NNX6-6]
DR CCDS; CCDS45951.1; -. [Q9NNX6-2]
DR CCDS; CCDS45952.1; -. [Q9NNX6-3]
DR CCDS; CCDS59344.1; -. [Q9NNX6-8]
DR PIR; A46274; A46274.
DR RefSeq; NP_001138365.1; NM_001144893.1.
DR RefSeq; NP_001138366.1; NM_001144894.1. [Q9NNX6-7]
DR RefSeq; NP_001138367.1; NM_001144895.1. [Q9NNX6-3]
DR RefSeq; NP_001138368.1; NM_001144896.1. [Q9NNX6-6]
DR RefSeq; NP_001138369.1; NM_001144897.1. [Q9NNX6-2]
DR RefSeq; NP_066978.1; NM_021155.3. [Q9NNX6-1]
DR PDB; 1K9I; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=250-404.
DR PDB; 1SL4; X-ray; 1.55 A; A=250-404.
DR PDB; 1SL5; X-ray; 1.80 A; A=250-388.
DR PDB; 2B6B; EM; 25.00 A; D=251-404.
DR PDB; 2IT5; X-ray; 2.40 A; A=250-388.
DR PDB; 2IT6; X-ray; 1.95 A; A=250-404.
DR PDB; 2XR5; X-ray; 1.42 A; A=254-404.
DR PDB; 2XR6; X-ray; 1.35 A; A=250-404.
DR PDB; 6GHV; X-ray; 2.10 A; A/B/C/D/E/F=250-404.
DR PDB; 7NL6; X-ray; 2.20 A; A=250-404.
DR PDB; 7NL7; X-ray; 2.10 A; A=250-404.
DR PDBsum; 1K9I; -.
DR PDBsum; 1SL4; -.
DR PDBsum; 1SL5; -.
DR PDBsum; 2B6B; -.
DR PDBsum; 2IT5; -.
DR PDBsum; 2IT6; -.
DR PDBsum; 2XR5; -.
DR PDBsum; 2XR6; -.
DR PDBsum; 6GHV; -.
DR PDBsum; 7NL6; -.
DR PDBsum; 7NL7; -.
DR AlphaFoldDB; Q9NNX6; -.
DR BMRB; Q9NNX6; -.
DR SMR; Q9NNX6; -.
DR BioGRID; 119051; 21.
DR DIP; DIP-60629N; -.
DR IntAct; Q9NNX6; 27.
DR STRING; 9606.ENSP00000315477; -.
DR BindingDB; Q9NNX6; -.
DR ChEMBL; CHEMBL1795114; -.
DR UniLectin; Q9NNX6; -.
DR GlyGen; Q9NNX6; 1 site.
DR iPTMnet; Q9NNX6; -.
DR PhosphoSitePlus; Q9NNX6; -.
DR BioMuta; CD209; -.
DR DMDM; 46396012; -.
DR REPRODUCTION-2DPAGE; Q9NNX6; -.
DR jPOST; Q9NNX6; -.
DR MassIVE; Q9NNX6; -.
DR PaxDb; Q9NNX6; -.
DR PeptideAtlas; Q9NNX6; -.
DR PRIDE; Q9NNX6; -.
DR ProteomicsDB; 33898; -.
DR ProteomicsDB; 81864; -. [Q9NNX6-1]
DR ProteomicsDB; 81865; -. [Q9NNX6-10]
DR ProteomicsDB; 81866; -. [Q9NNX6-11]
DR ProteomicsDB; 81867; -. [Q9NNX6-12]
DR ProteomicsDB; 81869; -. [Q9NNX6-2]
DR ProteomicsDB; 81870; -. [Q9NNX6-3]
DR ProteomicsDB; 81871; -. [Q9NNX6-4]
DR ProteomicsDB; 81872; -. [Q9NNX6-5]
DR ProteomicsDB; 81873; -. [Q9NNX6-6]
DR ProteomicsDB; 81874; -. [Q9NNX6-7]
DR ProteomicsDB; 81875; -. [Q9NNX6-8]
DR ProteomicsDB; 81876; -. [Q9NNX6-9]
DR ABCD; Q9NNX6; 23 sequenced antibodies.
DR Antibodypedia; 12203; 1524 antibodies from 45 providers.
DR DNASU; 30835; -.
DR Ensembl; ENST00000204801.12; ENSP00000204801.7; ENSG00000090659.18. [Q9NNX6-7]
DR Ensembl; ENST00000315591.12; ENSP00000315407.7; ENSG00000090659.18. [Q9NNX6-6]
DR Ensembl; ENST00000315599.12; ENSP00000315477.6; ENSG00000090659.18. [Q9NNX6-1]
DR Ensembl; ENST00000354397.10; ENSP00000346373.5; ENSG00000090659.18. [Q9NNX6-2]
DR Ensembl; ENST00000394161.9; ENSP00000377716.4; ENSG00000090659.18. [Q9NNX6-4]
DR Ensembl; ENST00000601256.1; ENSP00000470658.1; ENSG00000090659.18. [Q9NNX6-12]
DR Ensembl; ENST00000601951.5; ENSP00000468827.1; ENSG00000090659.18. [Q9NNX6-10]
DR Ensembl; ENST00000602261.5; ENSP00000471137.1; ENSG00000090659.18. [Q9NNX6-3]
DR GeneID; 30835; -.
DR KEGG; hsa:30835; -.
DR MANE-Select; ENST00000315599.12; ENSP00000315477.6; NM_021155.4; NP_066978.1.
DR UCSC; uc002mhr.3; human. [Q9NNX6-1]
DR CTD; 30835; -.
DR DisGeNET; 30835; -.
DR GeneCards; CD209; -.
DR HGNC; HGNC:1641; CD209.
DR HPA; ENSG00000090659; Tissue enhanced (adipose tissue, placenta).
DR MalaCards; CD209; -.
DR MIM; 604672; gene+phenotype.
DR MIM; 607948; phenotype.
DR MIM; 614371; phenotype.
DR neXtProt; NX_Q9NNX6; -.
DR OpenTargets; ENSG00000090659; -.
DR PharmGKB; PA26199; -.
DR VEuPathDB; HostDB:ENSG00000090659; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155012; -.
DR HOGENOM; CLU_1577990_0_0_1; -.
DR InParanoid; Q9NNX6; -.
DR OMA; VLMNSTC; -.
DR PhylomeDB; Q9NNX6; -.
DR TreeFam; TF333341; -.
DR PathwayCommons; Q9NNX6; -.
DR Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-HSA-8851680; Butyrophilin (BTN) family interactions.
DR SignaLink; Q9NNX6; -.
DR SIGNOR; Q9NNX6; -.
DR BioGRID-ORCS; 30835; 5 hits in 1071 CRISPR screens.
DR EvolutionaryTrace; Q9NNX6; -.
DR GeneWiki; DC-SIGN; -.
DR GenomeRNAi; 30835; -.
DR Pharos; Q9NNX6; Tchem.
DR PRO; PR:Q9NNX6; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NNX6; protein.
DR Bgee; ENSG00000090659; Expressed in lymph node and 129 other tissues.
DR ExpressionAtlas; Q9NNX6; baseline and differential.
DR Genevisible; Q9NNX6; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:CAFA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043657; C:host cell; IEA:GOC.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042605; F:peptide antigen binding; NAS:UniProtKB.
DR GO; GO:0046790; F:virion binding; TAS:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IDA:FlyBase.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019882; P:antigen processing and presentation; NAS:UniProtKB.
DR GO; GO:0097323; P:B cell adhesion; IDA:UniProtKB.
DR GO; GO:0009988; P:cell-cell recognition; TAS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0075733; P:intracellular transport of virus; TAS:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; NAS:UniProtKB.
DR GO; GO:0046968; P:peptide antigen transport; NAS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
DR GO; GO:1903902; P:positive regulation of viral life cycle; IMP:FlyBase.
DR GO; GO:0042129; P:regulation of T cell proliferation; IDA:MGI.
DR GO; GO:0046718; P:viral entry into host cell; IDA:FlyBase.
DR GO; GO:0019079; P:viral genome replication; NAS:UniProtKB.
DR GO; GO:0019062; P:virion attachment to host cell; TAS:UniProtKB.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Calcium;
KW Cell adhesion; Cell membrane; Disulfide bond; Endocytosis; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Immunity;
KW Innate immunity; Lectin; Mannose-binding; Membrane; Metal-binding;
KW Receptor; Reference proteome; Repeat; Secreted; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..404
FT /note="CD209 antigen"
FT /id="PRO_0000046595"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 59..404
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REPEAT 96..118
FT /note="1"
FT REPEAT 119..141
FT /note="2"
FT REPEAT 142..164
FT /note="3"
FT REPEAT 165..187
FT /note="4"
FT REPEAT 188..210
FT /note="5"
FT REPEAT 211..233
FT /note="6"
FT REPEAT 234..257
FT /note="7"
FT DOMAIN 263..378
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 96..257
FT /note="7 X approximate tandem repeats"
FT MOTIF 14..15
FT /note="Endocytosis signal"
FT MOTIF 16..18
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT MOTIF 31..34
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 256..267
FT DISULFID 284..377
FT DISULFID 356..369
FT VAR_SEQ 1..15
FT /note="MSDSKEPRLQQLGLL -> MASACPGSDFTSIHS (in isoform 5,
FT isoform 10, isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:11337487,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010037"
FT VAR_SEQ 16..59
FT /note="Missing (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:11337487"
FT /id="VSP_010038"
FT VAR_SEQ 30..34
FT /note="GYKSL -> RNQKC (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:11337487"
FT /id="VSP_010039"
FT VAR_SEQ 35..404
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:11337487"
FT /id="VSP_010040"
FT VAR_SEQ 36..59
FT /note="Missing (in isoform 6, isoform 10, isoform 11 and
FT isoform 12)"
FT /evidence="ECO:0000303|PubMed:11337487,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010041"
FT VAR_SEQ 74..309
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11337487"
FT /id="VSP_010042"
FT VAR_SEQ 142..233
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:11337487"
FT /id="VSP_010043"
FT VAR_SEQ 158..249
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11337487"
FT /id="VSP_010044"
FT VAR_SEQ 191..236
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:11337487"
FT /id="VSP_010047"
FT VAR_SEQ 301..321
FT /note="NFLQLQSSRSNRFTWMGLSDL -> LQAVLEQRRAQQRWGGRLRGI (in
FT isoform 12)"
FT /evidence="ECO:0000303|PubMed:11337487"
FT /id="VSP_010048"
FT VAR_SEQ 301..306
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11337487"
FT /id="VSP_010049"
FT VAR_SEQ 322..404
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:11337487"
FT /id="VSP_010050"
FT VARIANT 168
FT /note="E -> D (in dbSNP:rs1003686123)"
FT /id="VAR_050104"
FT VARIANT 214
FT /note="E -> D (in dbSNP:rs11465377)"
FT /id="VAR_036689"
FT VARIANT 242
FT /note="L -> V (in dbSNP:rs11465380)"
FT /id="VAR_036690"
FT VARIANT 382
FT /note="A -> S (in dbSNP:rs11465393)"
FT /id="VAR_050105"
FT MUTAGEN 14..15
FT /note="LL->AA: Loss of antigen internalization by
FT endocytosis."
FT /evidence="ECO:0000269|PubMed:11859097"
FT MUTAGEN 320
FT /note="D->A: Loss of binding to ICAM3 and HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:11799126"
FT MUTAGEN 324
FT /note="E->A: Loss of binding to ICAM3 and HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:11799126"
FT MUTAGEN 347
FT /note="E->Q: Loss of binding to ICAM3 and HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:11799126"
FT MUTAGEN 349
FT /note="N->D: Loss of binding to ICAM3 and HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:11799126"
FT MUTAGEN 350
FT /note="N->A: Loss of binding to ICAM3 and HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:11799126"
FT MUTAGEN 355
FT /note="D->A: Loss of binding to ICAM3 and HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:11799126"
FT MUTAGEN 365
FT /note="N->D: Loss of binding to ICAM3 and HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:11799126"
FT MUTAGEN 366
FT /note="D->A: Loss of binding to ICAM3 and HIV-1 gp120."
FT /evidence="ECO:0000269|PubMed:11799126"
FT CONFLICT 152
FT /note="W -> Q (in Ref. 4; AAK91848)"
FT /evidence="ECO:0000305"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:2XR6"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:2XR6"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:2XR6"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:2XR6"
FT STRAND 314..323
FT /evidence="ECO:0007829|PDB:2XR6"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:2XR6"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:2XR6"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:2XR6"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:2XR6"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:2XR6"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:2XR6"
SQ SEQUENCE 404 AA; 45775 MW; A23FA246014533C0 CRC64;
MSDSKEPRLQ QLGLLEEEQL RGLGFRQTRG YKSLAGCLGH GPLVLQLLSF TLLAGLLVQV
SKVPSSISQE QSRQDAIYQN LTQLKAAVGE LSEKSKLQEI YQELTQLKAA VGELPEKSKL
QEIYQELTRL KAAVGELPEK SKLQEIYQEL TWLKAAVGEL PEKSKMQEIY QELTRLKAAV
GELPEKSKQQ EIYQELTRLK AAVGELPEKS KQQEIYQELT RLKAAVGELP EKSKQQEIYQ
ELTQLKAAVE RLCHPCPWEW TFFQGNCYFM SNSQRNWHDS ITACKEVGAQ LVVIKSAEEQ
NFLQLQSSRS NRFTWMGLSD LNQEGTWQWV DGSPLLPSFK QYWNRGEPNN VGEEDCAEFS
GNGWNDDKCN LAKFWICKKS AASCSRDEEQ FLSPAPATPN PPPA
