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 27-MAR-2024, entry version 200. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 23. DR DIP; DIP-60629N; -. DR IntAct; Q9NNX6; 27. DR STRING; 9606.ENSP00000315477; -. DR BindingDB; Q9NNX6; -. DR ChEMBL; CHEMBL1795114; -. DR UniLectin; Q9NNX6; -. DR GlyCosmos; Q9NNX6; 1 site, No reported glycans. DR GlyGen; Q9NNX6; 1 site. DR iPTMnet; Q9NNX6; -. DR PhosphoSitePlus; Q9NNX6; -. DR SwissPalm; Q9NNX6; -. DR BioMuta; CD209; -. DR DMDM; 46396012; -. DR REPRODUCTION-2DPAGE; Q9NNX6; -. DR jPOST; Q9NNX6; -. DR MassIVE; Q9NNX6; -. DR PaxDb; 9606-ENSP00000315477; -. DR PeptideAtlas; 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; 1628 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 AGR; HGNC:1641; -. 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 OrthoDB; 3676313at2759; -. 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; 7 hits in 1147 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 130 other cell types or tissues. DR ExpressionAtlas; Q9NNX6; baseline and differential. 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:0016020; C:membrane; TAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0030246; F:carbohydrate binding; NAS:UniProtKB. 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:0006955; P:immune response; IBA:GO_Central. 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; Mannose-Binding Protein A, subunit A; 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 PANTHER; PTHR22802; C-TYPE LECTIN SUPERFAMILY MEMBER; 1. DR PANTHER; PTHR22802:SF197; CD209 ANTIGEN; 1. DR Pfam; PF00059; Lectin_C; 1. DR SMART; SM00034; CLECT; 1. DR SUPFAM; SSF56436; C-type lectin-like; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. DR Genevisible; Q9NNX6; HS. 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 //