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CD209 antigen (C-type lectin domain family 4 member L) (Dendritic cell-specific ICAM-3-grabbing non-integrin 1) (DC-SIGN) (DC-SIGN1) (CD antigen CD209)

 CD209_HUMAN             Reviewed;         404 AA.
Q9NNX6; A8KAM4; A8MVQ9; G5E9C4; Q2TB19; Q96QP7; Q96QP8; Q96QP9;
Q96QQ0; Q96QQ1; Q96QQ2; Q96QQ3; Q96QQ4; Q96QQ5; Q96QQ6; Q96QQ7;
Q96QQ8;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
23-MAY-2018, entry version 165.
RecName: Full=CD209 antigen;
AltName: Full=C-type lectin domain family 4 member L;
AltName: Full=Dendritic cell-specific ICAM-3-grabbing non-integrin 1;
Short=DC-SIGN;
Short=DC-SIGN1;
AltName: CD_antigen=CD209;
Name=CD209; Synonyms=CLEC4L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, FUNCTION
(MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 GP120.
TISSUE=Placenta;
PubMed=1518869; DOI=10.1073/pnas.89.17.8356;
Curtis B.M., Scharnowske S., Watson A.J.;
"Sequence and expression of a membrane-associated C-type lectin that
exhibits CD4-independent binding of human immunodeficiency virus
envelope glycoprotein gp 120.";
Proc. Natl. Acad. Sci. U.S.A. 89:8356-8360(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=10975799; DOI=10.4049/jimmunol.165.6.2937;
Soilleux E.J., Barten R., Trowsdale J.;
"DC-SIGN, a related gene, DC-SIGNR, and CD23 form a cluster on
19p13.";
J. Immunol. 165:2937-2942(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=11257134; DOI=10.1084/jem.193.6.671;
Bashirova A.A., Geijtenbeek T.B.H., van Duijnhoven G.C.F.,
van Vliet S.J., Eilering J.B.G., Martin M.P., Wu L., Martin T.D.,
Viebig N., Knolle P.A., Kewalramani V.N., van Kooyk Y., Carrington M.;
"A dendritic cell-specific intercellular adhesion molecule 3-grabbing
nonintegrin (DC-SIGN)-related protein is highly expressed on human
liver sinusoidal endothelial cells and promotes HIV-1 infection.";
J. Exp. Med. 193:671-678(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10; 11
AND 12), ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=11337487; DOI=10.1074/jbc.M009807200;
Mummidi S., Catano G., Lam L., Hoefle A., Telles V., Begum K.,
Jimenez F., Ahuja S.S., Ahuja S.K.;
"Extensive repertoire of membrane-bound and soluble dendritic cell-
specific ICAM-3-grabbing nonintegrin 1 (DC-SIGN1) and DC-SIGN2
isoforms. Inter-individual variation in expression of DC-SIGN
transcripts.";
J. Biol. Chem. 276:33196-33212(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, AND INTERACTION WITH ICAM3.
PubMed=10721995; DOI=10.1016/S0092-8674(00)80694-7;
Geijtenbeek T.B.H., Kwon D.S., Torensma R., van Vliet S.J.,
van Duijnhoven G.C.F., Middel J., Cornelissen I.L., Nottet H.S.,
Kewalramani V.N., Littman D.R., Figdor C.G., van Kooyk Y.;
"DC-SIGN, a dendritic cell-specific HIV-1-binding protein that
enhances trans-infection of T cells.";
Cell 100:587-597(2000).
[10]
FUNCTION, AND INTERACTION WITH ICAM2.
PubMed=11017109; DOI=10.1038/79815;
Geijtenbeek T.B.H., Krooshoop D.J., Bleijs D.A., van Vliet S.J.,
van Duijnhoven G.C.F., Grabovsky V., Alon R., Figdor C.G.,
van Kooyk Y.;
"DC-SIGN-ICAM-2 interaction mediates dendritic cell trafficking.";
Nat. Immunol. 1:353-357(2000).
[11]
SUBUNIT, AND LIGAND-BINDING.
PubMed=11384997; DOI=10.1074/jbc.M104565200;
Mitchell D.A., Fadden A.J., Drickamer K.;
"A novel mechanism of carbohydrate recognition by the C-type lectins
DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent
ligands.";
J. Biol. Chem. 276:28939-28945(2001).
[12]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH CYTOMEGALOVIRUS
GLYCOPROTEIN B (GB).
PubMed=12433371; DOI=10.1016/S1074-7613(02)00447-8;
Halary F., Amara A., Lortat-Jacob H., Messerle M., Delaunay T.,
Houles C., Fieschi F., Arenzana-Seisdedos F., Moreau J.-F.,
Dechanet-Merville J.;
"Human cytomegalovirus binding to DC-SIGN is required for dendritic
cell infection and target cell trans-infection.";
Immunity 17:653-664(2002).
[13]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH ICAM 3 AND HIV-1
GP120, AND MUTAGENESIS OF ASP-320; GLU-324; GLU-347; ASN-349; ASN-350;
ASP-355; ASN-365 AND ASP-366.
PubMed=11799126; DOI=10.1074/jbc.M111532200;
Geijtenbeek T.B.H., van Duijnhoven G.C.F., van Vliet S.J., Krieger E.,
Vriend G., Figdor C.G., van Kooyk Y.;
"Identification of different binding sites in the dendritic cell-
specific receptor DC-SIGN for intercellular adhesion molecule 3 and
HIV-1.";
J. Biol. Chem. 277:11314-11320(2002).
[14]
FUNCTION, AND MUTAGENESIS OF 14-LEU-LEU-15.
PubMed=11859097; DOI=10.4049/jimmunol.168.5.2118;
Engering A., Geijtenbeek T.B.H., van Vliet S.J., Wijers M.,
van Liempt E., Demaurex N., Lanzavecchia A., Fransen J., Figdor C.G.,
Piguet V., van Kooyk Y.;
"The dendritic cell-specific adhesion receptor DC-SIGN internalizes
antigen for presentation to T cells.";
J. Immunol. 168:2118-2126(2002).
[15]
ROLE IN HIV-1 INFECTION.
PubMed=11825572; DOI=10.1016/S1074-7613(02)00259-5;
Kwon D.S., Gregorio G., Bitton N., Hendrickson W.A., Littman D.R.;
"DC-SIGN-mediated internalization of HIV is required for trans-
enhancement of T cell infection.";
Immunity 16:135-144(2002).
[16]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 GP120;
HIV-2 GP120; SIV GP120 AND EBOLA GLYCOPROTEINS.
PubMed=12502850; DOI=10.1128/JVI.77.2.1337-1346.2003;
Lin G., Simmons G., Poehlmann S., Baribaud F., Ni H., Leslie G.J.,
Haggarty B.S., Bates P., Weissman D., Hoxie J.A., Doms R.W.;
"Differential N-linked glycosylation of human immunodeficiency virus
and Ebola virus envelope glycoproteins modulates interactions with DC-
SIGN and DC-SIGNR.";
J. Virol. 77:1337-1346(2003).
[17]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH DENGUE VIRUS
ENVELOPE E PROTEIN.
PubMed=12682107; DOI=10.1084/jem.20021840;
Tassaneetrithep B., Burgess T.H., Granelli-Piperno A.,
Trumpfheller C., Finke J., Sun W., Eller M.A., Pattanapanyasat K.,
Sarasombath S., Birx D.L., Steinman R.M., Schlesinger S.,
Marovich M.A.;
"DC-SIGN (CD209) mediates dengue virus infection of human dendritic
cells.";
J. Exp. Med. 197:823-829(2003).
[18]
FUNCTION (MICROBIAL INFECTION) IN HIV-1 INFECTION.
PubMed=12692233; DOI=10.1128/JVI.77.9.5313-5323.2003;
Nobile C., Moris A., Porrot F., Sol-Foulon N., Schwartz O.;
"Inhibition of human immunodeficiency virus type 1 Env-mediated fusion
by DC-SIGN.";
J. Virol. 77:5313-5323(2003).
[19]
FUNCTION.
PubMed=12574325; DOI=10.4049/jimmunol.170.4.1635;
Appelmelk B.J., van Die I., van Vliet S.J., Vandenbroucke-Grauls C.M.,
Geijtenbeek T.B.H., van Kooyk Y.;
"Carbohydrate profiling identifies new pathogens that interact with
dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic
cells.";
J. Immunol. 170:1635-1639(2003).
[20]
REVIEW ON ROLE IN HIV-1 INFECTION AND ON PATHOGEN BINDING.
PubMed=12949494; DOI=10.1038/nri1182;
van Kooyk Y., Geijtenbeek T.B.H.;
"DC-SIGN: escape mechanism for pathogens.";
Nat. Rev. Immunol. 3:697-709(2003).
[21]
REVIEW ON ROLE IN HIV-1 INFECTION.
PubMed=12960229; DOI=10.1189/jlb.0503208;
Turville S., Wilkinson J., Cameron P., Dable J., Cunningham A.L.;
"The role of dendritic cell C-type lectin receptors in HIV
pathogenesis.";
J. Leukoc. Biol. 74:710-718(2003).
[22]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EBOLAVIRUS
GLYCOPROTEIN.
PubMed=12504546; DOI=10.1006/viro.2002.1730;
Simmons G., Reeves J.D., Grogan C.C., Vandenberghe L.H., Baribaud F.,
Whitbeck J.C., Burke E., Buchmeier M.J., Soilleux E.J., Riley J.L.,
Doms R.W., Bates P., Poehlmann S.;
"DC-SIGN and DC-SIGNR bind ebola glycoproteins and enhance infection
of macrophages and endothelial cells.";
Virology 305:115-123(2003).
[23]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HCV E2
GLYCOPROTEIN.
PubMed=15371595; DOI=10.1073/pnas.0405695101;
Cormier E.G., Durso R.J., Tsamis F., Boussemart L., Manix C.,
Olson W.C., Gardner J.P., Dragic T.;
"L-SIGN (CD209L) and DC-SIGN (CD209) mediate transinfection of liver
cells by hepatitis C virus.";
Proc. Natl. Acad. Sci. U.S.A. 101:14067-14072(2004).
[24]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH SARS CORONAVIRUS
GLYCOPROTEIN.
PubMed=15140961; DOI=10.1128/JVI.78.11.5642-5650.2004;
Yang Z.Y., Huang Y., Ganesh L., Leung K., Kong W.P., Schwartz O.,
Subbarao K., Nabel G.J.;
"pH-dependent entry of severe acute respiratory syndrome coronavirus
is mediated by the spike glycoprotein and enhanced by dendritic cell
transfer through DC-SIGN.";
J. Virol. 78:5642-5650(2004).
[25]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MARBURG VIRUS
GLYCOPROTEIN.
PubMed=15479853; DOI=10.1128/JVI.78.21.12090-12095.2004;
Marzi A., Gramberg T., Simmons G., Moeller P., Rennekamp A.J.,
Krumbiegel M., Geier M., Eisemann J., Turza N., Saunier B.,
Steinkasserer A., Becker S., Bates P., Hofmann H., Poehlmann S.;
"DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus
and the S protein of severe acute respiratory syndrome coronavirus.";
J. Virol. 78:12090-12095(2004).
[26]
INTERACTION WITH CEACAM1.
PubMed=16246332; DOI=10.1016/j.febslet.2005.09.089;
van Gisbergen K.P., Ludwig I.S., Geijtenbeek T.B., van Kooyk Y.;
"Interactions of DC-SIGN with Mac-1 and CEACAM1 regulate contact
between dendritic cells and neutrophils.";
FEBS Lett. 579:6159-6168(2005).
[27]
POLYMORPHISM, AND INVOLVEMENT IN SUSCEPTIBILITY TO DENGUE VIRUS
INFECTION.
PubMed=15838506; DOI=10.1038/ng1550;
Sakuntabhai A., Turbpaiboon C., Casademont I., Chuansumrit A.,
Lowhnoo T., Kajaste-Rudnitski A., Kalayanarooj S.M.,
Tangnararatchakit K., Tangthawornchaikul N., Vasanawathana S.,
Chaiyaratana W., Yenchitsomanus P.T., Suriyaphol P., Avirutnan P.,
Chokephaibulkit K., Matsuda F., Yoksan S., Jacob Y., Lathrop G.M.,
Malasit P., Despres P., Julier C.;
"A variant in the CD209 promoter is associated with severity of dengue
disease.";
Nat. Genet. 37:507-513(2005).
[28]
FUNCTION (MICROBIAL INFECTION) BY M.TUBERCULOSIS.
PubMed=16092920; DOI=10.1042/BJ20050709;
Pitarque S., Herrmann J.L., Duteyrat J.L., Jackson M., Stewart G.R.,
Lecointe F., Payre B., Schwartz O., Young D.B., Marchal G.,
Lagrange P.H., Puzo G., Gicquel B., Nigou J., Neyrolles O.;
"Deciphering the molecular bases of Mycobacterium tuberculosis binding
to the lectin DC-SIGN reveals an underestimated complexity.";
Biochem. J. 392:615-624(2005).
[29]
FUNCTION (MICROBIAL INFECTION), AND INVOLVEMENT IN M.TUBERCULOSIS
SUSCEPTIBILITY.
PubMed=16379498; DOI=10.1371/journal.pmed.0030020;
Barreiro L.B., Neyrolles O., Babb C.L., Tailleux L., Quach H.,
McElreavey K., Helden P.D., Hoal E.G., Gicquel B., Quintana-Murci L.;
"Promoter variation in the DC-SIGN-encoding gene CD209 is associated
with tuberculosis.";
PLoS Med. 3:230-235(2006).
[30]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MEASLES VIRUS
HEMAGGLUTININ.
PubMed=16537615; DOI=10.1128/JVI.80.7.3477-3486.2006;
de Witte L., Abt M., Schneider-Schaulies S., van Kooyk Y.,
Geijtenbeek T.B.;
"Measles virus targets DC-SIGN to enhance dendritic cell infection.";
J. Virol. 80:3477-3486(2006).
[31]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH WEST-NILE VIRUS
ENVELOPE GLYCOPROTEIN.
PubMed=16415006; DOI=10.1128/JVI.80.3.1290-1301.2006;
Davis C.W., Nguyen H.Y., Hanna S.L., Sanchez M.D., Doms R.W.,
Pierson T.C.;
"West Nile virus discriminates between DC-SIGN and DC-SIGNR for
cellular attachment and infection.";
J. Virol. 80:1290-1301(2006).
[32]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HEPATITIS C VIRUS
E1 AND E2 PROTEINS.
PubMed=16816373; DOI=10.2353/ajpath.2006.051191;
Lai W.K., Sun P.J., Zhang J., Jennings A., Lalor P.F., Hubscher S.,
McKeating J.A., Adams D.H.;
"Expression of DC-SIGN and DC-SIGNR on human sinusoidal endothelium: a
role for capturing hepatitis C virus particles.";
Am. J. Pathol. 169:200-208(2006).
[33]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH M.BOVIS PROTEINS.
PubMed=21203928; DOI=10.1007/s13238-010-0101-3;
Carroll M.V., Sim R.B., Bigi F., Jaekel A., Antrobus R.,
Mitchell D.A.;
"Identification of four novel DC-SIGN ligands on Mycobacterium bovis
BCG.";
Protein Cell 1:859-870(2010).
[34]
INTERACTION WITH C1QBP.
PubMed=22700724; DOI=10.1182/blood-2011-07-369728;
Hosszu K.K., Valentino A., Vinayagasundaram U., Vinayagasundaram R.,
Joyce M.G., Ji Y., Peerschke E.I., Ghebrehiwet B.;
"DC-SIGN, C1q, and gC1qR form a trimolecular receptor complex on the
surface of monocyte-derived immature dendritic cells.";
Blood 120:1228-1236(2012).
[35]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HERPES SIMPLEX
VIRUS SURFACE PROTEINS.
PubMed=18796707; DOI=10.1099/vir.0.2008/003129-0;
de Jong M.A., de Witte L., Bolmstedt A., van Kooyk Y.,
Geijtenbeek T.B.;
"Dendritic cells mediate herpes simplex virus infection and
transmission through the C-type lectin DC-SIGN.";
J. Gen. Virol. 89:2398-2409(2008).
[36]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH INFLUENZAVIRUS
HEMAGGLUTININ.
PubMed=21191006; DOI=10.1128/JVI.01705-10;
Londrigan S.L., Turville S.G., Tate M.D., Deng Y.M., Brooks A.G.,
Reading P.C.;
"N-linked glycosylation facilitates sialic acid-independent attachment
and entry of influenza A viruses into cells expressing DC-SIGN or L-
SIGN.";
J. Virol. 85:2990-3000(2011).
[37]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH RIFT FEVER VALLEY
VIRUS GLYCOPROTEIN G.
PubMed=21767814; DOI=10.1016/j.chom.2011.06.007;
Lozach P.Y., Kuehbacher A., Meier R., Mancini R., Bitto D., Bouloy M.,
Helenius A.;
"DC-SIGN as a receptor for phleboviruses.";
Cell Host Microbe 10:75-88(2011).
[38]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 254-382 IN COMPLEX WITH
GLCNAC(2)-MAN(3) PENTASACCHARIDE.
PubMed=11739956; DOI=10.1126/science.1066371;
Feinberg H., Mitchell D.A., Drickamer K., Weis W.I.;
"Structural basis for selective recognition of oligosaccharides by DC-
SIGN and DC-SIGNR.";
Science 294:2163-2166(2001).
[39]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN
CYTOMEGALOVIRUS /HHV-5 SURFACE PROTEINS.
PubMed=22496863; DOI=10.1371/journal.pone.0034795;
Haspot F., Lavault A., Sinzger C., Laib Sampaio K., Stierhof Y.D.,
Pilet P., Bressolette-Bodin C., Halary F.;
"Human cytomegalovirus entry into dendritic cells occurs via a
macropinocytosis-like pathway in a pH-independent and cholesterol-
dependent manner.";
PLoS ONE 7:E34795-E34795(2012).
[40]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH RESPIRATORY
SYNCYTIAL VIRUS GLYCOPROTEIN G.
PubMed=22090124; DOI=10.1128/JVI.06096-11;
Johnson T.R., McLellan J.S., Graham B.S.;
"Respiratory syncytial virus glycoprotein G interacts with DC-SIGN and
L-SIGN to activate ERK1 and ERK2.";
J. Virol. 86:1339-1347(2012).
[41]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH JAPANESE
ENCEPHALITIS VIRUS E PROTEIN.
PubMed=24623090; DOI=10.1007/s00705-014-2042-2;
Shimojima M., Takenouchi A., Shimoda H., Kimura N., Maeda K.;
"Distinct usage of three C-type lectins by Japanese encephalitis
virus: DC-SIGN, DC-SIGNR, and LSECtin.";
Arch. Virol. 159:2023-2031(2014).
[42]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH LASSA VIRUS
GLYCOPROTEIN.
PubMed=23966408; DOI=10.1128/JVI.01893-13;
Goncalves A.R., Moraz M.L., Pasquato A., Helenius A., Lozach P.Y.,
Kunz S.;
"Role of DC-SIGN in Lassa virus entry into human dendritic cells.";
J. Virol. 87:11504-11515(2013).
[43]
FUNCTION (MICROBIAL INFECTION).
PubMed=22440960; DOI=10.1016/j.coviro.2011.12.005;
Backovic M., Rey F.A.;
"Virus entry: old viruses, new receptors.";
Curr. Opin. Virol. 2:4-13(2012).
-!- FUNCTION: Pathogen-recognition receptor expressed on the surface
of immature dendritic cells (DCs) and involved in initiation of
primary immune response. Thought to mediate the endocytosis of
pathogens which are subsequently degraded in lysosomal
compartments. The receptor returns to the cell membrane surface
and the pathogen-derived antigens are presented to resting T-cells
via MHC class II proteins to initiate the adaptive immune
response. {ECO:0000269|PubMed:11859097}.
-!- FUNCTION: On DCs it is a high affinity receptor for ICAM2 and
ICAM3 by binding to mannose-like carbohydrates. May act as a DC
rolling receptor that mediates transendothelial migration of DC
presursors from blood to tissues by binding endothelial ICAM2.
Seems to regulate DC-induced T-cell proliferation by binding to
ICAM3 on T-cells in the immunological synapse formed between DC
and T-cells. {ECO:0000269|PubMed:10721995,
ECO:0000269|PubMed:11017109, ECO:0000269|PubMed:12574325}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
HIV-1 and HIV-2. {ECO:0000269|PubMed:11799126,
ECO:0000269|PubMed:12502850, ECO:0000269|PubMed:1518869}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Ebolavirus. {ECO:0000269|PubMed:12502850,
ECO:0000269|PubMed:12504546}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Cytomegalovirus. {ECO:0000269|PubMed:12433371,
ECO:0000269|PubMed:22496863}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
HCV. {ECO:0000269|PubMed:15371595, ECO:0000269|PubMed:16816373}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Dengue virus. {ECO:0000269|PubMed:12682107}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Measles virus. {ECO:0000269|PubMed:16537615}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Herpes simplex virus 1. {ECO:0000269|PubMed:18796707}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Influenzavirus A. {ECO:0000269|PubMed:21191006}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
SARS coronavirus. {ECO:0000269|PubMed:15140961}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Japanese encephalitis virus. {ECO:0000269|PubMed:24623090}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Lassa virus (PubMed:23966408). Acts as an attachment receptor for
Marburg virusn. {ECO:0000269|PubMed:15479853}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Respiratory syncytial virus. {ECO:0000269|PubMed:22090124}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Rift valley fever virus and uukuniemi virus.
{ECO:0000269|PubMed:21767814}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
West-nile virus. {ECO:0000269|PubMed:16415006}.
-!- FUNCTION: (Microbial infection) Probably recognizes in a calcium-
dependent manner high mannose N-linked oligosaccharides in a
variety of bacterial pathogen antigens, including Leishmania
pifanoi LPG, Lewis-x antigen in Helicobacter pylori LPS, mannose
in Klebsiella pneumonae LPS, di-mannose and tri-mannose in
Mycobacterium tuberculosis ManLAM and Lewis-x antigen in
Schistosoma mansoni SEA (PubMed:16379498). Recognition of
M.tuberculosis by dendritic cells occurs partially via this
molecule (PubMed:16092920, PubMed:21203928).
{ECO:0000269|PubMed:16092920, ECO:0000269|PubMed:16379498,
ECO:0000269|PubMed:21203928}.
-!- SUBUNIT: Homotetramer. Interacts with C1QBP; the interaction is
indicative for a C1q:C1QBP:CD209 signaling complex. Interacts with
ICAM2 and ICAM3 by binding to mannose-like carbohydrates.
Interacts (via C-type lectin domain) with CEACAM1 (via Lewis X
moieties); this interaction is regulated by the glycosylation
pattern of CEACAM1 on cell types and regulates contact between
dendritic cells and neutrophils (PubMed:16246332).
{ECO:0000269|PubMed:10721995, ECO:0000269|PubMed:11017109,
ECO:0000269|PubMed:11384997, ECO:0000269|PubMed:11739956,
ECO:0000269|PubMed:16246332, ECO:0000269|PubMed:22700724}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 and HIV-2
gp120 (PubMed:11799126, PubMed:12502850, PubMed:1518869).
{ECO:0000269|PubMed:11799126, ECO:0000269|PubMed:12502850,
ECO:0000269|PubMed:1518869}.
-!- SUBUNIT: (Microbial infection) Interacts with ebolavirus envelope
glycoproteins (PubMed:12502850, PubMed:12504546).
{ECO:0000269|PubMed:12502850, ECO:0000269|PubMed:12504546}.
-!- SUBUNIT: (Microbial infection) Interacts with cytomegalovirus gB
protein (PubMed:12433371, PubMed:22496863).
{ECO:0000269|PubMed:12433371, ECO:0000269|PubMed:22496863}.
-!- SUBUNIT: (Microbial infection) Interacts with HCV E2 protein
(PubMed:15371595, PubMed:16816373). {ECO:0000269|PubMed:15371595,
ECO:0000269|PubMed:16816373}.
-!- SUBUNIT: (Microbial infection) Interacts with dengue virus major
envelope protein E. {ECO:0000269|PubMed:12682107}.
-!- SUBUNIT: (Microbial infection) Interacts with measles
hemagglutinin. {ECO:0000269|PubMed:16537615}.
-!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
1 surface proteins. {ECO:0000269|PubMed:18796707}.
-!- SUBUNIT: (Microbial infection) Interacts with Influenzavirus A
hemagglutinin. {ECO:0000269|PubMed:21191006}.
-!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus
glycoprotein. {ECO:0000269|PubMed:15140961}.
-!- SUBUNIT: (Microbial infection) Interacts with Japanese
encephalitis virus E protein. {ECO:0000269|PubMed:24623090}.
-!- SUBUNIT: (Microbial infection) Interacts with Lassa virus
Glycoprotein. {ECO:0000269|PubMed:23966408}.
-!- SUBUNIT: (Microbial infection) Interacts with marburg virus
glycoprotein. {ECO:0000269|PubMed:15479853}.
-!- SUBUNIT: (Microbial infection) Interacts with Respiratory
syncytial virus glycoprotein G. {ECO:0000269|PubMed:22090124}.
-!- SUBUNIT: (Microbial infection) Interacts with Rift valley fever
virus and uukuniemi virus envelope glycoprotein.
{ECO:0000269|PubMed:21767814}.
-!- SUBUNIT: (Microbial infection) Interacts with west-nile virus
envelope glycoprotein. {ECO:0000269|PubMed:16415006}.
-!- SUBUNIT: (Microbial infection) Interacts with whole M.bovis cells
in a Ca(2+)-dependent and independent manner; in vitro experiments
suggest it interacts with CH60.1 (groL1), DnaK, GADPH (gap) and
LrpG (PubMed:21203928). {ECO:0000269|PubMed:21203928}.
-!- INTERACTION:
Q03463:- (xeno); NbExp=2; IntAct=EBI-9257341, EBI-9257330;
Q08AM6:VAC14; NbExp=3; IntAct=EBI-9257341, EBI-2107455;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cell membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 5: Cell membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 6: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 7: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 8: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 9: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 10: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 11: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 12: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Comment=Additional isoforms seem to exist. Several splicing
events may be used independently in a modular way. Deletion of
the transmembrane domain encoding exon through alternative
splicing produces soluble isoforms.
{ECO:0000269|PubMed:11337487};
Name=1; Synonyms=mDC-SIGN1A type I;
IsoId=Q9NNX6-1; Sequence=Displayed;
Name=2; Synonyms=mDC-SIGN1A type II;
IsoId=Q9NNX6-2; Sequence=VSP_010049;
Name=3; Synonyms=mDC-SIGN1A type III;
IsoId=Q9NNX6-3; Sequence=VSP_010044;
Name=4; Synonyms=mDC-SIGN1A type IV;
IsoId=Q9NNX6-4; Sequence=VSP_010042;
Name=5; Synonyms=mDC-SIGN1B type I;
IsoId=Q9NNX6-5; Sequence=VSP_010037;
Name=6; Synonyms=sDC-SIGN1A type I;
IsoId=Q9NNX6-6; Sequence=VSP_010041;
Name=7; Synonyms=sDC-SIGN1A type II;
IsoId=Q9NNX6-7; Sequence=VSP_010038;
Name=8; Synonyms=sDC-SIGN1A type III;
IsoId=Q9NNX6-8; Sequence=VSP_010038, VSP_010043;
Name=9; Synonyms=sDC-SIGN1A type IV;
IsoId=Q9NNX6-9; Sequence=VSP_010039, VSP_010040;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=10; Synonyms=sDC-SIGN1B type I;
IsoId=Q9NNX6-10; Sequence=VSP_010037, VSP_010041;
Name=11; Synonyms=sDC-SIGN1B type II;
IsoId=Q9NNX6-11; Sequence=VSP_010037, VSP_010041, VSP_010047;
Name=12; Synonyms=sDC-SIGN1B type III;
IsoId=Q9NNX6-12; Sequence=VSP_010037, VSP_010041, VSP_010048,
VSP_010050;
-!- TISSUE SPECIFICITY: Predominantly expressed in dendritic cells and
in DC-residing tissues. Also found in placental macrophages,
endothelial cells of placental vascular channels, peripheral blood
mononuclear cells, and THP-1 monocytes.
{ECO:0000269|PubMed:11257134, ECO:0000269|PubMed:11337487}.
-!- DOMAIN: The tandem repeat domain, also called neck domain,
mediates oligomerization.
-!- POLYMORPHISM: Genetic variations in the CD209 promoter determine
M.tuberculosis susceptibility [MIM:607948] (PubMed:16379498).
{ECO:0000305|PubMed:16379498}.
-!- POLYMORPHISM: Genetic variations in CD209 may influence
susceptibility or resistance to dengue virus infection, as well as
disease progression and severity [MIM:614371]. A promoter
polymorphism in the CD209 gene is associated with protection from
dengue fever, but not dengue hemorrhagic fever.
-!- MISCELLANEOUS: In vitro, is a receptor for HIV-1 and transmits
HIV-1 either in trans without DC infection, or in cis following a
DC infection to permissive T-cells to induce a robust infection.
Bound HIV-1 remains infectious over a prolonged period of time and
it is proposed that bound HIV-1 is not degraded but protected in
non-lysosomal acidic organelles within the DCs close to the cell
membrane thus contributing to the HIV-1 infectious potential
during transport by DCs from the periphery to lymphoid organs.
-!- SEQUENCE CAUTION:
Sequence=AAK91858.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=DC-SIGN entry;
URL="https://en.wikipedia.org/wiki/DC-SIGN";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=DC-SIGN;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_00121";
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EMBL; M98457; AAF77072.1; -; mRNA.
EMBL; AF209479; AAG13814.1; -; Genomic_DNA.
EMBL; AF290886; AAK20997.1; -; mRNA.
EMBL; AY042221; AAK91846.1; -; mRNA.
EMBL; AY042222; AAK91847.1; -; mRNA.
EMBL; AY042223; AAK91848.1; -; mRNA.
EMBL; AY042224; AAK91849.1; -; mRNA.
EMBL; AY042225; AAK91850.1; -; mRNA.
EMBL; AY042226; AAK91851.1; -; mRNA.
EMBL; AY042227; AAK91852.1; -; mRNA.
EMBL; AY042228; AAK91853.1; -; mRNA.
EMBL; AY042229; AAK91854.1; -; mRNA.
EMBL; AY042230; AAK91855.1; -; mRNA.
EMBL; AY042231; AAK91856.1; -; mRNA.
EMBL; AY042232; AAK91857.1; -; mRNA.
EMBL; AY042233; AAK91858.1; ALT_SEQ; mRNA.
EMBL; AK293089; BAF85778.1; -; mRNA.
EMBL; AC008763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC008812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471139; EAW68991.1; -; Genomic_DNA.
EMBL; CH471139; EAW68993.1; -; Genomic_DNA.
EMBL; CH471139; EAW68997.1; -; Genomic_DNA.
EMBL; CH471139; EAW68998.1; -; Genomic_DNA.
EMBL; BC110615; AAI10616.1; -; mRNA.
CCDS; CCDS12186.1; -. [Q9NNX6-1]
CCDS; CCDS45949.1; -. [Q9NNX6-7]
CCDS; CCDS45950.1; -. [Q9NNX6-6]
CCDS; CCDS45951.1; -. [Q9NNX6-2]
CCDS; CCDS45952.1; -. [Q9NNX6-3]
CCDS; CCDS59344.1; -. [Q9NNX6-8]
PIR; A46274; A46274.
RefSeq; NP_001138365.1; NM_001144893.1.
RefSeq; NP_001138366.1; NM_001144894.1. [Q9NNX6-7]
RefSeq; NP_001138367.1; NM_001144895.1. [Q9NNX6-3]
RefSeq; NP_001138368.1; NM_001144896.1. [Q9NNX6-6]
RefSeq; NP_001138369.1; NM_001144897.1. [Q9NNX6-2]
RefSeq; NP_066978.1; NM_021155.3. [Q9NNX6-1]
UniGene; Hs.278694; -.
PDB; 1K9I; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=250-404.
PDB; 1SL4; X-ray; 1.55 A; A=250-404.
PDB; 1SL5; X-ray; 1.80 A; A=250-388.
PDB; 2B6B; EM; 25.00 A; D=251-404.
PDB; 2IT5; X-ray; 2.40 A; A=250-388.
PDB; 2IT6; X-ray; 1.95 A; A=250-404.
PDB; 2XR5; X-ray; 1.42 A; A=254-404.
PDB; 2XR6; X-ray; 1.35 A; A=250-404.
PDBsum; 1K9I; -.
PDBsum; 1SL4; -.
PDBsum; 1SL5; -.
PDBsum; 2B6B; -.
PDBsum; 2IT5; -.
PDBsum; 2IT6; -.
PDBsum; 2XR5; -.
PDBsum; 2XR6; -.
ProteinModelPortal; Q9NNX6; -.
SMR; Q9NNX6; -.
BioGrid; 119051; 14.
DIP; DIP-60629N; -.
IntAct; Q9NNX6; 3.
STRING; 9606.ENSP00000315477; -.
BindingDB; Q9NNX6; -.
ChEMBL; CHEMBL1795114; -.
iPTMnet; Q9NNX6; -.
PhosphoSitePlus; Q9NNX6; -.
BioMuta; CD209; -.
DMDM; 46396012; -.
REPRODUCTION-2DPAGE; Q9NNX6; -.
PaxDb; Q9NNX6; -.
PeptideAtlas; Q9NNX6; -.
PRIDE; Q9NNX6; -.
Ensembl; ENST00000204801; ENSP00000204801; ENSG00000090659. [Q9NNX6-7]
Ensembl; ENST00000315591; ENSP00000315407; ENSG00000090659. [Q9NNX6-6]
Ensembl; ENST00000315599; ENSP00000315477; ENSG00000090659. [Q9NNX6-1]
Ensembl; ENST00000354397; ENSP00000346373; ENSG00000090659. [Q9NNX6-2]
Ensembl; ENST00000394161; ENSP00000377716; ENSG00000090659. [Q9NNX6-4]
Ensembl; ENST00000601256; ENSP00000470658; ENSG00000090659. [Q9NNX6-12]
Ensembl; ENST00000601951; ENSP00000468827; ENSG00000090659. [Q9NNX6-10]
Ensembl; ENST00000602261; ENSP00000471137; ENSG00000090659. [Q9NNX6-3]
GeneID; 30835; -.
KEGG; hsa:30835; -.
UCSC; uc002mhr.3; human. [Q9NNX6-1]
CTD; 30835; -.
DisGeNET; 30835; -.
EuPathDB; HostDB:ENSG00000090659.17; -.
GeneCards; CD209; -.
HGNC; HGNC:1641; CD209.
HPA; CAB032436; -.
HPA; CAB033831; -.
MalaCards; CD209; -.
MIM; 604672; gene+phenotype.
MIM; 607948; phenotype.
MIM; 614371; phenotype.
neXtProt; NX_Q9NNX6; -.
OpenTargets; ENSG00000090659; -.
PharmGKB; PA26199; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00760000118924; -.
HOVERGEN; HBG050992; -.
InParanoid; Q9NNX6; -.
KO; K06563; -.
OMA; NLAKFWI; -.
OrthoDB; EOG091G0G9W; -.
PhylomeDB; Q9NNX6; -.
TreeFam; TF333341; -.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-8851680; Butyrophilin (BTN) family interactions.
EvolutionaryTrace; Q9NNX6; -.
GeneWiki; DC-SIGN; -.
GenomeRNAi; 30835; -.
PRO; PR:Q9NNX6; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000090659; -.
ExpressionAtlas; Q9NNX6; baseline and differential.
Genevisible; Q9NNX6; HS.
GO; GO:0009986; C:cell surface; HDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:CAFA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; TAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; NAS:UniProtKB.
GO; GO:0005537; F:mannose binding; TAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042605; F:peptide antigen binding; NAS:UniProtKB.
GO; GO:0046790; F:virion binding; TAS:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0019882; P:antigen processing and presentation; NAS:UniProtKB.
GO; GO:0097323; P:B cell adhesion; IDA:UniProtKB.
GO; GO:0009988; P:cell-cell recognition; TAS:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
GO; GO:0075733; P:intracellular transport of virus; TAS:UniProtKB.
GO; GO:0007159; P:leukocyte cell-cell adhesion; NAS:UniProtKB.
GO; GO:0019048; P:modulation by virus of host morphology or physiology; TAS:UniProtKB.
GO; GO:0046968; P:peptide antigen transport; NAS:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:0042129; P:regulation of T cell proliferation; IDA:MGI.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0019079; P:viral genome replication; NAS:UniProtKB.
GO; GO:0019062; P:virion attachment to host cell; TAS:UniProtKB.
CDD; cd03590; CLECT_DC-SIGN_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR033989; CD209-like_CTLD.
InterPro; IPR016187; CTDL_fold.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Calcium;
Cell adhesion; Cell membrane; Complete proteome; Disulfide bond;
Endocytosis; Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Immunity; Innate immunity; Lectin;
Mannose-binding; Membrane; Metal-binding; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 404 CD209 antigen.
/FTId=PRO_0000046595.
TOPO_DOM 1 37 Cytoplasmic. {ECO:0000305}.
TRANSMEM 38 58 Helical; Signal-anchor for type II
membrane protein. {ECO:0000305}.
TOPO_DOM 59 404 Extracellular. {ECO:0000305}.
REPEAT 96 118 1.
REPEAT 119 141 2.
REPEAT 142 164 3.
REPEAT 165 187 4.
REPEAT 188 210 5.
REPEAT 211 233 6.
REPEAT 234 257 7.
DOMAIN 263 378 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
REGION 96 257 7 X approximate tandem repeats.
MOTIF 14 15 Endocytosis signal.
MOTIF 16 18 Endocytosis signal. {ECO:0000255}.
MOTIF 31 34 Endocytosis signal. {ECO:0000255}.
METAL 347 347 Calcium.
METAL 349 349 Calcium.
METAL 351 351 Calcium; via carbonyl oxygen.
METAL 354 354 Calcium.
METAL 365 365 Calcium.
METAL 366 366 Calcium.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 256 267
DISULFID 284 377
DISULFID 356 369
VAR_SEQ 1 15 MSDSKEPRLQQLGLL -> MASACPGSDFTSIHS (in
isoform 5, isoform 10, isoform 11 and
isoform 12).
{ECO:0000303|PubMed:11337487,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010037.
VAR_SEQ 16 59 Missing (in isoform 7 and isoform 8).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010038.
VAR_SEQ 30 34 GYKSL -> RNQKC (in isoform 9).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010039.
VAR_SEQ 35 404 Missing (in isoform 9).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010040.
VAR_SEQ 36 59 Missing (in isoform 6, isoform 10,
isoform 11 and isoform 12).
{ECO:0000303|PubMed:11337487,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010041.
VAR_SEQ 74 309 Missing (in isoform 4).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010042.
VAR_SEQ 142 233 Missing (in isoform 8).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010043.
VAR_SEQ 158 249 Missing (in isoform 3).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010044.
VAR_SEQ 191 236 Missing (in isoform 11).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010047.
VAR_SEQ 301 321 NFLQLQSSRSNRFTWMGLSDL -> LQAVLEQRRAQQRWGG
RLRGI (in isoform 12).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010048.
VAR_SEQ 301 306 Missing (in isoform 2).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010049.
VAR_SEQ 322 404 Missing (in isoform 12).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010050.
VARIANT 168 168 E -> D (in dbSNP:rs11465377).
/FTId=VAR_050104.
VARIANT 214 214 E -> D (in dbSNP:rs11465377).
/FTId=VAR_036689.
VARIANT 242 242 L -> V (in dbSNP:rs11465380).
/FTId=VAR_036690.
VARIANT 382 382 A -> S (in dbSNP:rs11465393).
/FTId=VAR_050105.
MUTAGEN 14 15 LL->AA: Loss of antigen internalization
by endocytosis.
{ECO:0000269|PubMed:11859097}.
MUTAGEN 320 320 D->A: Loss of binding to ICAM3 and HIV-1
gp120. {ECO:0000269|PubMed:11799126}.
MUTAGEN 324 324 E->A: Loss of binding to ICAM3 and HIV-1
gp120. {ECO:0000269|PubMed:11799126}.
MUTAGEN 347 347 E->Q: Loss of binding to ICAM3 and HIV-1
gp120. {ECO:0000269|PubMed:11799126}.
MUTAGEN 349 349 N->D: Loss of binding to ICAM3 and HIV-1
gp120. {ECO:0000269|PubMed:11799126}.
MUTAGEN 350 350 N->A: Loss of binding to ICAM3 and HIV-1
gp120. {ECO:0000269|PubMed:11799126}.
MUTAGEN 355 355 D->A: Loss of binding to ICAM3 and HIV-1
gp120. {ECO:0000269|PubMed:11799126}.
MUTAGEN 365 365 N->D: Loss of binding to ICAM3 and HIV-1
gp120. {ECO:0000269|PubMed:11799126}.
MUTAGEN 366 366 D->A: Loss of binding to ICAM3 and HIV-1
gp120. {ECO:0000269|PubMed:11799126}.
CONFLICT 152 152 W -> Q (in Ref. 4; AAK91848).
{ECO:0000305}.
STRAND 261 263 {ECO:0000244|PDB:2XR6}.
STRAND 266 270 {ECO:0000244|PDB:2XR6}.
HELIX 277 286 {ECO:0000244|PDB:2XR6}.
HELIX 297 310 {ECO:0000244|PDB:2XR6}.
STRAND 314 323 {ECO:0000244|PDB:2XR6}.
STRAND 326 329 {ECO:0000244|PDB:2XR6}.
HELIX 337 342 {ECO:0000244|PDB:2XR6}.
STRAND 356 360 {ECO:0000244|PDB:2XR6}.
STRAND 363 367 {ECO:0000244|PDB:2XR6}.
STRAND 373 380 {ECO:0000244|PDB:2XR6}.
TURN 381 383 {ECO:0000244|PDB:2XR6}.
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


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