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C-type lectin domain family 4 member M (CD209 antigen-like protein 1) (DC-SIGN-related protein) (DC-SIGNR) (Dendritic cell-specific ICAM-3-grabbing non-integrin 2) (DC-SIGN2) (Liver/lymph node-specific ICAM-3-grabbing non-integrin) (L-SIGN) (CD antigen CD299)

 CLC4M_HUMAN             Reviewed;         399 AA.
Q9H2X3; A6NKI4; A8K8B3; Q69F40; Q969M4; Q96QP3; Q96QP4; Q96QP5;
Q96QP6; Q9BXS3; Q9H2Q9; Q9H8F0; Q9Y2A8;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 169.
RecName: Full=C-type lectin domain family 4 member M;
AltName: Full=CD209 antigen-like protein 1;
AltName: Full=DC-SIGN-related protein;
Short=DC-SIGNR;
AltName: Full=Dendritic cell-specific ICAM-3-grabbing non-integrin 2;
Short=DC-SIGN2;
AltName: Full=Liver/lymph node-specific ICAM-3-grabbing non-integrin;
Short=L-SIGN;
AltName: CD_antigen=CD299;
Name=CLEC4M; Synonyms=CD209L, CD209L1, CD299;
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 9).
TISSUE=Liver;
PubMed=10072769; DOI=10.1016/S0378-1119(99)00004-9;
Yokoyama-Kobayashi M., Yamaguchi T., Sekine S., Kato S.;
"Selection of cDNAs encoding putative type II membrane proteins on the
cell surface from a human full-length cDNA bank.";
Gene 228:161-167(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (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] (ISOFORMS 1; 2; 4; 5; 6 AND 7), ALTERNATIVE
SPLICING (ISOFORM 3), POLYMORPHISM, AND VARIANT GLN-164.
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), TISSUE SPECIFICITY, FUNCTION,
INTERACTION WITH ICAM3 AND HIV-1 GP120, AND POLYMORPHISM.
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASN-291.
Bruen S., Bashirova A., Carrington M., KewalRamani V.;
"L-SIGN interaction with HIV-1.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8 AND 10).
TISSUE=Placenta, and Testis;
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).
[7]
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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]
TISSUE SPECIFICITY, INTERACTION WITH HIV-1 GP120, AND ROLE IN HIV-1
INFECTION.
PubMed=11226297; DOI=10.1073/pnas.051631398;
Poehlmann S., Soilleux E.J., Baribaud F., Leslie G.J., Morris L.S.,
Trowsdale J., Lee B., Coleman N., Doms R.W.;
"DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds
to human and simian immunodeficiency viruses and activates infection
in trans.";
Proc. Natl. Acad. Sci. U.S.A. 98:2670-2675(2001).
[10]
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).
[11]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN
CYTOMEGALOVIRUS/HHV-5 GB PROTEIN.
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).
[12]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EBOLAVIRUS
GLYCOPROTEIN.
PubMed=12050398; DOI=10.1128/JVI.76.13.6841-6844.2002;
Alvarez C.P., Lasala F., Carrillo J., Muniz O., Corbi A.L.,
Delgado R.;
"C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola
virus in cis and in trans.";
J. Virol. 76:6841-6844(2002).
[13]
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).
[14]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH SARS CORONAVIRUS
SPIKE 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).
[15]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HEPATITIS C VIRUS
E2 PROTEIN.
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).
[16]
INTERACTION WITH SARS CORONAVIRUS S PROTEIN, AND TISSUE SPECIFICITY.
PubMed=15496474; DOI=10.1073/pnas.0403812101;
Jeffers S.A., Tusell S.M., Gillim-Ross L., Hemmila E.M.,
Achenbach J.E., Babcock G.J., Thomas W.D. Jr., Thackray L.B.,
Young M.D., Mason R.J., Ambrosino D.M., Wentworth D.E.,
Demartini J.C., Holmes K.V.;
"CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome
coronavirus.";
Proc. Natl. Acad. Sci. U.S.A. 101:15748-15753(2004).
[17]
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).
[18]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN CORONAVIRUS
229E SPIKE GLYCOPROTEIN.
PubMed=17037540; DOI=10.1007/978-0-387-33012-9_44;
Jeffers S.A., Hemmila E.M., Holmes K.V.;
"Human coronavirus 229E can use CD209L (L-SIGN) to enter cells.";
Adv. Exp. Med. Biol. 581:265-269(2006).
[19]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH WEST-NILE VIRUS
ENVELOPE PROTEIN.
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).
[20]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH M.BOVIS LPRG.
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).
[21]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 GP120.
PubMed=21277928; DOI=10.1016/j.humimm.2011.01.012;
da Silva R.C., Segat L., Crovella S.;
"Role of DC-SIGN and L-SIGN receptors in HIV-1 vertical
transmission.";
Hum. Immunol. 72:305-311(2011).
[22]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH INFLUENZAVIRUS A
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).
[23]
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).
[24]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 265-394 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).
[25]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 216-399, AND DISULFIDE
BONDS.
PubMed=15509576; DOI=10.1074/jbc.M409925200;
Feinberg H., Guo Y., Mitchell D.A., Drickamer K., Weis W.I.;
"Extended neck regions stabilize tetramers of the receptors DC-SIGN
and DC-SIGNR.";
J. Biol. Chem. 280:1327-1335(2005).
[26]
X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 250-399, AND DISULFIDE
BONDS.
PubMed=15784257; DOI=10.1016/j.jmb.2005.01.063;
Snyder G.A., Colonna M., Sun P.D.;
"The structure of DC-SIGNR with a portion of its repeat domain lends
insights to modeling of the receptor tetramer.";
J. Mol. Biol. 347:979-989(2005).
-!- FUNCTION: Probable pathogen-recognition receptor involved in
peripheral immune surveillance in liver. May mediate the
endocytosis of pathogens which are subsequently degraded in
lysosomal compartments. Is a receptor for ICAM3, probably by
binding to mannose-like carbohydrates.
{ECO:0000269|PubMed:11257134}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Ebolavirus. {ECO:0000269|PubMed:12050398,
ECO:0000269|PubMed:12502850}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Hepatitis C virus. {ECO:0000269|PubMed:15371595,
ECO:0000269|PubMed:16816373}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
HIV-1. {ECO:0000269|PubMed:12502850, ECO:0000269|PubMed:21203928}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Human coronavirus 229E. {ECO:0000269|PubMed:17037540}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Human cytomegalovirus/HHV-5. {ECO:0000269|PubMed:12433371}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
Influenzavirus. {ECO:0000269|PubMed:21191006}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
SARS coronavirus. {ECO:0000269|PubMed:15479853}.
-!- FUNCTION: (Microbial infection) Acts as an attachment receptor for
West-nile virus. {ECO:0000269|PubMed:15479853}.
-!- 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
Marburg virus glycoprotein. {ECO:0000269|PubMed:15479853}.
-!- FUNCTION: (Microbial infection) Recognition of M.bovis by
dendritic cells may occur partially via this molecule.
{ECO:0000269|PubMed:21277928}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11384997,
ECO:0000269|PubMed:11739956}.
-!- SUBUNIT: (Microbial infection) Interacts with ebola virus
glycoprotein (PubMed:12050398, PubMed:12502850).
{ECO:0000269|PubMed:12050398, ECO:0000269|PubMed:12502850}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus E1
and E2 protein (PubMed:15371595, PubMed:16816373).
{ECO:0000269|PubMed:15371595, ECO:0000269|PubMed:16816373}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 gp120
(PubMed:21277928, PubMed:12502850). {ECO:0000269|PubMed:12502850,
ECO:0000269|PubMed:21277928}.
-!- SUBUNIT: (Microbial infection) Interacts with human coronavirus
229E spike glycoprotein. {ECO:0000269|PubMed:17037540}.
-!- SUBUNIT: (Microbial infection) Interacts with human
cytomegalovirus/HHV-5 gB protein. {ECO:0000269|PubMed:12433371}.
-!- SUBUNIT: (Microbial infection) Interacts with influenzavirus
hemagglutinin. {ECO:0000269|PubMed:21191006}.
-!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus
spike glycoprotein. {ECO:0000269|PubMed:15479853}.
-!- SUBUNIT: (Microbial infection) Interacts with west-nile virus
envelope protein E. {ECO:0000269|PubMed:16415006}.
-!- SUBUNIT: (Microbial infection) Interacts with Japanese
encephalitis virus E protein. {ECO:0000269|PubMed:24623090}.
-!- SUBUNIT: (Microbial infection) Interacts with Marburg virus
glycoprotein. {ECO:0000269|PubMed:15479853}.
-!- SUBUNIT: (Microbial infection) Interacts with M.bovis LprG.
{ECO:0000269|PubMed:21203928}.
-!- 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 5: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 6: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 7: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 10: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=10;
Comment=Additional isoforms seem to exist. Several splicing
events may occur independently in a modular way. Deletion of the
transmembrane domain encoding exon through alternative splicing
produces soluble isoforms.;
Name=1; Synonyms=mDC-SIGN2 type I;
IsoId=Q9H2X3-1; Sequence=Displayed;
Name=2; Synonyms=mDC-SIGN2 type III, mDC-SIGN2 type IV;
IsoId=Q9H2X3-2; Sequence=VSP_010063, VSP_010064;
Note=May be due to intron retention.;
Name=3; Synonyms=mDC-SIGN2 type V;
IsoId=Q9H2X3-3; Sequence=VSP_010065, VSP_010066;
Name=4; Synonyms=mDC-SIGN2 type VI;
IsoId=Q9H2X3-4; Sequence=VSP_010060, VSP_010062, VSP_010065,
VSP_010066;
Name=5; Synonyms=sDC-SIGN2 type I;
IsoId=Q9H2X3-5; Sequence=VSP_010058, VSP_010061, VSP_010062;
Name=6; Synonyms=sDC-SIGN2 type II;
IsoId=Q9H2X3-6; Sequence=VSP_010058, VSP_010063, VSP_010064;
Note=May be due to intron retention.;
Name=7; Synonyms=sDC-SIGN2 type III;
IsoId=Q9H2X3-7; Sequence=VSP_010058, VSP_010059;
Name=8;
IsoId=Q9H2X3-8; Sequence=VSP_010061;
Note=Non-canonical intron-exon splice junction.;
Name=9;
IsoId=Q9H2X3-9; Sequence=VSP_010056, VSP_010065, VSP_010066;
Name=10;
IsoId=Q9H2X3-10; Sequence=VSP_010056, VSP_010057, VSP_010063,
VSP_010064;
Note=May be due to intron retention.;
-!- TISSUE SPECIFICITY: Predominantly highly expressed in liver
sinusoidal endothelial cells and in lymph node. Found in placental
endothelium but not in macrophages. Expressed in type II alveolar
cells and lung endothelial cells. {ECO:0000269|PubMed:11226297,
ECO:0000269|PubMed:11257134, ECO:0000269|PubMed:15496474}.
-!- DOMAIN: The tandem repeat domain, also called neck domain,
mediates oligomerization.
-!- POLYMORPHISM: The number of repeats in the tandem repeat domain is
shown to vary between 3 and 9 per allele thus contributing to a
further variability in addition to alternative splicing. The shown
7 repeat-containing form has been shown to be the most frequent
one (53.9%) in a study with 350 Caucasian individuals.
-!- MISCELLANEOUS: In vitro, is a receptor for HIV-1 and transmits
HIV-1 to permissive T-cells.
-!- SEQUENCE CAUTION:
Sequence=AAR04559.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=DC-SIGNR;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_00122";
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EMBL; AB015629; BAA76496.1; -; mRNA.
EMBL; AF245219; AAG13848.2; -; mRNA.
EMBL; AF209481; AAG13815.2; -; Genomic_DNA.
EMBL; AF209480; AAG13815.2; JOINED; Genomic_DNA.
EMBL; AY042234; AAK91859.1; -; mRNA.
EMBL; AY042235; AAK91860.1; -; mRNA.
EMBL; AY042236; AAK91861.1; -; mRNA.
EMBL; AY042237; AAK91862.1; -; mRNA.
EMBL; AY042238; AAK91863.1; -; mRNA.
EMBL; AY042239; AAK91864.1; -; mRNA.
EMBL; AY042240; AAK91865.1; -; mRNA.
EMBL; AF290887; AAK20998.1; -; mRNA.
EMBL; AY343913; AAR04559.1; ALT_SEQ; mRNA.
EMBL; AK023750; BAB14667.1; -; mRNA.
EMBL; AK292278; BAF84967.1; -; mRNA.
EMBL; AC008812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC038851; AAH38851.1; -; mRNA.
CCDS; CCDS12187.1; -. [Q9H2X3-1]
CCDS; CCDS59346.1; -. [Q9H2X3-4]
CCDS; CCDS59347.1; -. [Q9H2X3-7]
CCDS; CCDS59348.1; -. [Q9H2X3-9]
RefSeq; NP_001138377.1; NM_001144905.1.
RefSeq; NP_001138378.1; NM_001144906.1. [Q9H2X3-7]
RefSeq; NP_001138379.1; NM_001144907.1. [Q9H2X3-5]
RefSeq; NP_001138380.1; NM_001144908.1. [Q9H2X3-4]
RefSeq; NP_001138381.1; NM_001144909.1.
RefSeq; NP_001138382.1; NM_001144910.1. [Q9H2X3-8]
RefSeq; NP_001138383.1; NM_001144911.1. [Q9H2X3-9]
RefSeq; NP_055072.3; NM_014257.4. [Q9H2X3-1]
RefSeq; XP_006722678.1; XM_006722615.2. [Q9H2X3-3]
UniGene; Hs.421437; -.
PDB; 1K9J; X-ray; 1.90 A; A/B=262-399.
PDB; 1SL6; X-ray; 2.25 A; A/B/C/D/E/F=216-399.
PDB; 1XAR; X-ray; 2.25 A; A/B=216-399.
PDB; 1XPH; X-ray; 1.41 A; A=250-399.
PDB; 1Z0Y; Model; -; A/B/C/D=85-399.
PDB; 3JQH; X-ray; 2.20 A; A=101-264.
PDBsum; 1K9J; -.
PDBsum; 1SL6; -.
PDBsum; 1XAR; -.
PDBsum; 1XPH; -.
PDBsum; 1Z0Y; -.
PDBsum; 3JQH; -.
ProteinModelPortal; Q9H2X3; -.
SMR; Q9H2X3; -.
BioGrid; 115615; 7.
IntAct; Q9H2X3; 3.
MINT; Q9H2X3; -.
STRING; 9606.ENSP00000316228; -.
ChEMBL; CHEMBL2176858; -.
iPTMnet; Q9H2X3; -.
PhosphoSitePlus; Q9H2X3; -.
BioMuta; CLEC4M; -.
DMDM; 46395990; -.
PaxDb; Q9H2X3; -.
PeptideAtlas; Q9H2X3; -.
PRIDE; Q9H2X3; -.
DNASU; 10332; -.
Ensembl; ENST00000248228; ENSP00000248228; ENSG00000104938. [Q9H2X3-8]
Ensembl; ENST00000327325; ENSP00000316228; ENSG00000104938. [Q9H2X3-1]
Ensembl; ENST00000359059; ENSP00000351954; ENSG00000104938. [Q9H2X3-5]
Ensembl; ENST00000595496; ENSP00000470132; ENSG00000104938. [Q9H2X3-7]
Ensembl; ENST00000596363; ENSP00000471125; ENSG00000104938. [Q9H2X3-9]
Ensembl; ENST00000597522; ENSP00000471132; ENSG00000104938. [Q9H2X3-4]
GeneID; 10332; -.
KEGG; hsa:10332; -.
UCSC; uc002mhz.4; human. [Q9H2X3-1]
CTD; 10332; -.
DisGeNET; 10332; -.
EuPathDB; HostDB:ENSG00000104938.16; -.
GeneCards; CLEC4M; -.
HGNC; HGNC:13523; CLEC4M.
HPA; CAB033689; -.
HPA; CAB033691; -.
HPA; HPA042661; -.
MIM; 605872; gene.
neXtProt; NX_Q9H2X3; -.
OpenTargets; ENSG00000104938; -.
PharmGKB; PA26200; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00760000118924; -.
HOVERGEN; HBG050992; -.
InParanoid; Q9H2X3; -.
KO; K06563; -.
OMA; DNYWICK; -.
OrthoDB; EOG091G0G9W; -.
PhylomeDB; Q9H2X3; -.
TreeFam; TF333341; -.
EvolutionaryTrace; Q9H2X3; -.
GeneWiki; CLEC4M; -.
GenomeRNAi; 10332; -.
PRO; PR:Q9H2X3; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104938; -.
ExpressionAtlas; Q9H2X3; baseline and differential.
Genevisible; Q9H2X3; HS.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; TAS:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
GO; GO:0030246; F:carbohydrate binding; NAS:UniProtKB.
GO; GO:0030369; F:ICAM-3 receptor activity; NAS:UniProtKB.
GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042605; F:peptide antigen binding; NAS:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
GO; GO:0046790; F:virion binding; TAS:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IDA:CACAO.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0019882; P:antigen processing and presentation; NAS:UniProtKB.
GO; GO:0009988; P:cell-cell recognition; TAS:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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: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 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 1 399 C-type lectin domain family 4 member M.
/FTId=PRO_0000046626.
TOPO_DOM 1 49 Cytoplasmic. {ECO:0000305}.
TRANSMEM 50 70 Helical; Signal-anchor for type II
membrane protein. {ECO:0000305}.
TOPO_DOM 71 399 Extracellular. {ECO:0000305}.
REPEAT 108 130 1.
REPEAT 131 153 2.
REPEAT 154 176 3.
REPEAT 177 199 4.
REPEAT 200 222 5.
REPEAT 223 245 6.
REPEAT 246 268 7.
DOMAIN 274 390 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
REGION 108 269 7 X approximate tandem repeats.
MOTIF 14 15 Endocytosis signal. {ECO:0000250}.
METAL 359 359 Calcium.
METAL 361 361 Calcium.
METAL 363 363 Calcium; via carbonyl oxygen.
METAL 366 366 Calcium.
METAL 377 377 Calcium.
METAL 378 378 Calcium.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 361 361 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 265 395
DISULFID 268 279
DISULFID 296 389
DISULFID 368 381
VAR_SEQ 16 43 Missing (in isoform 9 and isoform 10).
{ECO:0000303|PubMed:10072769,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_010056.
VAR_SEQ 44 71 Missing (in isoform 10).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010057.
VAR_SEQ 44 71 GCLGHGALVLQLLSFMLLAGVLVAILVQ -> VPFLLGP
(in isoform 5, isoform 6 and isoform 7).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010058.
VAR_SEQ 147 261 Missing (in isoform 7).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010059.
VAR_SEQ 170 238 Missing (in isoform 4).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010060.
VAR_SEQ 177 199 Missing (in isoform 5 and isoform 8).
{ECO:0000303|PubMed:11257134,
ECO:0000303|PubMed:11337487,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_010061.
VAR_SEQ 239 261 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:11337487}.
/FTId=VSP_010062.
VAR_SEQ 262 272 ERLCRHCPKDW -> GEFLHIKGPWA (in isoform 2,
isoform 6 and isoform 10).
{ECO:0000303|PubMed:11337487,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_010063.
VAR_SEQ 273 399 Missing (in isoform 2, isoform 6 and
isoform 10).
{ECO:0000303|PubMed:11337487,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_010064.
VAR_SEQ 313 324 NFLQLQTSRSNR -> LPAVLEQWRTQQ (in isoform
3, isoform 4 and isoform 9).
{ECO:0000303|PubMed:10072769,
ECO:0000303|PubMed:11337487}.
/FTId=VSP_010065.
VAR_SEQ 325 399 Missing (in isoform 3, isoform 4 and
isoform 9). {ECO:0000303|PubMed:10072769,
ECO:0000303|PubMed:11337487}.
/FTId=VSP_010066.
VARIANT 164 164 R -> Q (in dbSNP:rs11465376).
{ECO:0000269|PubMed:11337487}.
/FTId=VAR_050107.
VARIANT 205 205 Y -> C (in dbSNP:rs479448).
/FTId=VAR_050108.
VARIANT 251 251 Y -> C (in dbSNP:rs479448).
/FTId=VAR_050109.
VARIANT 291 291 D -> N (in dbSNP:rs2277998).
{ECO:0000269|Ref.5}.
/FTId=VAR_021957.
CONFLICT 99 99 A -> T (in Ref. 5; BAB14667).
{ECO:0000305}.
HELIX 220 232 {ECO:0000244|PDB:1SL6}.
HELIX 262 264 {ECO:0000244|PDB:1XPH}.
STRAND 273 275 {ECO:0000244|PDB:1XPH}.
STRAND 278 282 {ECO:0000244|PDB:1XPH}.
HELIX 289 298 {ECO:0000244|PDB:1XPH}.
HELIX 309 322 {ECO:0000244|PDB:1XPH}.
STRAND 326 331 {ECO:0000244|PDB:1XPH}.
STRAND 333 335 {ECO:0000244|PDB:1K9J}.
HELIX 349 354 {ECO:0000244|PDB:1XPH}.
STRAND 362 365 {ECO:0000244|PDB:1XAR}.
STRAND 368 372 {ECO:0000244|PDB:1XPH}.
STRAND 375 379 {ECO:0000244|PDB:1XPH}.
STRAND 385 392 {ECO:0000244|PDB:1XPH}.
SEQUENCE 399 AA; 45350 MW; 0FADC99F72AEA593 CRC64;
MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTGCLGHGA LVLQLLSFML
LAGVLVAILV QVSKVPSSLS QEQSEQDAIY QNLTQLKAAV GELSEKSKLQ EIYQELTQLK
AAVGELPEKS KLQEIYQELT RLKAAVGELP EKSKLQEIYQ ELTRLKAAVG ELPEKSKLQE
IYQELTRLKA AVGELPEKSK LQEIYQELTE LKAAVGELPE KSKLQEIYQE LTQLKAAVGE
LPDQSKQQQI YQELTDLKTA FERLCRHCPK DWTFFQGNCY FMSNSQRNWH DSVTACQEVR
AQLVVIKTAE EQNFLQLQTS RSNRFSWMGL SDLNQEGTWQ WVDGSPLSPS FQRYWNSGEP
NNSGNEDCAE FSGSGWNDNR CDVDNYWICK KPAACFRDE


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