CD209_HUMAN » CD209 antigen

CD209_HUMAN » CD209 antigen
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
CD209_HUMAN » CD209 antigen » C-type lectin domain family 4 member L;Dendritic cell-specific ICAM-3-grabbing non-integrin 1;DC-SIGN; DC-SIGN1;
Hydrophobic Thickness 29.2 ± 3.8 Å
Tilt Angle 3 ± 1°
ΔGtransfer -19.8 kcal/mol
ΔGfold -11.1 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology In
TM Segments 43-63 (40-63)
Pathways

Measles (KEGG)

Phagosome (KEGG)

Tuberculosis (KEGG)

PDB 1sl5 (250-388), 2it5 (250-388), 1sl4 (250-404), 2it6 (250-404), 2xr6 (250-404), 2b6b (251-404), 2xr5 (254-404), 1k9i (A/B...=250-404)
OPM none
Complexes

CD209:CD209_HUMAN

Interactions

CD209, Complex: Oligomer of CD209 antigen, PDBID: 1K9I

CEAM1, Complex: CEAM1:CD209, PubMed

CLC4M, Complex: CLC4M:CD209, PubMed

ICAM2, Complex: CD209:ICAM2, PubMed

ICAM3, Complex: CD209:ICAM3, PubMed

ITAM, Complex: CD209:ITAM, PubMed

Domains

AA: 273-379, PDBID: 1K9I, Subunit G, Seq Identity:100%, Lectin C-type domain

UniProt annotation for CD209_HUMAN » CD209 antigen
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. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, cytomegalovirus gB, HCV E2, dengue virus gE, 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.

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.

SUBUNIT: Homotetramer. Binds to many viral surface glycoproteins such as HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus envelope glycoproteins, cytomegalovirus gB, HCV E2 and dengue virus major envelope protein E. Interacts with C1QBP; the interaction is indicative for a C1q:C1QBP:CD209 signaling complex.

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.

DOMAIN: The tandem repeat domain, also called neck domain, mediates oligomerization.

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.

UniProt features for CD209_HUMAN » CD209 antigen
CHAIN 1 404 CD209 antigen.
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.
REGION 96 257 7 X approximate tandem repeats.
MOTIF 14 15 Endocytosis signal.
MOTIF 16 18 Endocytosis signal (Potential).
MOTIF 31 34 Endocytosis signal (Potential).
DISULFID 256 267
DISULFID 284 377
DISULFID 356 369
Amino Acid Sequence for CD209_HUMAN » CD209 antigen
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