Q9NNX6 (CD209_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CD209 antigen

Alternative name(s):
C-type lectin domain family 4 member L
Dendritic cell-specific ICAM-3-grabbing non-integrin 1
Short name=DC-SIGN
Short name=DC-SIGN1
CD_antigen=CD209

Gene names

Name:	CD209
Synonyms:	CLEC4L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.9 Ref.10 Ref.14 Ref.15 Ref.17 Ref.18 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. Ref.9 Ref.10 Ref.14 Ref.15 Ref.17 Ref.18
Subunit structure	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. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.21 Ref.23
Subcellular location	Isoform 1: Cell membrane; Single-pass type II membrane protein Probable Ref.1. Isoform 2: Cell membrane; Single-pass type II membrane protein Probable Ref.1. Isoform 3: Cell membrane; Single-pass type II membrane protein Probable Ref.1. Isoform 4: Cell membrane; Single-pass type II membrane protein Probable Ref.1. Isoform 5: Cell membrane; Single-pass type II membrane protein Probable Ref.1. Isoform 6: Secreted Probable Ref.1. Isoform 7: Secreted Probable Ref.1. Isoform 8: Secreted Probable Ref.1. Isoform 9: Secreted Probable Ref.1. Isoform 10: Secreted Probable Ref.1. Isoform 11: Secreted Probable Ref.1. Isoform 12: Secreted Probable Ref.1.
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. Ref.3 Ref.4
Domain	The tandem repeat domain, also called neck domain, mediates oligomerization.
Polymorphism	Genetic variations in CD209 determine Mycobacterium tuberculosis susceptibility [MIM:607948]. 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 similarities	Contains 1 C-type lectin domain.
Sequence caution	The sequence AAK91858.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
Biological process	Adaptive immunity Cell adhesion Endocytosis Host-virus interaction Immunity Innate immunity
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Mannose-binding Metal-binding
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell-cell recognition Traceable author statement Ref.4. Source: UniProtKB endocytosis Inferred from electronic annotation. Source: UniProtKB-KW heterophilic cell-cell adhesion Traceable author statement Ref.1. Source: UniProtKB innate immune response Inferred from electronic annotation. Source: UniProtKB-KW intracellular signal transduction Non-traceable author statement Ref.4. Source: UniProtKB intracellular virion transport Traceable author statement Ref.4. Source: UniProtKB leukocyte cell-cell adhesion Non-traceable author statement Ref.4. Source: UniProtKB peptide antigen transport Non-traceable author statement Ref.4. Source: UniProtKB regulation of T cell proliferation Inferred from direct assay PubMed 12456590. Source: MGI viral attachment to host cell Traceable author statement Ref.4. Source: UniProtKB viral genome replication Non-traceable author statement Ref.4. Source: UniProtKB
Cellular_component	cytoplasm Non-traceable author statement Ref.4. Source: UniProtKB extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Traceable author statement Ref.1. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	mannose binding Traceable author statement Ref.1. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptide antigen binding Non-traceable author statement Ref.4. Source: UniProtKB virion binding Traceable author statement Ref.4. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]

Note: 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.

Isoform 1 (identifier: Q9NNX6-1)

Also known as: mDC-SIGN1A type I;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NNX6-2)

Also known as: mDC-SIGN1A type II;

The sequence of this isoform differs from the canonical sequence as follows:
     301-306: Missing.

Isoform 3 (identifier: Q9NNX6-3)

Also known as: mDC-SIGN1A type III;

The sequence of this isoform differs from the canonical sequence as follows:
     143-235: LQEIYQELTW...VGELPEKSKQ → L

Isoform 4 (identifier: Q9NNX6-4)

Also known as: mDC-SIGN1A type IV;

The sequence of this isoform differs from the canonical sequence as follows:
     74-309: Missing.

Isoform 5 (identifier: Q9NNX6-5)

Also known as: mDC-SIGN1B type I;

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSDSKEPRLQQLGLL → MASACPGSDFTSIHS

Isoform 6 (identifier: Q9NNX6-6)

Also known as: sDC-SIGN1A type I;

The sequence of this isoform differs from the canonical sequence as follows:
     36-59: Missing.

Isoform 7 (identifier: Q9NNX6-7)

Also known as: sDC-SIGN1A type II;

The sequence of this isoform differs from the canonical sequence as follows:
     16-59: Missing.

Isoform 8 (identifier: Q9NNX6-8)

Also known as: sDC-SIGN1A type III;

The sequence of this isoform differs from the canonical sequence as follows:
     16-59: Missing.
     142-233: Missing.

Isoform 9 (identifier: Q9NNX6-9)

Also known as: sDC-SIGN1A type IV;

The sequence of this isoform differs from the canonical sequence as follows:
     30-34: GYKSL → RNQKC
     35-404: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 10 (identifier: Q9NNX6-10)

Also known as: sDC-SIGN1B type I;

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSDSKEPRLQQLGLL → MASACPGSDFTSIHS
     36-59: Missing.

Isoform 11 (identifier: Q9NNX6-11)

Also known as: sDC-SIGN1B type II;

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSDSKEPRLQQLGLL → MASACPGSDFTSIHS
     36-59: Missing.
     191-236: Missing.

Isoform 12 (identifier: Q9NNX6-12)

Also known as: sDC-SIGN1B type III;

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSDSKEPRLQQLGLL → MASACPGSDFTSIHS
     36-59: Missing.
     301-321: NFLQLQSSRSNRFTWMGLSDL → LQAVLEQRRAQQRWGGRLRGI
     322-404: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 404

404

CD209 antigen

PRO_0000046595

Regions

Topological domain

1 – 37

37

Cytoplasmic Probable

Transmembrane

38 – 58

21

Helical; Signal-anchor for type II membrane protein; Probable

Topological domain

59 – 404

346

Extracellular Probable

Repeat

96 – 118

23

1

Repeat

119 – 141

23

2

Repeat

142 – 164

23

3

Repeat

165 – 187

23

4

Repeat

188 – 210

23

5

Repeat

211 – 233

23

6

Repeat

234 – 257

24

7

Domain

263 – 378

116

C-type lectin

Region

96 – 257

162

7 X approximate tandem repeats

Motif

14 – 15

2

Endocytosis signal

Motif

16 – 18

3

Endocytosis signal Potential

Motif

31 – 34

4

Endocytosis signal Potential

Sites

Metal binding

347

1

Calcium

Metal binding

349

1

Calcium

Metal binding

351

1

Calcium; via carbonyl oxygen

Metal binding

354

1

Calcium

Metal binding

365

1

Calcium

Metal binding

366

1

Calcium

Amino acid modifications

Glycosylation

80

1

N-linked (GlcNAc...) Potential

Disulfide bond

256 ↔ 267

Disulfide bond

284 ↔ 377

Disulfide bond

356 ↔ 369

Natural variations

Alternative sequence

1 – 15

15

MSDSK…QLGLL → MASACPGSDFTSIHS in isoform 5, isoform 10, isoform 11 and isoform 12.

VSP_010037

Alternative sequence

16 – 59

44

Missing in isoform 7 and isoform 8.

VSP_010038

Alternative sequence

30 – 34

5

GYKSL → RNQKC in isoform 9.

VSP_010039

Alternative sequence

35 – 404

370

Missing in isoform 9.

VSP_010040

Alternative sequence

36 – 59

24

Missing in isoform 6, isoform 10, isoform 11 and isoform 12.

VSP_010041

Alternative sequence

74 – 309

236

Missing in isoform 4.

VSP_010042

Alternative sequence

142 – 233

92

Missing in isoform 8.

VSP_010043

Alternative sequence

143 – 235

93

LQEIY…EKSKQ → L in isoform 3.

VSP_010044

Alternative sequence

191 – 236

46

Missing in isoform 11.

VSP_010047

Alternative sequence

301 – 321

21

NFLQL…GLSDL → LQAVLEQRRAQQRWGGRLRG I in isoform 12.

VSP_010048

Alternative sequence

301 – 306

6

Missing in isoform 2.

VSP_010049

Alternative sequence

322 – 404

83

Missing in isoform 12.

VSP_010050

Natural variant

168

1

E → D.
Corresponds to variant rs11465377 [ dbSNP | Ensembl ].

VAR_050104

Natural variant

214

1

E → D.
Corresponds to variant rs11465377 [ dbSNP | Ensembl ].

VAR_036689

Natural variant

242

1

L → V.
Corresponds to variant rs11465380 [ dbSNP | Ensembl ].

VAR_036690

Natural variant

382

1

A → S.
Corresponds to variant rs11465393 [ dbSNP | Ensembl ].

VAR_050105

Experimental info

Mutagenesis

14 – 15

2

LL → AA: Loss of antigen internalization by endocytosis. Ref.14

Mutagenesis

320

1

D → A: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14

Mutagenesis

324

1

E → A: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14

Mutagenesis

347

1

E → Q: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14

Mutagenesis

349

1

N → D: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14

Mutagenesis

350

1

N → A: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14

Mutagenesis

355

1

D → A: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14

Mutagenesis

365

1

N → D: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14

Mutagenesis

366

1

D → A: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

404

Helix Strand Turn

Details...

Beta strand

261 – 263

3

Beta strand

266 – 270

5

Helix

277 – 286

10

Helix

297 – 310

14

Beta strand

314 – 323

10

Beta strand

326 – 329

4

Helix

337 – 342

6

Beta strand

356 – 360

5

Beta strand

363 – 367

5

Beta strand

373 – 380

8

Turn

381 – 383

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (mDC-SIGN1A type I) [UniParc]. Last modified October 1, 2000. Version 1. Checksum: A23FA246014533C0	FASTA	404	45,775
	10 20 30 40 50 60 MSDSKEPRLQ QLGLLEEEQL RGLGFRQTRG YKSLAGCLGH GPLVLQLLSF TLLAGLLVQV 70 80 90 100 110 120 SKVPSSISQE QSRQDAIYQN LTQLKAAVGE LSEKSKLQEI YQELTQLKAA VGELPEKSKL 130 140 150 160 170 180 QEIYQELTRL KAAVGELPEK SKLQEIYQEL TWLKAAVGEL PEKSKMQEIY QELTRLKAAV 190 200 210 220 230 240 GELPEKSKQQ EIYQELTRLK AAVGELPEKS KQQEIYQELT RLKAAVGELP EKSKQQEIYQ 250 260 270 280 290 300 ELTQLKAAVE RLCHPCPWEW TFFQGNCYFM SNSQRNWHDS ITACKEVGAQ LVVIKSAEEQ 310 320 330 340 350 360 NFLQLQSSRS NRFTWMGLSD LNQEGTWQWV DGSPLLPSFK QYWNRGEPNN VGEEDCAEFS 370 380 390 400 GNGWNDDKCN LAKFWICKKS AASCSRDEEQ FLSPAPATPN PPPA
	Isoform 2 (mDC-SIGN1A type II) [UniParc]. Checksum: D925764886701D2E	FASTA	398	45,031
	10 20 30 40 50 60 MSDSKEPRLQ QLGLLEEEQL RGLGFRQTRG YKSLAGCLGH GPLVLQLLSF TLLAGLLVQV 70 80 90 100 110 120 SKVPSSISQE QSRQDAIYQN LTQLKAAVGE LSEKSKLQEI YQELTQLKAA VGELPEKSKL 130 140 150 160 170 180 QEIYQELTRL KAAVGELPEK SKLQEIYQEL TWLKAAVGEL PEKSKMQEIY QELTRLKAAV 190 200 210 220 230 240 GELPEKSKQQ EIYQELTRLK AAVGELPEKS KQQEIYQELT RLKAAVGELP EKSKQQEIYQ 250 260 270 280 290 300 ELTQLKAAVE RLCHPCPWEW TFFQGNCYFM SNSQRNWHDS ITACKEVGAQ LVVIKSAEEQ 310 320 330 340 350 360 SSRSNRFTWM GLSDLNQEGT WQWVDGSPLL PSFKQYWNRG EPNNVGEEDC AEFSGNGWND 370 380 390 DKCNLAKFWI CKKSAASCSR DEEQFLSPAP ATPNPPPA
	Isoform 3 (mDC-SIGN1A type III) [UniParc]. Checksum: 95761618EF36AFBE	FASTA	312	35,178
	10 20 30 40 50 60 MSDSKEPRLQ QLGLLEEEQL RGLGFRQTRG YKSLAGCLGH GPLVLQLLSF TLLAGLLVQV 70 80 90 100 110 120 SKVPSSISQE QSRQDAIYQN LTQLKAAVGE LSEKSKLQEI YQELTQLKAA VGELPEKSKL 130 140 150 160 170 180 QEIYQELTRL KAAVGELPEK SKLQEIYQEL TQLKAAVERL CHPCPWEWTF FQGNCYFMSN 190 200 210 220 230 240 SQRNWHDSIT ACKEVGAQLV VIKSAEEQNF LQLQSSRSNR FTWMGLSDLN QEGTWQWVDG 250 260 270 280 290 300 SPLLPSFKQY WNRGEPNNVG EEDCAEFSGN GWNDDKCNLA KFWICKKSAA SCSRDEEQFL 310 SPAPATPNPP PA
	Isoform 4 (mDC-SIGN1A type IV) [UniParc]. Checksum: 901718CE96B9F59C	FASTA	168	18,646
	10 20 30 40 50 60 MSDSKEPRLQ QLGLLEEEQL RGLGFRQTRG YKSLAGCLGH GPLVLQLLSF TLLAGLLVQV 70 80 90 100 110 120 SKVPSSISQE QSRSNRFTWM GLSDLNQEGT WQWVDGSPLL PSFKQYWNRG EPNNVGEEDC 130 140 150 160 AEFSGNGWND DKCNLAKFWI CKKSAASCSR DEEQFLSPAP ATPNPPPA
	Isoform 5 (mDC-SIGN1B type I) [UniParc]. Checksum: D4D570727D9DCC30	FASTA	404	45,571
	10 20 30 40 50 60 MASACPGSDF TSIHSEEEQL RGLGFRQTRG YKSLAGCLGH GPLVLQLLSF TLLAGLLVQV 70 80 90 100 110 120 SKVPSSISQE QSRQDAIYQN LTQLKAAVGE LSEKSKLQEI YQELTQLKAA VGELPEKSKL 130 140 150 160 170 180 QEIYQELTRL KAAVGELPEK SKLQEIYQEL TWLKAAVGEL PEKSKMQEIY QELTRLKAAV 190 200 210 220 230 240 GELPEKSKQQ EIYQELTRLK AAVGELPEKS KQQEIYQELT RLKAAVGELP EKSKQQEIYQ 250 260 270 280 290 300 ELTQLKAAVE RLCHPCPWEW TFFQGNCYFM SNSQRNWHDS ITACKEVGAQ LVVIKSAEEQ 310 320 330 340 350 360 NFLQLQSSRS NRFTWMGLSD LNQEGTWQWV DGSPLLPSFK QYWNRGEPNN VGEEDCAEFS 370 380 390 400 GNGWNDDKCN LAKFWICKKS AASCSRDEEQ FLSPAPATPN PPPA
	Isoform 6 (sDC-SIGN1A type I) [UniParc]. Checksum: BCF9CC45ABEF6B02	FASTA	380	43,330
	10 20 30 40 50 60 MSDSKEPRLQ QLGLLEEEQL RGLGFRQTRG YKSLAVSKVP SSISQEQSRQ DAIYQNLTQL 70 80 90 100 110 120 KAAVGELSEK SKLQEIYQEL TQLKAAVGEL PEKSKLQEIY QELTRLKAAV GELPEKSKLQ 130 140 150 160 170 180 EIYQELTWLK AAVGELPEKS KMQEIYQELT RLKAAVGELP EKSKQQEIYQ ELTRLKAAVG 190 200 210 220 230 240 ELPEKSKQQE IYQELTRLKA AVGELPEKSK QQEIYQELTQ LKAAVERLCH PCPWEWTFFQ 250 260 270 280 290 300 GNCYFMSNSQ RNWHDSITAC KEVGAQLVVI KSAEEQNFLQ LQSSRSNRFT WMGLSDLNQE 310 320 330 340 350 360 GTWQWVDGSP LLPSFKQYWN RGEPNNVGEE DCAEFSGNGW NDDKCNLAKF WICKKSAASC 370 380 SRDEEQFLSP APATPNPPPA
	Isoform 7 (sDC-SIGN1A type II) [UniParc]. Checksum: 6ABE2B9AAEDFAAA8	FASTA	360	41,009
	10 20 30 40 50 60 MSDSKEPRLQ QLGLLVSKVP SSISQEQSRQ DAIYQNLTQL KAAVGELSEK SKLQEIYQEL 70 80 90 100 110 120 TQLKAAVGEL PEKSKLQEIY QELTRLKAAV GELPEKSKLQ EIYQELTWLK AAVGELPEKS 130 140 150 160 170 180 KMQEIYQELT RLKAAVGELP EKSKQQEIYQ ELTRLKAAVG ELPEKSKQQE IYQELTRLKA 190 200 210 220 230 240 AVGELPEKSK QQEIYQELTQ LKAAVERLCH PCPWEWTFFQ GNCYFMSNSQ RNWHDSITAC 250 260 270 280 290 300 KEVGAQLVVI KSAEEQNFLQ LQSSRSNRFT WMGLSDLNQE GTWQWVDGSP LLPSFKQYWN 310 320 330 340 350 360 RGEPNNVGEE DCAEFSGNGW NDDKCNLAKF WICKKSAASC SRDEEQFLSP APATPNPPPA
	Isoform 8 (sDC-SIGN1A type III) [UniParc]. Checksum: 113E1ED1B5748693	FASTA	268	30,427
	10 20 30 40 50 60 MSDSKEPRLQ QLGLLVSKVP SSISQEQSRQ DAIYQNLTQL KAAVGELSEK SKLQEIYQEL 70 80 90 100 110 120 TQLKAAVGEL PEKSKLQEIY QELTRLKAAV GELPEKSKQQ EIYQELTQLK AAVERLCHPC 130 140 150 160 170 180 PWEWTFFQGN CYFMSNSQRN WHDSITACKE VGAQLVVIKS AEEQNFLQLQ SSRSNRFTWM 190 200 210 220 230 240 GLSDLNQEGT WQWVDGSPLL PSFKQYWNRG EPNNVGEEDC AEFSGNGWND DKCNLAKFWI 250 260 CKKSAASCSR DEEQFLSPAP ATPNPPPA
	Isoform 9 (sDC-SIGN1A type IV) [UniParc]. Checksum: 51F5A6911CDAC150	FASTA	34	4,046
	10 20 30 MSDSKEPRLQ QLGLLEEEQL RGLGFRQTRR NQKC
	Isoform 10 (sDC-SIGN1B type I) [UniParc]. Checksum: F3D098F9FB7D044B	FASTA	380	43,126
	10 20 30 40 50 60 MASACPGSDF TSIHSEEEQL RGLGFRQTRG YKSLAVSKVP SSISQEQSRQ DAIYQNLTQL 70 80 90 100 110 120 KAAVGELSEK SKLQEIYQEL TQLKAAVGEL PEKSKLQEIY QELTRLKAAV GELPEKSKLQ 130 140 150 160 170 180 EIYQELTWLK AAVGELPEKS KMQEIYQELT RLKAAVGELP EKSKQQEIYQ ELTRLKAAVG 190 200 210 220 230 240 ELPEKSKQQE IYQELTRLKA AVGELPEKSK QQEIYQELTQ LKAAVERLCH PCPWEWTFFQ 250 260 270 280 290 300 GNCYFMSNSQ RNWHDSITAC KEVGAQLVVI KSAEEQNFLQ LQSSRSNRFT WMGLSDLNQE 310 320 330 340 350 360 GTWQWVDGSP LLPSFKQYWN RGEPNNVGEE DCAEFSGNGW NDDKCNLAKF WICKKSAASC 370 380 SRDEEQFLSP APATPNPPPA
	Isoform 11 (sDC-SIGN1B type II) [UniParc]. Checksum: 8E796FC4111C86BF	FASTA	334	37,844
	10 20 30 40 50 60 MASACPGSDF TSIHSEEEQL RGLGFRQTRG YKSLAVSKVP SSISQEQSRQ DAIYQNLTQL 70 80 90 100 110 120 KAAVGELSEK SKLQEIYQEL TQLKAAVGEL PEKSKLQEIY QELTRLKAAV GELPEKSKLQ 130 140 150 160 170 180 EIYQELTWLK AAVGELPEKS KMQEIYQELT RLKAAVGELP EKSKQQEIYQ ELTQLKAAVE 190 200 210 220 230 240 RLCHPCPWEW TFFQGNCYFM SNSQRNWHDS ITACKEVGAQ LVVIKSAEEQ NFLQLQSSRS 250 260 270 280 290 300 NRFTWMGLSD LNQEGTWQWV DGSPLLPSFK QYWNRGEPNN VGEEDCAEFS GNGWNDDKCN 310 320 330 LAKFWICKKS AASCSRDEEQ FLSPAPATPN PPPA
	Isoform 12 (sDC-SIGN1B type III) [UniParc]. Checksum: C8C0951B915FC5BF	FASTA	297	33,874
	10 20 30 40 50 60 MASACPGSDF TSIHSEEEQL RGLGFRQTRG YKSLAVSKVP SSISQEQSRQ DAIYQNLTQL 70 80 90 100 110 120 KAAVGELSEK SKLQEIYQEL TQLKAAVGEL PEKSKLQEIY QELTRLKAAV GELPEKSKLQ 130 140 150 160 170 180 EIYQELTWLK AAVGELPEKS KMQEIYQELT RLKAAVGELP EKSKQQEIYQ ELTRLKAAVG 190 200 210 220 230 240 ELPEKSKQQE IYQELTRLKA AVGELPEKSK QQEIYQELTQ LKAAVERLCH PCPWEWTFFQ 250 260 270 280 290 GNCYFMSNSQ RNWHDSITAC KEVGAQLVVI KSAEEQLQAV LEQRRAQQRW GGRLRGI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp 120." Curtis B.M., Scharnowske S., Watson A.J. Proc. Natl. Acad. Sci. U.S.A. 89:8356-8360(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH HIV-1 GP120. Tissue: Placenta.
[2]	"DC-SIGN, a related gene, DC-SIGNR, and CD23 form a cluster on 19p13." Soilleux E.J., Barten R., Trowsdale J. J. Immunol. 165:2937-2942(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[3]	"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." 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. J. Exp. Med. 193:671-678(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[4]	"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." Mummidi S., Catano G., Lam L., Hoefle A., Telles V., Begum K., Jimenez F., Ahuja S.S., Ahuja S.K. J. Biol. Chem. 276:33196-33212(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10; 11 AND 12), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Uterus.
[6]	"The DNA sequence and biology of human chromosome 19." 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. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
[9]	"DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells." 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. Cell 100:587-597(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ICAM3.
[10]	"DC-SIGN-ICAM-2 interaction mediates dendritic cell trafficking." 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. Nat. Immunol. 1:353-357(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ICAM2.
[11]	"A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands." Mitchell D.A., Fadden A.J., Drickamer K. J. Biol. Chem. 276:28939-28945(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, LIGAND-BINDING.
[12]	"Human cytomegalovirus binding to DC-SIGN is required for dendritic cell infection and target cell trans-infection." Halary F., Amara A., Lortat-Jacob H., Messerle M., Delaunay T., Houles C., Fieschi F., Arenzana-Seisdedos F., Moreau J.-F., Dechanet-Merville J. Immunity 17:653-664(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CYTOMEGALOVIRUS GLYCOPROTEIN B (GB).
[13]	"Identification of different binding sites in the dendritic cell-specific receptor DC-SIGN for intercellular adhesion molecule 3 and HIV-1." Geijtenbeek T.B.H., van Duijnhoven G.C.F., van Vliet S.J., Krieger E., Vriend G., Figdor C.G., van Kooyk Y. J. Biol. Chem. 277:11314-11320(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ICAM 3 AND HIV-1 GP120, MUTAGENESIS OF ASP-320; GLU-324; GLU-347; ASN-349; ASN-350; ASP-355; ASN-365 AND ASP-366.
[14]	"The dendritic cell-specific adhesion receptor DC-SIGN internalizes antigen for presentation to T cells." 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. J. Immunol. 168:2118-2126(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 14-LEU-LEU-15.
[15]	"DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection." Kwon D.S., Gregorio G., Bitton N., Hendrickson W.A., Littman D.R. Immunity 16:135-144(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN HIV-1 INFECTION.
[16]	"Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR." 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. J. Virol. 77:1337-1346(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 GP120; HIV-2 GP120; SIV GP120 AND EBOLA GLYCOPROTEINS.
[17]	"Inhibition of human immunodeficiency virus type 1 Env-mediated fusion by DC-SIGN." Nobile C., Moris A., Porrot F., Sol-Foulon N., Schwartz O. J. Virol. 77:5313-5323(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HIV-1 INFECTION.
[18]	"Carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells." Appelmelk B.J., van Die I., van Vliet S.J., Vandenbroucke-Grauls C.M., Geijtenbeek T.B.H., van Kooyk Y. J. Immunol. 170:1635-1639(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"DC-SIGN: escape mechanism for pathogens." van Kooyk Y., Geijtenbeek T.B.H. Nat. Rev. Immunol. 3:697-709(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN HIV-1 INFECTION AND ON PATHOGEN BINDING.
[20]	"The role of dendritic cell C-type lectin receptors in HIV pathogenesis." Turville S., Wilkinson J., Cameron P., Dable J., Cunningham A.L. J. Leukoc. Biol. 74:710-718(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN HIV-1 INFECTION.
[21]	"L-SIGN (CD209L) and DC-SIGN (CD209) mediate transinfection of liver cells by hepatitis C virus." Cormier E.G., Durso R.J., Tsamis F., Boussemart L., Manix C., Olson W.C., Gardner J.P., Dragic T. Proc. Natl. Acad. Sci. U.S.A. 101:14067-14072(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HCV E2 GLYCOPROTEIN.
[22]	"A variant in the CD209 promoter is associated with severity of dengue disease." 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. Nat. Genet. 37:507-513(2005) [PubMed] [Europe PMC] [Abstract] Cited for: POLYMORPHISM, INVOLVEMENT IN SUSCEPTIBILITY TO DENGUE VIRUS INFECTION.
[23]	"DC-SIGN, C1q, and gC1qR form a trimolecular receptor complex on the surface of monocyte-derived immature dendritic cells." Hosszu K.K., Valentino A., Vinayagasundaram U., Vinayagasundaram R., Joyce M.G., Ji Y., Peerschke E.I., Ghebrehiwet B. Blood 120:1228-1236(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH C1QBP.
[24]	"Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR." Feinberg H., Mitchell D.A., Drickamer K., Weis W.I. Science 294:2163-2166(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 254-382 IN COMPLEX WITH GLCNAC(2)-MAN(3) PENTASACCHARIDE.
[25]	"Promoter variation in the DC-SIGN-encoding gene CD209 is associated with tuberculosis." 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. PLoS Med. 3:230-235(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MYCOBACTERIUM TUBERCULOSIS SUSCEPTIBILITY.
+	Additional computationally mapped references.

Web resources

Wikipedia

DC-SIGN entry

Functional Glycomics Gateway - Glycan Binding

DC-SIGN

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M98457 mRNA. Translation: AAF77072.1.
AF209479 Genomic DNA. Translation: AAG13814.1.
AF290886 mRNA. Translation: AAK20997.1.
AY042221 mRNA. Translation: AAK91846.1.
AY042222 mRNA. Translation: AAK91847.1.
AY042223 mRNA. Translation: AAK91848.1.
AY042224 mRNA. Translation: AAK91849.1.
AY042225 mRNA. Translation: AAK91850.1.
AY042226 mRNA. Translation: AAK91851.1.
AY042227 mRNA. Translation: AAK91852.1.
AY042228 mRNA. Translation: AAK91853.1.
AY042229 mRNA. Translation: AAK91854.1.
AY042230 mRNA. Translation: AAK91855.1.
AY042231 mRNA. Translation: AAK91856.1.
AY042232 mRNA. Translation: AAK91857.1.
AY042233 mRNA. Translation: AAK91858.1. Sequence problems.
AK293089 mRNA. Translation: BAF85778.1.
AC008763 Genomic DNA. No translation available.
AC008812 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW68991.1.
CH471139 Genomic DNA. Translation: EAW68993.1.
CH471139 Genomic DNA. Translation: EAW68998.1.
BC110615 mRNA. Translation: AAI10616.1.

IPI

IPI00045017.
IPI00045033.
IPI00290006.
IPI00290007.
IPI00382673.
IPI00382675.
IPI00382677.
IPI00410201.
IPI00410204.
IPI00410289.
IPI00410294.
IPI00410295.
IPI00872805.

PIR

A46274.

RefSeq

NP_001138365.1. NM_001144893.1.
NP_001138366.1. NM_001144894.1.
NP_001138367.1. NM_001144895.1.
NP_001138368.1. NM_001144896.1.
NP_001138369.1. NM_001144897.1.
NP_066978.1. NM_021155.3.

UniGene

Hs.278694.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K9I	X-ray	2.50	A/B/C/D/E/F/G/H/I/J	250-404	[»]
1SL4	X-ray	1.55	A	250-404	[»]
1SL5	X-ray	1.80	A	250-388	[»]
2B6B	electron microscopy	25.00	D	251-404	[»]
2IT5	X-ray	2.40	A	250-388	[»]
2IT6	X-ray	1.95	A	250-404	[»]
2XR5	X-ray	1.42	A	254-404	[»]
2XR6	X-ray	1.35	A	250-404	[»]

ProteinModelPortal

Q9NNX6.

ModBase

Search...

PTM databases

PhosphoSite

Q9NNX6.

Polymorphism databases

DMDM

46396012.

2D gel databases

REPRODUCTION-2DPAGE

Q9NNX6.

Proteomic databases

PaxDb

Q9NNX6.

PRIDE

Q9NNX6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000204801; ENSP00000204801; ENSG00000090659.
ENST00000301357; ENSP00000301357; ENSG00000090659.
ENST00000315591; ENSP00000315407; ENSG00000090659.
ENST00000315599; ENSP00000315477; ENSG00000090659.
ENST00000354397; ENSP00000346373; ENSG00000090659.
ENST00000394161; ENSP00000377716; ENSG00000090659.
ENST00000601256; ENSP00000470658; ENSG00000090659.
ENST00000601951; ENSP00000468827; ENSG00000090659.

GeneID

30835.

KEGG

hsa:30835.

UCSC

uc002mhq.2. human.
uc002mhr.2. human.
uc002mhs.2. human.
uc002mht.2. human.
uc002mhu.2. human.
uc002mhv.2. human.
uc002mhx.2. human.
uc010dvp.2. human.
uc010dvq.2. human.
uc010dvr.2. human.

Organism-specific databases

CTD

30835.

GeneCards

GC19M007804.

HGNC

HGNC:1641. CD209.

HPA

CAB032436.
CAB033831.

MIM

604672. gene+phenotype.
607948. phenotype.
614371. phenotype.

neXtProt

NX_Q9NNX6.

PharmGKB

PA26199.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG311341.

HOVERGEN

HBG050992.

KO

K06563.

OMA

LAKFWIC.

OrthoDB

EOG40K7ZZ.

PhylomeDB

Q9NNX6.

Gene expression databases

ArrayExpress

Q9NNX6.

Bgee

Q9NNX6.

Genevestigator

Q9NNX6.

GermOnline

ENSG00000090659. Homo sapiens.

Family and domain databases

Gene3D

3.10.100.10. 1 hit.

InterPro

IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]

Pfam

PF00059. Lectin_C. 1 hit.
[Graphical view]

SMART

SM00034. CLECT. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.

PROSITE

PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1795114.

EvolutionaryTrace

Q9NNX6.

GenomeRNAi

30835.

NextBio

52950.

SOURCE

Search...

Entry information

Entry name

CD209_HUMAN

Accession

Primary (citable) accession number: Q9NNX6
Secondary accession number(s): A8KAM4 , A8MVQ9, Q2TB19, Q96QP7, Q96QP8, Q96QP9, Q96QQ0, Q96QQ1, Q96QQ2, Q96QQ3, Q96QQ4, Q96QQ5, Q96QQ6, Q96QQ7, Q96QQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.