Q9H2X3 (CLC4M_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
C-type lectin domain family 4 member M

Alternative name(s):
CD209 antigen-like protein 1
DC-SIGN-related protein
Short name=DC-SIGNR
Dendritic cell-specific ICAM-3-grabbing non-integrin 2
Short name=DC-SIGN2
Liver/lymph node-specific ICAM-3-grabbing non-integrin
Short name=L-SIGN
CD_antigen=CD299

Gene names

Name:	CLEC4M
Synonyms:	CD209L, CD209L1, CD299

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	399 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. 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, HCV E2, and human SARS coronavirus protein S. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. Is presumably a coreceptor for the SARS coronavirus. Ref.4 Ref.9
Subunit structure	Homotetramer. Binds to many viral surface glycoproteins such as HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus S protein. Ref.4 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Isoform 1: Cell membrane; Single-pass type II membrane protein Potential. Isoform 2: Cell membrane; Single-pass type II membrane protein Potential. Isoform 3: Cell membrane; Single-pass type II membrane protein Potential. Isoform 5: Secreted Potential. Isoform 6: Secreted Potential. Isoform 7: Secreted Potential. Isoform 10: Secreted Potential.
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. Ref.4 Ref.9 Ref.13
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 similarities	Contains 1 C-type lectin domain.
Sequence caution	The sequence AAR04559.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
Biological process	Adaptive immunity 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.3. Source: UniProtKB endocytosis Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW intracellular signal transduction Non-traceable author statement Ref.3. Source: UniProtKB intracellular virion transport Traceable author statement Ref.3. Source: UniProtKB leukocyte cell-cell adhesion Non-traceable author statement Ref.3. Source: UniProtKB peptide antigen transport Non-traceable author statement Ref.3. Source: UniProtKB viral attachment to host cell Traceable author statement Ref.3. Source: UniProtKB viral genome replication Non-traceable author statement Ref.3. Source: UniProtKB
Cellular_component	cytoplasm Non-traceable author statement Ref.3. Source: UniProtKB extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	ICAM-3 receptor activity Non-traceable author statement Ref.4. Source: UniProtKB carbohydrate binding Non-traceable author statement Ref.3. Source: UniProtKB mannose binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptide antigen binding Non-traceable author statement Ref.3. Source: UniProtKB virion binding Traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]

Note: 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.

Isoform 1 (identifier: Q9H2X3-1)

Also known as: mDC-SIGN2 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: Q9H2X3-2)

Also known as: mDC-SIGN2 type III; mDC-SIGN2 type IV;

The sequence of this isoform differs from the canonical sequence as follows:
     262-272: ERLCRHCPKDW → GEFLHIKGPWA
     273-399: Missing.

Note: May be due to intron retention.

Isoform 3 (identifier: Q9H2X3-3)

Also known as: mDC-SIGN2 type V;

The sequence of this isoform differs from the canonical sequence as follows:
     313-324: NFLQLQTSRSNR → LPAVLEQWRTQQ
     325-399: Missing.

Isoform 4 (identifier: Q9H2X3-4)

Also known as: mDC-SIGN2 type VI;

The sequence of this isoform differs from the canonical sequence as follows:
     170-238: Missing.
     239-261: Missing.
     313-324: NFLQLQTSRSNR → LPAVLEQWRTQQ
     325-399: Missing.

Isoform 5 (identifier: Q9H2X3-5)

Also known as: sDC-SIGN2 type I;

The sequence of this isoform differs from the canonical sequence as follows:
     44-71: GCLGHGALVLQLLSFMLLAGVLVAILVQ → VPFLLGP
     177-199: Missing.
     239-261: Missing.

Isoform 6 (identifier: Q9H2X3-6)

Also known as: sDC-SIGN2 type II;

The sequence of this isoform differs from the canonical sequence as follows:
     44-71: GCLGHGALVLQLLSFMLLAGVLVAILVQ → VPFLLGP
     262-272: ERLCRHCPKDW → GEFLHIKGPWA
     273-399: Missing.

Note: May be due to intron retention.

Isoform 7 (identifier: Q9H2X3-7)

Also known as: sDC-SIGN2 type III;

The sequence of this isoform differs from the canonical sequence as follows:
     44-71: GCLGHGALVLQLLSFMLLAGVLVAILVQ → VPFLLGP
     147-261: Missing.

Isoform 8 (identifier: Q9H2X3-8)

The sequence of this isoform differs from the canonical sequence as follows:
     177-199: Missing.

Note: Non-canonical intron-exon splice junction.

Isoform 9 (identifier: Q9H2X3-9)

The sequence of this isoform differs from the canonical sequence as follows:
     16-43: Missing.
     313-324: NFLQLQTSRSNR → LPAVLEQWRTQQ
     325-399: Missing.

Isoform 10 (identifier: Q9H2X3-10)

The sequence of this isoform differs from the canonical sequence as follows:
     16-43: Missing.
     44-71: Missing.
     262-272: ERLCRHCPKDW → GEFLHIKGPWA
     273-399: Missing.

Note: May be due to intron retention.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 399

399

C-type lectin domain family 4 member M

PRO_0000046626

Regions

Topological domain

1 – 49

49

Cytoplasmic Probable

Transmembrane

50 – 70

21

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

Topological domain

71 – 399

329

Extracellular Probable

Repeat

108 – 130

23

1

Repeat

131 – 153

23

2

Repeat

154 – 176

23

3

Repeat

177 – 199

23

4

Repeat

200 – 222

23

5

Repeat

223 – 245

23

6

Repeat

246 – 268

23

7

Domain

274 – 390

117

C-type lectin

Region

108 – 269

162

7 X approximate tandem repeats

Motif

14 – 15

2

Endocytosis signal By similarity

Sites

Metal binding

359

1

Calcium

Metal binding

361

1

Calcium

Metal binding

363

1

Calcium; via carbonyl oxygen

Metal binding

366

1

Calcium

Metal binding

377

1

Calcium

Metal binding

378

1

Calcium

Amino acid modifications

Glycosylation

92

1

N-linked (GlcNAc...) Potential

Glycosylation

361

1

N-linked (GlcNAc...) Potential

Disulfide bond

265 ↔ 395

Ref.15 Ref.16

Disulfide bond

268 ↔ 279

Ref.15 Ref.16

Disulfide bond

296 ↔ 389

Ref.15 Ref.16

Disulfide bond

368 ↔ 381

Ref.15 Ref.16

Natural variations

Alternative sequence

16 – 43

28

Missing in isoform 9 and isoform 10.

VSP_010056

Alternative sequence

44 – 71

28

Missing in isoform 10.

VSP_010057

Alternative sequence

44 – 71

28

GCLGH…AILVQ → VPFLLGP in isoform 5, isoform 6 and isoform 7.

VSP_010058

Alternative sequence

147 – 261

115

Missing in isoform 7.

VSP_010059

Alternative sequence

170 – 238

69

Missing in isoform 4.

VSP_010060

Alternative sequence

177 – 199

23

Missing in isoform 5 and isoform 8.

VSP_010061

Alternative sequence

239 – 261

23

Missing in isoform 4 and isoform 5.

VSP_010062

Alternative sequence

262 – 272

11

ERLCRHCPKDW → GEFLHIKGPWA in isoform 2, isoform 6 and isoform 10.

VSP_010063

Alternative sequence

273 – 399

127

Missing in isoform 2, isoform 6 and isoform 10.

VSP_010064

Alternative sequence

313 – 324

12

NFLQL…SRSNR → LPAVLEQWRTQQ in isoform 3, isoform 4 and isoform 9.

VSP_010065

Alternative sequence

325 – 399

75

Missing in isoform 3, isoform 4 and isoform 9.

VSP_010066

Natural variant

164

1

R → Q. Ref.3
Corresponds to variant rs11465376 [ dbSNP | Ensembl ].

VAR_050107

Natural variant

205

1

Y → C.
Corresponds to variant rs479448 [ dbSNP | Ensembl ].

VAR_050108

Natural variant

251

1

Y → C.
Corresponds to variant rs479448 [ dbSNP | Ensembl ].

VAR_050109

Natural variant

291

1

D → N. Ref.5
Corresponds to variant rs2277998 [ dbSNP | Ensembl ].

VAR_021957

Experimental info

Sequence conflict

99

1

A → T in BAB14667. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

399

Helix Strand Turn

Details...

Helix

220 – 232

13

Helix

262 – 264

3

Beta strand

273 – 275

3

Beta strand

278 – 282

5

Helix

289 – 298

10

Helix

309 – 322

14

Beta strand

326 – 331

6

Beta strand

333 – 335

3

Helix

349 – 354

6

Beta strand

362 – 365

4

Beta strand

368 – 372

5

Beta strand

375 – 379

5

Beta strand

385 – 392

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (mDC-SIGN2 type I) [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 0FADC99F72AEA593	FASTA	399	45,350
	10 20 30 40 50 60 MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTGCLGHGA LVLQLLSFML 70 80 90 100 110 120 LAGVLVAILV QVSKVPSSLS QEQSEQDAIY QNLTQLKAAV GELSEKSKLQ EIYQELTQLK 130 140 150 160 170 180 AAVGELPEKS KLQEIYQELT RLKAAVGELP EKSKLQEIYQ ELTRLKAAVG ELPEKSKLQE 190 200 210 220 230 240 IYQELTRLKA AVGELPEKSK LQEIYQELTE LKAAVGELPE KSKLQEIYQE LTQLKAAVGE 250 260 270 280 290 300 LPDQSKQQQI YQELTDLKTA FERLCRHCPK DWTFFQGNCY FMSNSQRNWH DSVTACQEVR 310 320 330 340 350 360 AQLVVIKTAE EQNFLQLQTS RSNRFSWMGL SDLNQEGTWQ WVDGSPLSPS FQRYWNSGEP 370 380 390 NNSGNEDCAE FSGSGWNDNR CDVDNYWICK KPAACFRDE
	Isoform 2 (mDC-SIGN2 type III) (mDC-SIGN2 type IV) [UniParc]. Checksum: B26BE2F2DE541F5E	FASTA	272	30,481
	10 20 30 40 50 60 MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTGCLGHGA LVLQLLSFML 70 80 90 100 110 120 LAGVLVAILV QVSKVPSSLS QEQSEQDAIY QNLTQLKAAV GELSEKSKLQ EIYQELTQLK 130 140 150 160 170 180 AAVGELPEKS KLQEIYQELT RLKAAVGELP EKSKLQEIYQ ELTRLKAAVG ELPEKSKLQE 190 200 210 220 230 240 IYQELTRLKA AVGELPEKSK LQEIYQELTE LKAAVGELPE KSKLQEIYQE LTQLKAAVGE 250 260 270 LPDQSKQQQI YQELTDLKTA FGEFLHIKGP WA
	Isoform 3 (mDC-SIGN2 type V) [UniParc]. Checksum: B22BD6E0C926649A	FASTA	324	36,769
	10 20 30 40 50 60 MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTGCLGHGA LVLQLLSFML 70 80 90 100 110 120 LAGVLVAILV QVSKVPSSLS QEQSEQDAIY QNLTQLKAAV GELSEKSKLQ EIYQELTQLK 130 140 150 160 170 180 AAVGELPEKS KLQEIYQELT RLKAAVGELP EKSKLQEIYQ ELTRLKAAVG ELPEKSKLQE 190 200 210 220 230 240 IYQELTRLKA AVGELPEKSK LQEIYQELTE LKAAVGELPE KSKLQEIYQE LTQLKAAVGE 250 260 270 280 290 300 LPDQSKQQQI YQELTDLKTA FERLCRHCPK DWTFFQGNCY FMSNSQRNWH DSVTACQEVR 310 320 AQLVVIKTAE EQLPAVLEQW RTQQ
	Isoform 4 (mDC-SIGN2 type VI) [UniParc]. Checksum: B50EB1500097CB70	FASTA	232	26,283
	10 20 30 40 50 60 MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTGCLGHGA LVLQLLSFML 70 80 90 100 110 120 LAGVLVAILV QVSKVPSSLS QEQSEQDAIY QNLTQLKAAV GELSEKSKLQ EIYQELTQLK 130 140 150 160 170 180 AAVGELPEKS KLQEIYQELT RLKAAVGELP EKSKLQEIYQ ELTRLKAAVE RLCRHCPKDW 190 200 210 220 230 TFFQGNCYFM SNSQRNWHDS VTACQEVRAQ LVVIKTAEEQ LPAVLEQWRT QQ
	Isoform 5 (sDC-SIGN2 type I) [UniParc]. Checksum: C6FDEF92C1B073C6	FASTA	332	37,954
	10 20 30 40 50 60 MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTVPFLLGP VSKVPSSLSQ 70 80 90 100 110 120 EQSEQDAIYQ NLTQLKAAVG ELSEKSKLQE IYQELTQLKA AVGELPEKSK LQEIYQELTR 130 140 150 160 170 180 LKAAVGELPE KSKLQEIYQE LTRLKAAVGE LPEKSKLQEI YQELTELKAA VGELPEKSKL 190 200 210 220 230 240 QEIYQELTQL KAAVERLCRH CPKDWTFFQG NCYFMSNSQR NWHDSVTACQ EVRAQLVVIK 250 260 270 280 290 300 TAEEQNFLQL QTSRSNRFSW MGLSDLNQEG TWQWVDGSPL SPSFQRYWNS GEPNNSGNED 310 320 330 CAEFSGSGWN DNRCDVDNYW ICKKPAACFR DE
	Isoform 6 (sDC-SIGN2 type II) [UniParc]. Checksum: 86F69F6CD6055D6E	FASTA	251	28,373
	10 20 30 40 50 60 MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTVPFLLGP VSKVPSSLSQ 70 80 90 100 110 120 EQSEQDAIYQ NLTQLKAAVG ELSEKSKLQE IYQELTQLKA AVGELPEKSK LQEIYQELTR 130 140 150 160 170 180 LKAAVGELPE KSKLQEIYQE LTRLKAAVGE LPEKSKLQEI YQELTRLKAA VGELPEKSKL 190 200 210 220 230 240 QEIYQELTEL KAAVGELPEK SKLQEIYQEL TQLKAAVGEL PDQSKQQQIY QELTDLKTAF 250 GEFLHIKGPW A
	Isoform 7 (sDC-SIGN2 type III) [UniParc]. Checksum: 2BB0AAF2C506495E	FASTA	263	30,131
	10 20 30 40 50 60 MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTVPFLLGP VSKVPSSLSQ 70 80 90 100 110 120 EQSEQDAIYQ NLTQLKAAVG ELSEKSKLQE IYQELTQLKA AVGELPEKSK LQEIYQELTR 130 140 150 160 170 180 LKAAVERLCR HCPKDWTFFQ GNCYFMSNSQ RNWHDSVTAC QEVRAQLVVI KTAEEQNFLQ 190 200 210 220 230 240 LQTSRSNRFS WMGLSDLNQE GTWQWVDGSP LSPSFQRYWN SGEPNNSGNE DCAEFSGSGW 250 260 NDNRCDVDNY WICKKPAACF RDE
	Isoform 8 [UniParc]. Checksum: 36CB19991F23BE90	FASTA	376	42,724
	10 20 30 40 50 60 MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTGCLGHGA LVLQLLSFML 70 80 90 100 110 120 LAGVLVAILV QVSKVPSSLS QEQSEQDAIY QNLTQLKAAV GELSEKSKLQ EIYQELTQLK 130 140 150 160 170 180 AAVGELPEKS KLQEIYQELT RLKAAVGELP EKSKLQEIYQ ELTRLKAAVG ELPEKSKLQE 190 200 210 220 230 240 IYQELTELKA AVGELPEKSK LQEIYQELTQ LKAAVGELPD QSKQQQIYQE LTDLKTAFER 250 260 270 280 290 300 LCRHCPKDWT FFQGNCYFMS NSQRNWHDSV TACQEVRAQL VVIKTAEEQN FLQLQTSRSN 310 320 330 340 350 360 RFSWMGLSDL NQEGTWQWVD GSPLSPSFQR YWNSGEPNNS GNEDCAEFSG SGWNDNRCDV 370 DNYWICKKPA ACFRDE
	Isoform 9 [UniParc]. Checksum: 70228F848F2DE64F	FASTA	296	33,528
	10 20 30 40 50 60 MSDSKEPRVQ QLGLLGCLGH GALVLQLLSF MLLAGVLVAI LVQVSKVPSS LSQEQSEQDA 70 80 90 100 110 120 IYQNLTQLKA AVGELSEKSK LQEIYQELTQ LKAAVGELPE KSKLQEIYQE LTRLKAAVGE 130 140 150 160 170 180 LPEKSKLQEI YQELTRLKAA VGELPEKSKL QEIYQELTRL KAAVGELPEK SKLQEIYQEL 190 200 210 220 230 240 TELKAAVGEL PEKSKLQEIY QELTQLKAAV GELPDQSKQQ QIYQELTDLK TAFERLCRHC 250 260 270 280 290 PKDWTFFQGN CYFMSNSQRN WHDSVTACQE VRAQLVVIKT AEEQLPAVLE QWRTQQ
	Isoform 10 [UniParc]. Checksum: 45F01AD20E279619	FASTA	216	24,408
	10 20 30 40 50 60 MSDSKEPRVQ QLGLLVSKVP SSLSQEQSEQ DAIYQNLTQL KAAVGELSEK SKLQEIYQEL 70 80 90 100 110 120 TQLKAAVGEL PEKSKLQEIY QELTRLKAAV GELPEKSKLQ EIYQELTRLK AAVGELPEKS 130 140 150 160 170 180 KLQEIYQELT RLKAAVGELP EKSKLQEIYQ ELTELKAAVG ELPEKSKLQE IYQELTQLKA 190 200 210 AVGELPDQSK QQQIYQELTD LKTAFGEFLH IKGPWA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Selection of cDNAs encoding putative type II membrane proteins on the cell surface from a human full-length cDNA bank." Yokoyama-Kobayashi M., Yamaguchi T., Sekine S., Kato S. Gene 228:161-167(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9). Tissue: Liver.
[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 / MRNA] (ISOFORM 1).
[3]	"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; 4; 5; 6 AND 7), ALTERNATIVE SPLICING (ISOFORM 3), POLYMORPHISM, VARIANT GLN-164.
[4]	"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 8), TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH ICAM3 AND HIV-1 GP120, POLYMORPHISM.
[5]	"L-SIGN interaction with HIV-1." Bruen S., Bashirova A., Carrington M., KewalRamani V. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-291.
[6]	"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] (ISOFORMS 8 AND 10). Tissue: Placenta and Testis.
[7]	"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].
[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 1). Tissue: Brain.
[9]	"DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds to human and simian immunodeficiency viruses and activates infection in trans." Poehlmann S., Soilleux E.J., Baribaud F., Leslie G.J., Morris L.S., Trowsdale J., Lee B., Coleman N., Doms R.W. Proc. Natl. Acad. Sci. U.S.A. 98:2670-2675(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INTERACTION WITH HIV-1 GP120, ROLE IN HIV-1 INFECTION.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus." 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. Proc. Natl. Acad. Sci. U.S.A. 101:15748-15753(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SARS CORONAVIRUS S PROTEIN, TISSUE SPECIFICITY.
[14]	"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 (1.9 ANGSTROMS) OF 265-394 IN COMPLEX WITH GLCNAC(2)-MAN(3) PENTASACCHARIDE.
[15]	"Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR." Feinberg H., Guo Y., Mitchell D.A., Drickamer K., Weis W.I. J. Biol. Chem. 280:1327-1335(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 216-399, DISULFIDE BONDS.
[16]	"The structure of DC-SIGNR with a portion of its repeat domain lends insights to modeling of the receptor tetramer." Snyder G.A., Colonna M., Sun P.D. J. Mol. Biol. 347:979-989(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 250-399, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

DC-SIGNR

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB015629 mRNA. Translation: BAA76496.1.
AF245219 mRNA. Translation: AAG13848.2.
AF209481, AF209480 Genomic DNA. Translation: AAG13815.2.
AY042234 mRNA. Translation: AAK91859.1.
AY042235 mRNA. Translation: AAK91860.1.
AY042236 mRNA. Translation: AAK91861.1.
AY042237 mRNA. Translation: AAK91862.1.
AY042238 mRNA. Translation: AAK91863.1.
AY042239 mRNA. Translation: AAK91864.1.
AY042240 mRNA. Translation: AAK91865.1.
AF290887 mRNA. Translation: AAK20998.1.
AY343913 mRNA. Translation: AAR04559.1. Sequence problems.
AK023750 mRNA. Translation: BAB14667.1.
AK292278 mRNA. Translation: BAF84967.1.
AC008812 Genomic DNA. No translation available.
BC038851 mRNA. Translation: AAH38851.1.

IPI

IPI00003402.
IPI00156091.
IPI00290003.
IPI00382671.
IPI00385903.
IPI00409772.
IPI00410004.
IPI00410005.
IPI00410009.
IPI00642143.
IPI00874038.

RefSeq

NP_001138377.1. NM_001144905.1.
NP_001138378.1. NM_001144906.1.
NP_001138379.1. NM_001144907.1.
NP_001138380.1. NM_001144908.1.
NP_001138381.1. NM_001144909.1.
NP_001138382.1. NM_001144910.1.
NP_001138383.1. NM_001144911.1.
NP_055072.3. NM_014257.4.

UniGene

Hs.421437.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K9J	X-ray	1.90	A/B	262-399	[»]
1SL6	X-ray	2.25	A/B/C/D/E/F	216-399	[»]
1XAR	X-ray	2.25	A/B	216-399	[»]
1XPH	X-ray	1.41	A	250-399	[»]
1Z0Y	model	-	A/B/C/D	85-399	[»]
3JQH	X-ray	2.20	A	101-264	[»]

ProteinModelPortal

Q9H2X3.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H2X3. 1 interaction.

MINT

MINT-1489134.

PTM databases

PhosphoSite

Q9H2X3.

Polymorphism databases

DMDM

46395990.

Proteomic databases

PaxDb

Q9H2X3.

PRIDE

Q9H2X3.

Protocols and materials databases

DNASU

10332.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000327325; ENSP00000316228; ENSG00000104938.
ENST00000357361; ENSP00000349924; ENSG00000104938.
ENST00000359059; ENSP00000351954; ENSG00000104938.
ENST00000595496; ENSP00000470132; ENSG00000104938.
ENST00000596363; ENSP00000471125; ENSG00000104938.
ENST00000597522; ENSP00000471132; ENSG00000104938.

GeneID

10332.

KEGG

hsa:10332.

UCSC

uc002mhy.2. human.
uc002mhz.3. human.
uc002mia.3. human.
uc002mic.3. human.
uc002mih.3. human.
uc010dvt.3. human.
uc010xjw.2. human.

Organism-specific databases

CTD

10332.

GeneCards

GC19P007828.

HGNC

HGNC:13523. CLEC4M.

HPA

CAB033689.
CAB033691.
HPA042661.

MIM

605872. gene.

neXtProt

NX_Q9H2X3.

PharmGKB

PA26200.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG314197.

HOVERGEN

HBG050992.

InParanoid

Q9H2X3.

KO

K06563.

OMA

DNYWICK.

OrthoDB

EOG40K7ZZ.

PhylomeDB

Q9H2X3.

Gene expression databases

ArrayExpress

Q9H2X3.

Bgee

Q9H2X3.

Genevestigator

Q9H2X3.

GermOnline

ENSG00000104938. 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

EvolutionaryTrace

Q9H2X3.

GenomeRNAi

10332.

NextBio

39173.

SOURCE

Search...

Entry information

Entry name

CLC4M_HUMAN

Accession

Primary (citable) accession number: Q9H2X3
Secondary accession number(s): A6NKI4 , A8K8B3, Q69F40, Q969M4, Q96QP3, Q96QP4, Q96QP5, Q96QP6, Q9BXS3, Q9H2Q9, Q9H8F0, Q9Y2A8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 121 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.