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Q9H2X3 (CLC4M_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processAdaptive immunity
Endocytosis
Host-virus interaction
Immunity
Innate immunity
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal-anchor
Transmembrane
Transmembrane helix
   LigandCalcium
Lectin
Mannose-binding
Metal-binding
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation

Non-traceable author statement Ref.3. Source: UniProtKB

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 transport of virus

Traceable author statement Ref.3. Source: UniProtKB

leukocyte cell-cell adhesion

Non-traceable author statement Ref.3. Source: UniProtKB

modulation by virus of host morphology or physiology

Traceable author statement Ref.3. Source: UniProtKB

peptide antigen transport

Non-traceable author statement Ref.3. Source: UniProtKB

viral genome replication

Non-traceable author statement Ref.3. Source: UniProtKB

virion attachment to host cell

Traceable author statement Ref.3. Source: UniProtKB

   Cellular_componentcytoplasm

Non-traceable author statement Ref.3. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

membrane

Traceable author statement Ref.3. Source: UniProtKB

   Molecular_functionICAM-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

receptor activity

Non-traceable author statement Ref.4. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399C-type lectin domain family 4 member M
PRO_0000046626

Regions

Topological domain1 – 4949Cytoplasmic Probable
Transmembrane50 – 7021Helical; Signal-anchor for type II membrane protein; Probable
Topological domain71 – 399329Extracellular Probable
Repeat108 – 130231
Repeat131 – 153232
Repeat154 – 176233
Repeat177 – 199234
Repeat200 – 222235
Repeat223 – 245236
Repeat246 – 268237
Domain274 – 390117C-type lectin
Region108 – 2691627 X approximate tandem repeats
Motif14 – 152Endocytosis signal By similarity

Sites

Metal binding3591Calcium
Metal binding3611Calcium
Metal binding3631Calcium; via carbonyl oxygen
Metal binding3661Calcium
Metal binding3771Calcium
Metal binding3781Calcium

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation3611N-linked (GlcNAc...) Potential
Disulfide bond265 ↔ 395 Ref.15 Ref.16
Disulfide bond268 ↔ 279 Ref.15 Ref.16
Disulfide bond296 ↔ 389 Ref.15 Ref.16
Disulfide bond368 ↔ 381 Ref.15 Ref.16

Natural variations

Alternative sequence16 – 4328Missing in isoform 9 and isoform 10.
VSP_010056
Alternative sequence44 – 7128Missing in isoform 10.
VSP_010057
Alternative sequence44 – 7128GCLGH…AILVQ → VPFLLGP in isoform 5, isoform 6 and isoform 7.
VSP_010058
Alternative sequence147 – 261115Missing in isoform 7.
VSP_010059
Alternative sequence170 – 23869Missing in isoform 4.
VSP_010060
Alternative sequence177 – 19923Missing in isoform 5 and isoform 8.
VSP_010061
Alternative sequence239 – 26123Missing in isoform 4 and isoform 5.
VSP_010062
Alternative sequence262 – 27211ERLCRHCPKDW → GEFLHIKGPWA in isoform 2, isoform 6 and isoform 10.
VSP_010063
Alternative sequence273 – 399127Missing in isoform 2, isoform 6 and isoform 10.
VSP_010064
Alternative sequence313 – 32412NFLQL…SRSNR → LPAVLEQWRTQQ in isoform 3, isoform 4 and isoform 9.
VSP_010065
Alternative sequence325 – 39975Missing in isoform 3, isoform 4 and isoform 9.
VSP_010066
Natural variant1641R → Q. Ref.3
Corresponds to variant rs11465376 [ dbSNP | Ensembl ].
VAR_050107
Natural variant2051Y → C.
Corresponds to variant rs479448 [ dbSNP | Ensembl ].
VAR_050108
Natural variant2511Y → C.
Corresponds to variant rs479448 [ dbSNP | Ensembl ].
VAR_050109
Natural variant2911D → N. Ref.5
Corresponds to variant rs2277998 [ dbSNP | Ensembl ].
VAR_021957

Experimental info

Sequence conflict991A → T in BAB14667. Ref.5

Secondary structure

........................... 399
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (mDC-SIGN2 type I) [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 0FADC99F72AEA593

FASTA39945,350
        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 

« Hide

Isoform 2 (mDC-SIGN2 type III) (mDC-SIGN2 type IV) [UniParc].

Checksum: B26BE2F2DE541F5E
Show »

FASTA27230,481
Isoform 3 (mDC-SIGN2 type V) [UniParc].

Checksum: B22BD6E0C926649A
Show »

FASTA32436,769
Isoform 4 (mDC-SIGN2 type VI) [UniParc].

Checksum: B50EB1500097CB70
Show »

FASTA23226,283
Isoform 5 (sDC-SIGN2 type I) [UniParc].

Checksum: C6FDEF92C1B073C6
Show »

FASTA33237,954
Isoform 6 (sDC-SIGN2 type II) [UniParc].

Checksum: 86F69F6CD6055D6E
Show »

FASTA25128,373
Isoform 7 (sDC-SIGN2 type III) [UniParc].

Checksum: 2BB0AAF2C506495E
Show »

FASTA26330,131
Isoform 8 [UniParc].

Checksum: 36CB19991F23BE90
Show »

FASTA37642,724
Isoform 9 [UniParc].

Checksum: 70228F848F2DE64F
Show »

FASTA29633,528
Isoform 10 [UniParc].

Checksum: 45F01AD20E279619
Show »

FASTA21624,408

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.

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.
RefSeqNP_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.
UniGeneHs.421437.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K9JX-ray1.90A/B262-399[»]
1SL6X-ray2.25A/B/C/D/E/F216-399[»]
1XARX-ray2.25A/B216-399[»]
1XPHX-ray1.41A250-399[»]
1Z0Ymodel-A/B/C/D85-399[»]
3JQHX-ray2.20A101-264[»]
ProteinModelPortalQ9H2X3.
SMRQ9H2X3. Positions 91-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115615. 5 interactions.
IntActQ9H2X3. 1 interaction.
MINTMINT-1489134.

Chemistry

ChEMBLCHEMBL2176858.

PTM databases

PhosphoSiteQ9H2X3.

Polymorphism databases

DMDM46395990.

Proteomic databases

PaxDbQ9H2X3.
PRIDEQ9H2X3.

Protocols and materials databases

DNASU10332.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327325; ENSP00000316228; ENSG00000104938. [Q9H2X3-1]
ENST00000357361; ENSP00000349924; ENSG00000104938. [Q9H2X3-3]
ENST00000359059; ENSP00000351954; ENSG00000104938. [Q9H2X3-5]
ENST00000595496; ENSP00000470132; ENSG00000104938. [Q9H2X3-7]
ENST00000596363; ENSP00000471125; ENSG00000104938. [Q9H2X3-9]
ENST00000597522; ENSP00000471132; ENSG00000104938. [Q9H2X3-4]
GeneID10332.
KEGGhsa:10332.
UCSCuc002mhy.2. human. [Q9H2X3-10]
uc002mhz.3. human. [Q9H2X3-4]
uc002mia.3. human. [Q9H2X3-7]
uc002mic.3. human. [Q9H2X3-9]
uc002mih.3. human. [Q9H2X3-8]
uc010xjw.2. human. [Q9H2X3-5]

Organism-specific databases

CTD10332.
GeneCardsGC19P007828.
HGNCHGNC:13523. CLEC4M.
HPACAB033689.
CAB033691.
HPA042661.
MIM605872. gene.
neXtProtNX_Q9H2X3.
PharmGKBPA26200.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG314197.
HOVERGENHBG050992.
InParanoidQ9H2X3.
KOK06563.
OMADNYWICK.
OrthoDBEOG7DFXC9.
PhylomeDBQ9H2X3.
TreeFamTF333341.

Gene expression databases

ArrayExpressQ9H2X3.
BgeeQ9H2X3.
GenevestigatorQ9H2X3.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9H2X3.
GeneWikiCLEC4M.
GenomeRNAi10332.
NextBio39173.
PROQ9H2X3.
SOURCESearch...

Entry information

Entry nameCLC4M_HUMAN
AccessionPrimary (citable) accession number: Q9H2X3
Secondary accession number(s): A6NKI4 expand/collapse secondary AC list , 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: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries