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Q9R007 (CLC5A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 5 member A
Alternative name(s):
C-type lectin superfamily member 5
Myeloid DAP12-associating lectin 1
Short name=MDL-1
Gene names
Name:Clec5a
Synonyms:Clecsf5, Mdl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a positive regulator of osteoclastogenesis. Cell surface receptor that signals via TYROBP. Regulates inflammatory responses. Acts as a key regulator of synovial injury and bone erosion during autoimmune joint inflammation. Critical macrophage receptor for dengue virus serotypes 1-4. The binding of dengue virus to CLEC5A triggers signaling through phosphylation of TYROBP, this interaction does not result in viral entry but stimulates proinflammatory cytokine release. Ref.1 Ref.5 Ref.7 Ref.8

Subunit structure

Monomer. Homodimer. The majority of CLEC5A is expressed as a monomeric form on macrophages. Interacts with TYROBP/DAP12. The interaction with TYROBP is required for CLEC5 cell surface expression. Interacts with HCST/DAP10. Forms an CLEC5A/TYROBP/HCST trimolecular complex depending almost solely on TYROBP. Ref.1 Ref.6 Ref.7

Subcellular location

Cell membrane; Single-pass type II membrane protein Ref.6.

Tissue specificity

Expressed in macrophage cell line J-774, but not in T-cell lines, B-cell lines, or mast cell lines. Strong expression in bone marrow cells or thioglycollate induced neutrophils (at protein level). Ref.1 Ref.6 Ref.8

Induction

Up-regulated during the differentiation of myeloid cell line 32Dcl3 into neutrophils.

Post-translational modification

N-glycosylated. Contains sialic acid residues. Ref.6 Ref.7

Involvement in disease

Involved in the pathogenetic mechanisms of Japanese encephalitis virus (JEV) infection of the brain. JEV infection of young mice results in increased expression of CLEC5A in spleen and brain with consequent activation of proinflammatory cytokines secretion.

Sequence similarities

Contains 1 C-type lectin domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q9R007-3)

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 1 (identifier: Q9R007-1)

The sequence of this isoform differs from the canonical sequence as follows:
     28-57: PQVFGKSNDGFVPTESYGTTSVQNVSQIFG → SQIFG
Isoform 2 (identifier: Q9R007-2)

The sequence of this isoform differs from the canonical sequence as follows:
     118-118: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190C-type lectin domain family 5 member A
PRO_0000046633

Regions

Topological domain1 – 44Cytoplasmic Potential
Transmembrane5 – 2521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain26 – 190165Extracellular Potential
Domain80 – 186107C-type lectin

Amino acid modifications

Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Disulfide bond101 ↔ 185 By similarity
Disulfide bond163 ↔ 177 By similarity

Natural variations

Alternative sequence28 – 5730PQVFG…SQIFG → SQIFG in isoform 1.
VSP_041577
Alternative sequence1181Missing in isoform 2.
VSP_012840

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified June 28, 2011. Version 2.
Checksum: AB6AACB3A8D36637

FASTA19021,696
        10         20         30         40         50         60 
MNWHMIISGL IVVVIKVVGM TFFLLYFPQV FGKSNDGFVP TESYGTTSVQ NVSQIFGRND 

        70         80         90        100        110        120 
ESTMPTRSYG TVCPRNWDFH QGKCFFFSFS ESPWKDSMDY CATQGSTLAI VNTPEKLKYL 

       130        140        150        160        170        180 
QDIAGIENYF IGLVRQPGEK KWRWINNSVF NGNVTNQDQN FDCVTIGLTK TYDAASCEVS 

       190 
YRWICEMNAK 

« Hide

Isoform 1 [UniParc].

Checksum: 626D64392A513282
Show »

FASTA16519,055
Isoform 2 [UniParc].

Checksum: 28C26A90421D745D
Show »

FASTA18921,567

References

« Hide 'large scale' references
[1]"Myeloid DAP12-associating lectin (MDL)-1 is a cell surface receptor involved in the activation of myeloid cells."
Bakker A.B.H., Baker E., Sutherland G.R., Phillips J.H., Lanier L.L.
Proc. Natl. Acad. Sci. U.S.A. 96:9792-9796(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TYROBP.
Strain: BALB/c.
Tissue: Myeloid.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Adipose tissue and Bone.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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 3).
[5]"CLEC5A is critical for dengue-virus-induced lethal disease."
Chen S.T., Lin Y.L., Huang M.T., Wu M.F., Cheng S.C., Lei H.Y., Lee C.K., Chiou T.W., Wong C.H., Hsieh S.L.
Nature 453:672-676(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A DENGUE VIRUS RECEPTOR.
[6]"Expression and functional role of MDL-1 (CLEC5A) in mouse myeloid lineage cells."
Aoki N., Kimura Y., Kimura S., Nagato T., Azumi M., Kobayashi H., Sato K., Tateno M.
J. Leukoc. Biol. 85:508-517(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH HCST, SUBCELLULAR LOCATION, GLYCOSYLATION, SIALIC ACID CONTENT.
[7]"Signal adaptor DAP10 associates with MDL-1 and triggers osteoclastogenesis in cooperation with DAP12."
Inui M., Kikuchi Y., Aoki N., Endo S., Maeda T., Sugahara-Tobinai A., Fujimura S., Nakamura A., Kumanogoh A., Colonna M., Takai T.
Proc. Natl. Acad. Sci. U.S.A. 106:4816-4821(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCST, GLYCOSYLATION, FUNCTION.
[8]"Myeloid DAP12-associating lectin (MDL)-1 regulates synovial inflammation and bone erosion associated with autoimmune arthritis."
Joyce-Shaikh B., Bigler M.E., Chao C.C., Murphy E.E., Blumenschein W.M., Adamopoulos I.E., Heyworth P.G., Antonenko S., Bowman E.P., McClanahan T.K., Phillips J.H., Cua D.J.
J. Exp. Med. 207:579-589(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, FUNCTION.
[9]"Expression profile of Japanese encephalitis virus induced neuroinflammation and its implication in disease severity."
Gupta N., Lomash V., Rao P.V.
J. Clin. Virol. 49:4-10(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN JAPANESE ENCEPHALITIS VIRUS INFECTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF139769 mRNA. Translation: AAF02492.1.
AK036697 mRNA. Translation: BAC29537.1.
AK046600 mRNA. Translation: BAC32802.1.
AK137482 mRNA. Translation: BAE23374.1.
CH466533 Genomic DNA. Translation: EDL13570.1.
BC104364 mRNA. Translation: AAI04365.1.
BC104365 mRNA. Translation: AAI04366.1.
CCDSCCDS20036.1. [Q9R007-3]
CCDS20037.1. [Q9R007-1]
RefSeqNP_001033693.1. NM_001038604.1. [Q9R007-3]
NP_067339.1. NM_021364.2. [Q9R007-1]
UniGeneMm.103765.

3D structure databases

ProteinModelPortalQ9R007.
SMRQ9R007. Positions 72-189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48775N.

Proteomic databases

PRIDEQ9R007.

Protocols and materials databases

DNASU23845.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000101491; ENSMUSP00000099030; ENSMUSG00000029915. [Q9R007-1]
ENSMUST00000129948; ENSMUSP00000121848; ENSMUSG00000029915. [Q9R007-3]
ENSMUST00000177178; ENSMUSP00000135240; ENSMUSG00000029915.
GeneID23845.
KEGGmmu:23845.
UCSCuc009bna.1. mouse. [Q9R007-3]
uc009bnb.1. mouse. [Q9R007-1]
uc009bnc.1. mouse. [Q9R007-2]

Organism-specific databases

CTD23601.
MGIMGI:1345151. Clec5a.

Phylogenomic databases

eggNOGNOG269413.
GeneTreeENSGT00730000111396.
HOGENOMHOG000252978.
HOVERGENHBG081250.
InParanoidQ3SXC9.
KOK10073.
OMAFNCVTIG.
OrthoDBEOG7GQXX7.
PhylomeDBQ9R007.
TreeFamTF337735.

Gene expression databases

BgeeQ9R007.
CleanExMM_CLEC5A.
GenevestigatorQ9R007.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
PROSITEPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio303527.
PROQ9R007.
SOURCESearch...

Entry information

Entry nameCLC5A_MOUSE
AccessionPrimary (citable) accession number: Q9R007
Secondary accession number(s): Q3SXC9, Q3UV97, Q8BL24
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot