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Q9NY25

- CLC5A_HUMAN

UniProt

Q9NY25 - CLC5A_HUMAN

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Protein
C-type lectin domain family 5 member A
Gene
CLEC5A, CLECSF5, MDL1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 By similarity. Critical macrophage receptor for dengue virus serotypes 1-4. The binding of dengue virus to CLEC5A triggers signaling through the phosphylation of TYROBP, this interaction does not result in viral entry, but stimulates proinflammatory cytokine release.2 Publications

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. virus receptor activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cellular defense response Source: ProtInc
  2. innate immune response Source: UniProtKB
  3. negative regulation of apoptotic process Source: UniProtKB
  4. negative regulation of myeloid cell apoptotic process Source: Ensembl
  5. osteoblast development Source: UniProtKB
  6. positive regulation of cytokine secretion Source: Ensembl
  7. response to virus Source: GOC
  8. signal transduction Source: ProtInc
  9. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Immunity, Innate immunity

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiREACT_147694. DAP12 interactions.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CLEC5A
Synonyms:CLECSF5, MDL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:2054. CLEC5A.

Subcellular locationi

Cell membrane; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44Cytoplasmic Reviewed prediction
Transmembranei5 – 2723Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini28 – 188161Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. integral component of plasma membrane Source: ProtInc
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161K → I: Abolishes interaction with TYROBP. 1 Publication

Organism-specific databases

PharmGKBiPA26583.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188C-type lectin domain family 5 member A
PRO_0000046632Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi71 ↔ 82 By similarity
Glycosylationi93 – 931N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi99 ↔ 183 By similarity
Glycosylationi144 – 1441N-linked (GlcNAc...) Reviewed prediction
Glycosylationi151 – 1511N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi161 ↔ 175 By similarity

Post-translational modificationi

N-glycosylated. Contains sialic acid residues By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9NY25.
PRIDEiQ9NY25.

Expressioni

Tissue specificityi

Expressed in peripheral blood monocytes and in the monocyte/macrophage cell lines U-937 and Mono-Mac-6, but not in cell lines of other origins. Expression is down-regulated when monocytes differentiate into dendritic cells.1 Publication

Gene expression databases

ArrayExpressiQ9NY25.
BgeeiQ9NY25.
CleanExiHS_CLEC5A.
GenevestigatoriQ9NY25.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

DIPiDIP-60627N.
STRINGi9606.ENSP00000265306.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi76 – 783
Beta strandi81 – 855
Helixi92 – 1009
Turni101 – 1033
Helixi112 – 12211
Beta strandi127 – 1337
Turni135 – 1373
Beta strandi138 – 1425
Turni143 – 1453
Beta strandi152 – 1543
Beta strandi161 – 17313
Beta strandi179 – 1868

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YHFX-ray1.90A/B/C/D/E/F/G/H/I70-187[»]
ProteinModelPortaliQ9NY25.
SMRiQ9NY25. Positions 70-187.

Miscellaneous databases

EvolutionaryTraceiQ9NY25.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 184107C-type lectin
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG269413.
HOGENOMiHOG000252978.
HOVERGENiHBG081250.
InParanoidiQ9NY25.
KOiK10073.
OMAiFNCVTIG.
PhylomeDBiQ9NY25.
TreeFamiTF337735.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NY25-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MNWHMIISGL IVVVLKVVGM TLFLLYFPQI FNKSNDGFTT TRSYGTVSQI    50
FGSSSPSPNG FITTRSYGTV CPKDWEFYQA RCFFLSTSES SWNESRDFCK 100
GKGSTLAIVN TPEKLKFLQD ITDAEKYFIG LIYHREEKRW RWINNSVFNG 150
NVTNQNQNFN CATIGLTKTF DAASCDISYR RICEKNAK 188
Length:188
Mass (Da):21,521
Last modified:October 1, 2000 - v1
Checksum:i94A2DBD520DC1985
GO
Isoform 2 (identifier: Q9NY25-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     116-116: Missing.

Show »
Length:187
Mass (Da):21,393
Checksum:i9FC97A17AF8C62F9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411R → H.
Corresponds to variant rs35942193 [ dbSNP | Ensembl ].
VAR_050110

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei116 – 1161Missing in isoform 2.
VSP_012839

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF139768 mRNA. Translation: AAF02491.1.
AJ271684 mRNA. Translation: CAB71334.1.
AC073647 Genomic DNA. Translation: AAS07444.1.
BC093714 mRNA. Translation: AAH93714.1.
BC112099 mRNA. Translation: AAI12100.1.
BC113098 mRNA. Translation: AAI13099.1.
CCDSiCCDS5870.1. [Q9NY25-1]
RefSeqiNP_037384.1. NM_013252.2. [Q9NY25-1]
UniGeneiHs.446235.

Genome annotation databases

EnsembliENST00000546910; ENSP00000449999; ENSG00000258227. [Q9NY25-1]
ENST00000567443; ENSP00000455144; ENSG00000261180. [Q9NY25-1]
GeneIDi23601.
KEGGihsa:23601.
UCSCiuc003vwv.1. human. [Q9NY25-1]
uc003vww.1. human. [Q9NY25-2]

Polymorphism databases

DMDMi59797971.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

MDL-1

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF139768 mRNA. Translation: AAF02491.1 .
AJ271684 mRNA. Translation: CAB71334.1 .
AC073647 Genomic DNA. Translation: AAS07444.1 .
BC093714 mRNA. Translation: AAH93714.1 .
BC112099 mRNA. Translation: AAI12100.1 .
BC113098 mRNA. Translation: AAI13099.1 .
CCDSi CCDS5870.1. [Q9NY25-1 ]
RefSeqi NP_037384.1. NM_013252.2. [Q9NY25-1 ]
UniGenei Hs.446235.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YHF X-ray 1.90 A/B/C/D/E/F/G/H/I 70-187 [» ]
ProteinModelPortali Q9NY25.
SMRi Q9NY25. Positions 70-187.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-60627N.
STRINGi 9606.ENSP00000265306.

Polymorphism databases

DMDMi 59797971.

Proteomic databases

PaxDbi Q9NY25.
PRIDEi Q9NY25.

Protocols and materials databases

DNASUi 23601.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000546910 ; ENSP00000449999 ; ENSG00000258227 . [Q9NY25-1 ]
ENST00000567443 ; ENSP00000455144 ; ENSG00000261180 . [Q9NY25-1 ]
GeneIDi 23601.
KEGGi hsa:23601.
UCSCi uc003vwv.1. human. [Q9NY25-1 ]
uc003vww.1. human. [Q9NY25-2 ]

Organism-specific databases

CTDi 23601.
GeneCardsi GC07M141627.
HGNCi HGNC:2054. CLEC5A.
MIMi 604987. gene.
neXtProti NX_Q9NY25.
PharmGKBi PA26583.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG269413.
HOGENOMi HOG000252978.
HOVERGENi HBG081250.
InParanoidi Q9NY25.
KOi K10073.
OMAi FNCVTIG.
PhylomeDBi Q9NY25.
TreeFami TF337735.

Enzyme and pathway databases

Reactomei REACT_147694. DAP12 interactions.

Miscellaneous databases

EvolutionaryTracei Q9NY25.
GeneWikii CLEC5A.
GenomeRNAii 23601.
NextBioi 46284.
PROi Q9NY25.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NY25.
Bgeei Q9NY25.
CleanExi HS_CLEC5A.
Genevestigatori Q9NY25.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view ]
Pfami PF00059. Lectin_C. 1 hit.
[Graphical view ]
SMARTi SM00034. CLECT. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
PROSITEi PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 2), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TYROBP, MUTAGENESIS OF LYS-16.
  2. "Expression of MDL-1 in human blood and cell lines."
    Mueller A., Merz H., Feller A.C.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    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 1).
  5. Cited for: FUNCTION AS A DENGUE VIRUS RECEPTOR.
  6. "Structural flexibility of the macrophage dengue virus receptor CLEC5A: Implications for ligand binding and signaling."
    Watson A.A., Lebedev A.A., Hall B.A., Fenton-May A.E., Vagin A.A., Dejnirattisai W., Felce J., Mongkolsapaya J., Palma A.S., Liu Y., Feizi T., Screaton G.R., Murshudov G.N., O'Callaghan C.A.
    J. Biol. Chem. 286:24208-24218(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 71-187, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH DENGUE VIRUS.

Entry informationi

Entry nameiCLC5A_HUMAN
AccessioniPrimary (citable) accession number: Q9NY25
Secondary accession number(s): Q52M11, Q9UKQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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