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Protein

C-type lectin domain family 9 member A

Gene

CLEC9A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as an endocytic receptor on a small subset of myeloid cells specialized for the uptake and processing of material from dead cells. Recognizes filamentous form of actin in association with particular actin-binding domains of cytoskeletal proteins, including spectrin, exposed when cell membranes are damaged, and mediate the cross-presentation of dead-cell associated antigens in a Syk-dependent manner.2 Publications

GO - Molecular functioni

GO - Biological processi

  • positive regulation of cytokine secretion Source: UniProtKB
  • receptor-mediated endocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
C-type lectin domain family 9 member A
Gene namesi
Name:CLEC9A
ORF Names:UNQ9341/PRO34046
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:26705. CLEC9A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3535CytoplasmicSequence analysisAdd
BLAST
Transmembranei36 – 5621Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini57 – 241185ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311W → A: Abolishes binding to damaged cells; when associated with A-227. 1 Publication
Mutagenesisi227 – 2271W → A: Abolishes binding to damaged cells; when associated with A-131. 1 Publication

Organism-specific databases

PharmGKBiPA142672093.

Polymorphism and mutation databases

BioMutaiCLEC9A.
DMDMi73917794.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241C-type lectin domain family 9 member APRO_0000046637Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence analysis
Disulfide bondi113 ↔ 124PROSITE-ProRule annotation1 Publication
Disulfide bondi141 ↔ 232PROSITE-ProRule annotation1 Publication
Disulfide bondi211 ↔ 224PROSITE-ProRule annotation1 Publication
Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ6UXN8.
PRIDEiQ6UXN8.

PTM databases

PhosphoSiteiQ6UXN8.

Expressioni

Tissue specificityi

In peripheral blood highly restricted on the surface of BDCA31+ dendritic cells and on a small subset of CD14+ and CD16- monocytes.2 Publications

Gene expression databases

BgeeiQ6UXN8.
CleanExiHS_CLEC9A.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi9606.ENSP00000348074.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi118 – 1203Combined sources
Beta strandi123 – 1275Combined sources
Helixi134 – 14310Combined sources
Helixi154 – 16411Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi172 – 1798Combined sources
Turni181 – 1833Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi210 – 2156Combined sources
Beta strandi218 – 2269Combined sources
Beta strandi228 – 2358Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VPPX-ray1.64A/B110-241[»]
ProteinModelPortaliQ6UXN8.
SMRiQ6UXN8. Positions 111-237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini120 – 233114C-type lectinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi5 – 106ITAM-like

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104266.
HOGENOMiHOG000048721.
HOVERGENiHBG056591.
InParanoidiQ6UXN8.
KOiK17515.
OMAiDYWVGLS.
OrthoDBiEOG7T1RCH.
PhylomeDBiQ6UXN8.
TreeFamiTF336674.

Family and domain databases

Gene3Di3.10.100.10. 2 hits.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6UXN8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHEEEIYTSL QWDSPAPDTY QKCLSSNKCS GACCLVMVIS CVFCMGLLTA
60 70 80 90 100
SIFLGVKLLQ VSTIAMQQQE KLIQQERALL NFTEWKRSCA LQMKYCQAFM
110 120 130 140 150
QNSLSSAHNS SPCPNNWIQN RESCYYVSEI WSIWHTSQEN CLKEGSTLLQ
160 170 180 190 200
IESKEEMDFI TGSLRKIKGS YDYWVGLSQD GHSGRWLWQD GSSPSPGLLP
210 220 230 240
AERSQSANQV CGYVKSNSLL SSNCSTWKYF ICEKYALRSS V
Length:241
Mass (Da):27,324
Last modified:July 5, 2004 - v1
Checksum:i6158B3AC44EEC9C3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071A → G.
Corresponds to variant rs11831360 [ dbSNP | Ensembl ].
VAR_050112

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU339276 mRNA. Translation: ABZ04557.1.
AY358265 mRNA. Translation: AAQ88632.1.
CCDSiCCDS8611.1.
RefSeqiNP_997228.1. NM_207345.3.
UniGeneiHs.531189.

Genome annotation databases

EnsembliENST00000355819; ENSP00000348074; ENSG00000197992.
GeneIDi283420.
KEGGihsa:283420.
UCSCiuc001qxa.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU339276 mRNA. Translation: ABZ04557.1.
AY358265 mRNA. Translation: AAQ88632.1.
CCDSiCCDS8611.1.
RefSeqiNP_997228.1. NM_207345.3.
UniGeneiHs.531189.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VPPX-ray1.64A/B110-241[»]
ProteinModelPortaliQ6UXN8.
SMRiQ6UXN8. Positions 111-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000348074.

PTM databases

PhosphoSiteiQ6UXN8.

Polymorphism and mutation databases

BioMutaiCLEC9A.
DMDMi73917794.

Proteomic databases

PaxDbiQ6UXN8.
PRIDEiQ6UXN8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355819; ENSP00000348074; ENSG00000197992.
GeneIDi283420.
KEGGihsa:283420.
UCSCiuc001qxa.4. human.

Organism-specific databases

CTDi283420.
GeneCardsiCLEC9A.
HGNCiHGNC:26705. CLEC9A.
MIMi612252. gene.
neXtProtiNX_Q6UXN8.
PharmGKBiPA142672093.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00700000104266.
HOGENOMiHOG000048721.
HOVERGENiHBG056591.
InParanoidiQ6UXN8.
KOiK17515.
OMAiDYWVGLS.
OrthoDBiEOG7T1RCH.
PhylomeDBiQ6UXN8.
TreeFamiTF336674.

Miscellaneous databases

GenomeRNAii283420.
NextBioi93890.
PROiQ6UXN8.
SOURCEiSearch...

Gene expression databases

BgeeiQ6UXN8.
CleanExiHS_CLEC9A.

Family and domain databases

Gene3Di3.10.100.10. 2 hits.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CLEC9A is a novel activation C-type lectin-like receptor expressed on BDCA3+ dendritic cells and a subset of monocytes."
    Huysamen C., Willment J.A., Dennehy K.M., Brown G.D.
    J. Biol. Chem. 283:16693-16701(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Tumor therapy in mice via antigen targeting to a novel, DC-restricted C-type lectin."
    Sancho D., Mourao-Sa D., Joffre O.P., Schulz O., Rogers N.C., Pennington D.J., Carlyle J.R., Reis e Sousa C.
    J. Clin. Invest. 118:2098-2110(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, FUNCTION.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 110-241, FUNCTION, DISULFIDE BONDS, SUBUNIT, MUTAGENESIS OF TRP-131 AND TRP-227.

Entry informationi

Entry nameiCLC9A_HUMAN
AccessioniPrimary (citable) accession number: Q6UXN8
Secondary accession number(s): B0ZBM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 5, 2004
Last modified: March 16, 2016
This is version 92 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 12
    Human chromosome 12: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.