Q8WTT0 · CLC4C_HUMAN
- ProteinC-type lectin domain family 4 member C
- GeneCLEC4C
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids213 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Lectin-type cell surface receptor which may play a role in antigen capturing by dendritic cells (PubMed:11748283, PubMed:21880719, PubMed:25995448).
Specifically recognizes non-sialylated galactose-terminated biantennary glycans containing the trisaccharide epitope Gal(beta1-3/4)GlcNAc(beta1-2)Man (PubMed:21880719, PubMed:25995448).
Binds to serum IgG (PubMed:25995448).
Efficiently targets ligand into antigen-processing and peptide-loading compartments for presentation to T-cells (PubMed:11748283).
May mediate potent inhibition of induction of IFN-alpha/beta expression in plasmacytoid dendritic cells (PubMed:11748283, PubMed:21880719).
May act as a signaling receptor that activates protein-tyrosine kinases and mobilizes intracellular calcium (PubMed:11748283).
Specifically recognizes non-sialylated galactose-terminated biantennary glycans containing the trisaccharide epitope Gal(beta1-3/4)GlcNAc(beta1-2)Man (PubMed:21880719, PubMed:25995448).
Binds to serum IgG (PubMed:25995448).
Efficiently targets ligand into antigen-processing and peptide-loading compartments for presentation to T-cells (PubMed:11748283).
May mediate potent inhibition of induction of IFN-alpha/beta expression in plasmacytoid dendritic cells (PubMed:11748283, PubMed:21880719).
May act as a signaling receptor that activates protein-tyrosine kinases and mobilizes intracellular calcium (PubMed:11748283).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 139 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 172 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 174 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 178 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 178 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 184-186 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: NFR | ||||||
Binding site | 194 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 194 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 194-195 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: ND | ||||||
Binding site | 195 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 202 | a carbohydrate (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | external side of plasma membrane | |
Cellular Component | ficolin-1-rich granule membrane | |
Cellular Component | plasma membrane | |
Cellular Component | secretory granule membrane | |
Cellular Component | tertiary granule membrane | |
Molecular Function | carbohydrate binding | |
Molecular Function | metal ion binding | |
Biological Process | adaptive immune response | |
Biological Process | antifungal innate immune response |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameC-type lectin domain family 4 member C
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8WTT0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-21 | Cytoplasmic | ||||
Sequence: MVPEEEPQDREKGLWWFQLKV | ||||||
Transmembrane | 22-44 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: WSMAVVSILLLSVCFTVSSVVPH | ||||||
Topological domain | 45-213 | Extracellular | ||||
Sequence: NFMYSKTVKRLSKLREYQQYHPSLTCVMEGKDIEDWSCCPTPWTSFQSSCYFISTGMQSWTKSQKNCSVMGADLVVINTREEQDFIIQNLKRNSSYFLGLSDPGGRRHWQWVDQTPYNENVTFWHSGEPNNLDERCAIINFRSSEEWGWNDIHCHVPQKSICKMKKIYI |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 139 | Significantly impairs carbohydrate binding for the trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man. | ||||
Sequence: S → A | ||||||
Mutagenesis | 184 | Abolishes carbohydrate binding for the trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man. | ||||
Sequence: N → A | ||||||
Mutagenesis | 186 | Significantly impairs carbohydrate binding for the trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man. | ||||
Sequence: R → A | ||||||
Mutagenesis | 200 | Significantly impairs carbohydrate binding for the trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man. | ||||
Sequence: V → A | ||||||
Mutagenesis | 202 | Significantly impairs carbohydrate binding for the trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man. | ||||
Sequence: Q → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 299 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000046615 | 1-213 | C-type lectin domain family 4 member C | |||
Sequence: MVPEEEPQDREKGLWWFQLKVWSMAVVSILLLSVCFTVSSVVPHNFMYSKTVKRLSKLREYQQYHPSLTCVMEGKDIEDWSCCPTPWTSFQSSCYFISTGMQSWTKSQKNCSVMGADLVVINTREEQDFIIQNLKRNSSYFLGLSDPGGRRHWQWVDQTPYNENVTFWHSGEPNNLDERCAIINFRSSEEWGWNDIHCHVPQKSICKMKKIYI | ||||||
Disulfide bond | 70↔82 | |||||
Sequence: CVMEGKDIEDWSC | ||||||
Disulfide bond | 83↔94 | |||||
Sequence: CPTPWTSFQSSC | ||||||
Glycosylation | 110 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 111↔206 | |||||
Sequence: CSVMGADLVVINTREEQDFIIQNLKRNSSYFLGLSDPGGRRHWQWVDQTPYNENVTFWHSGEPNNLDERCAIINFRSSEEWGWNDIHCHVPQKSIC | ||||||
Glycosylation | 137 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 164 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 180↔198 | |||||
Sequence: CAIINFRSSEEWGWNDIHC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in plasmacytoid dendritic cells (PDCs). Constitutively expressed in immature monocyte-derived dendritic cells (iMDDC) and is significantly down-regulated upon maturation with LPS but not with TNF-alpha.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8WTT0 | CLDN22 Q8N7P3 | 3 | EBI-12913226, EBI-17766761 | |
BINARY | Q8WTT0 | KTN1 Q86UP2-3 | 3 | EBI-12913226, EBI-12007212 | |
BINARY | Q8WTT0 | MAL P21145 | 4 | EBI-12913226, EBI-3932027 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 90-207 | C-type lectin | ||||
Sequence: FQSSCYFISTGMQSWTKSQKNCSVMGADLVVINTREEQDFIIQNLKRNSSYFLGLSDPGGRRHWQWVDQTPYNENVTFWHSGEPNNLDERCAIINFRSSEEWGWNDIHCHVPQKSICK |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8WTT0-1
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.
- Name1
- Length213
- Mass (Da)25,038
- Last updated2002-03-01 v1
- Checksum5DC82C95BE2378C1
Q8WTT0-2
- Name2
- Differences from canonical
- 11-41: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_012845 | 11-41 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 66 | in Ref. 3; AAQ88590 | ||||
Sequence: P → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF325459 EMBL· GenBank· DDBJ | AAL37358.1 EMBL· GenBank· DDBJ | mRNA | ||
AF325460 EMBL· GenBank· DDBJ | AAL37359.1 EMBL· GenBank· DDBJ | mRNA | ||
AF293615 EMBL· GenBank· DDBJ | AAL37036.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358223 EMBL· GenBank· DDBJ | AAQ88590.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471116 EMBL· GenBank· DDBJ | EAW88655.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471116 EMBL· GenBank· DDBJ | EAW88656.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC074967 EMBL· GenBank· DDBJ | AAH74967.1 EMBL· GenBank· DDBJ | mRNA | ||
BC074968 EMBL· GenBank· DDBJ | AAH74968.1 EMBL· GenBank· DDBJ | mRNA | ||
BC102015 EMBL· GenBank· DDBJ | AAI02016.1 EMBL· GenBank· DDBJ | mRNA | ||
BC102016 EMBL· GenBank· DDBJ | AAI02017.1 EMBL· GenBank· DDBJ | mRNA | ||
BC102017 EMBL· GenBank· DDBJ | AAI02018.1 EMBL· GenBank· DDBJ | mRNA | ||
BC114338 EMBL· GenBank· DDBJ | AAI14339.1 EMBL· GenBank· DDBJ | mRNA |