Q8VCH2 · CLM5_MOUSE
- ProteinCMRF35-like molecule 5
- GeneCd300ld
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids221 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as an activating receptor in myeloid cells and mast cells.
(Microbial infection) Acts as a functional murine norovirus (MNV) receptor. Primary determinant of MNV species tropism and is sufficient to render cells permissive to infection by MNV. Can render nonmurine mammalian cells susceptible to MNV infection (PubMed:27540007, PubMed:27681626).
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 | plasma membrane | |
Molecular Function | virus receptor activity | |
Biological Process | immune system process | |
Biological Process | regulation of interleukin-6 production | |
Biological Process | regulation of tumor necrosis factor production |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameCMRF35-like molecule 5
- Short namesCLM-5
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8VCH2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 19-177 | Extracellular | ||||
Sequence: QDSVTGPEEVSGQEQGSLTVQCRYSSYWKGYKKYWCRGVPQRSCDILVETDKSEQLVKKNRVSIRDNQRDFIFTVTMEDLRMSDAGIYWCGITKGGPDPMFKVNVNIDQAPKSSMMTTTATVLKSIQPSAENTGKEQVTQSKEVTQSRPHTRSLLSSIY | ||||||
Transmembrane | 178-198 | Helical | ||||
Sequence: FLLMVFVELPLLLSMLSAVLW | ||||||
Topological domain | 199-221 | Cytoplasmic | ||||
Sequence: VTRPQRCFGRGENDLVKTHSPVA |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 165-170 | Decreases surface expression in transfected pro-B cells and impairs interaction with FCER1G. | ||||
Sequence: SRPHTR → NSLFIW | ||||||
Mutagenesis | 177-186 | Increases surface expression in transfected pro-B cells and impairs interaction with FCER1G. | ||||
Sequence: YFLLMVFVEL → SFLLMVFVVV |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 56 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MWQFSALLLFFLPGCCTA | ||||||
Chain | PRO_0000320128 | 19-221 | CMRF35-like molecule 5 | |||
Sequence: QDSVTGPEEVSGQEQGSLTVQCRYSSYWKGYKKYWCRGVPQRSCDILVETDKSEQLVKKNRVSIRDNQRDFIFTVTMEDLRMSDAGIYWCGITKGGPDPMFKVNVNIDQAPKSSMMTTTATVLKSIQPSAENTGKEQVTQSKEVTQSRPHTRSLLSSIYFLLMVFVELPLLLSMLSAVLWVTRPQRCFGRGENDLVKTHSPVA | ||||||
Disulfide bond | 40↔108 | |||||
Sequence: CRYSSYWKGYKKYWCRGVPQRSCDILVETDKSEQLVKKNRVSIRDNQRDFIFTVTMEDLRMSDAGIYWC |
Post-translational modification
O-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in dendritic cells, macrophages and granulocytes. Present on the surface of granulocytes and monocytes/macrophages (at protein level).
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-124 | Ig-like V-type | ||||
Sequence: QDSVTGPEEVSGQEQGSLTVQCRYSSYWKGYKKYWCRGVPQRSCDILVETDKSEQLVKKNRVSIRDNQRDFIFTVTMEDLRMSDAGIYWCGITKGGPDPMFKVNVN | ||||||
Region | 38-48 | May play an important role in murine norovirus (MNV) binding | ||||
Sequence: VQCRYSSYWKG | ||||||
Region | 165-170 | Important for maintaining surface expression and for interaction with FCER1G | ||||
Sequence: SRPHTR | ||||||
Region | 177-186 | Important for maintaining surface expression and for interaction with FCER1G | ||||
Sequence: YFLLMVFVEL |
Sequence similarities
Belongs to the CD300 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length221
- Mass (Da)24,954
- Last updated2002-03-01 v1
- ChecksumC9E6203BE64922C1
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 20-21 | in Ref. 2; AB292062 | ||||
Sequence: DS → NP | ||||||
Sequence conflict | 41-48 | in Ref. 2; AB292062 | ||||
Sequence: RYSSYWKG → QYTSDWKD | ||||||
Sequence conflict | 55 | in Ref. 2; AB292062 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 60 | in Ref. 2; AB292062 | ||||
Sequence: R → K | ||||||
Sequence conflict | 63-66 | in Ref. 2; AB292062 | ||||
Sequence: DILV → VFLI | ||||||
Sequence conflict | 88 | in Ref. 2; AB292062 | ||||
Sequence: D → E | ||||||
Sequence conflict | 94 | in Ref. 2; AB292062 | ||||
Sequence: T → I | ||||||
Sequence conflict | 113-118 | in Ref. 2; AB292062 | ||||
Sequence: GGPDPM → AGYDPV | ||||||
Sequence conflict | 124-127 | in Ref. 2; AB292062 | ||||
Sequence: NIDQ → SINP | ||||||
Sequence conflict | 188 | in Ref. 3; BAC30893 | ||||
Sequence: L → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY457051 EMBL· GenBank· DDBJ | AAR27942.1 EMBL· GenBank· DDBJ | mRNA | ||
AB292062 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AK041292 EMBL· GenBank· DDBJ | BAC30893.1 EMBL· GenBank· DDBJ | mRNA | ||
BC019814 EMBL· GenBank· DDBJ | AAH19814.1 EMBL· GenBank· DDBJ | mRNA |