Q9XSW3 · MBL2_PIG
- ProteinMannose-binding protein C
- GeneMBL2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids240 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages. According to some authors, it only binds mannose (PubMed:8602463).
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 | collagen trimer | |
Cellular Component | extracellular space | |
Cellular Component | multivesicular body | |
Molecular Function | D-mannose binding | |
Biological Process | complement activation, classical pathway | |
Biological Process | complement activation, lectin pathway | |
Biological Process | positive regulation of phagocytosis | |
Biological Process | surfactant homeostasis |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMannose-binding protein C
- Short namesMBP-C
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus
Accessions
- Primary accessionQ9XSW3
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MSLFPSLHLLLLIVMTAS | ||||||
Chain | PRO_0000397216 | 19-240 | Mannose-binding protein C | |||
Sequence: HTETENCEDIQNTCLVISCDSPGINGLPGKDGLDGAKGEKGEPGQGLIGLQGLPGMVGPQGSPGIPGLPGLKGQKGDSGIDPGNSLANLRSELDNIKKWLIFAQGKQVGKKLYLTNGKKMSFNGVKALCAQFQASVATPTNSRENQAIQELAGTEAFLGITDEYTEGQFVDLTGKRVRYQNWNDGEPNNADSAEHCVEILKDGKWNDIFCSSQLSAVCEFPA | ||||||
Modified residue | 46 | Hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 72 | Hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 81 | Hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 87 | Hydroxyproline | ||||
Sequence: P | ||||||
Disulfide bond | 147↔236 | |||||
Sequence: CAQFQASVATPTNSRENQAIQELAGTEAFLGITDEYTEGQFVDLTGKRVRYQNWNDGEPNNADSAEHCVEILKDGKWNDIFCSSQLSAVC | ||||||
Disulfide bond | 214↔228 | |||||
Sequence: CVEILKDGKWNDIFC |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Expressed in liver. Weakly expressed in kidney and testis.
Interaction
Subunit
Interacts with MASP1 and MASP2. Interacts with MEP1A and MEP1B and may inhibit their catalytic activity (By similarity).
Forms oligomeric complexes of 2 or 3 homotrimers
Forms oligomeric complexes of 2 or 3 homotrimers
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 39-61 | Collagen-like 1 | ||||
Sequence: SPGINGLPGKDGLDGAKGEKGEP | ||||||
Region | 48-102 | Disordered | ||||
Sequence: KDGLDGAKGEKGEPGQGLIGLQGLPGMVGPQGSPGIPGLPGLKGQKGDSGIDPGN | ||||||
Domain | 67-97 | Collagen-like 2 | ||||
Sequence: GLQGLPGMVGPQGSPGIPGLPGLKGQKGDSG | ||||||
Coiled coil | 104-122 | |||||
Sequence: LANLRSELDNIKKWLIFAQ | ||||||
Domain | 126-237 | C-type lectin | ||||
Sequence: VGKKLYLTNGKKMSFNGVKALCAQFQASVATPTNSRENQAIQELAGTEAFLGITDEYTEGQFVDLTGKRVRYQNWNDGEPNNADSAEHCVEILKDGKWNDIFCSSQLSAVCE |
Domain
The coiled-coil domain mediates trimerization.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length240
- Mass (Da)25,523
- Last updated1999-11-01 v1
- Checksum52BD865A21D3D563
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 19 | in Ref. 3; AA sequence | ||||
Sequence: H → S | ||||||
Sequence conflict | 28 | in Ref. 3; AA sequence | ||||
Sequence: I → K | ||||||
Sequence conflict | 39 | in Ref. 3; AA sequence | ||||
Sequence: S → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF164576 EMBL· GenBank· DDBJ | AAD45377.1 EMBL· GenBank· DDBJ | mRNA | ||
EF028163 EMBL· GenBank· DDBJ | ABK78779.1 EMBL· GenBank· DDBJ | Genomic DNA |