P98064 · MASP1_MOUSE
- ProteinMannan-binding lectin serine protease 1
- GeneMasp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids704 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Also plays a role in development.
Activity regulation
Inhibited by SERPING1 and A2M.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 73 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 81 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 126 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 128 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 144 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 145 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 147 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 164 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 165 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 168 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 240 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 250 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 287 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 289 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Site | 453-454 | Cleavage; by autolysis | ||||
Sequence: RI | ||||||
Active site | 495 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 557 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 651 | Charge relay system | ||||
Sequence: S |
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 | cytosol | |
Cellular Component | extracellular space | |
Cellular Component | nucleoplasm | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent protein binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | complement activation, lectin pathway | |
Biological Process | zymogen activation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMannan-binding lectin serine protease 1
- EC number
- Alternative names
- Cleaved into 2 chains
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 accessionP98064
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Mice are smaller and more vulnerable indicating developmental and growth defects. Mice serum has low C4 and C3 cleavage activity together with low MASP2 activation.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 37 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MRFLSFWRLLLYHALCLALPEVSA | ||||||
Chain | PRO_0000027596 | 25-453 | Mannan-binding lectin serine protease 1 heavy chain | |||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGTFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVSLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQTHSVQILFRSDNSGENRGWRLSYRAAGNECPKLQPPVYGKIEPSQAVYSFKDQVLVSCDTGYKVLKDNEVMDTFQIECLKDGAWSNKIPTCKIVDCGAPAGLKHGLVTFSTRNNLTTYKSEIRYSCQQPYYKMLHNTTGVYTCSAHGTWTNEVLKRSLPTCLPVCGVPKFSRKQISR | ||||||
Chain | PRO_0000027595 | 25-704 | Mannan-binding lectin serine protease 1 | |||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGTFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVSLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQTHSVQILFRSDNSGENRGWRLSYRAAGNECPKLQPPVYGKIEPSQAVYSFKDQVLVSCDTGYKVLKDNEVMDTFQIECLKDGAWSNKIPTCKIVDCGAPAGLKHGLVTFSTRNNLTTYKSEIRYSCQQPYYKMLHNTTGVYTCSAHGTWTNEVLKRSLPTCLPVCGVPKFSRKQISRIFNGRPAQKGTMPWIAMLSHLNGQPFCGGSLLGSNWVLTAAHCLHQSLDPEEPTLHSSYLLSPSDFKIIMGKHWRRRSDEDEQHLHVKRTTLHPLYNPSTFENDLGLVELSESPRLNDFVMPVCLPEQPSTEGTMVIVSGWGKQFLQRFPENLMEIEIPIVNSDTCQEAYTPLKKKVTKDMICAGEKEGGKDACAGDSGGPMVTKDAERDQWYLVGVVSWGEDCGKKDRYGVYSYIYPNKDWIQRITGVRN | ||||||
Glycosylation | 54 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 78↔96 | |||||
Sequence: CEYDYVKVETEDQVLATFC | ||||||
Disulfide bond | 148↔162 | |||||
Sequence: CKEREDEELSCDHYC | ||||||
Disulfide bond | 158↔171 | |||||
Sequence: CDHYCHNYIGGYYC | ||||||
Modified residue | 164 | (3R)-3-hydroxyasparagine | ||||
Sequence: N | ||||||
Disulfide bond | 173↔186 | |||||
Sequence: CRFGYILHTDNRTC | ||||||
Glycosylation | 183 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 190↔217 | |||||
Sequence: CSGNLFTQRTGTITSPDYPNPYPKSSEC | ||||||
Disulfide bond | 247↔265 | |||||
Sequence: CPYDYIKIKAGSKVWGPFC | ||||||
Disulfide bond | 306↔354 | |||||
Sequence: CPKLQPPVYGKIEPSQAVYSFKDQVLVSCDTGYKVLKDNEVMDTFQIEC | ||||||
Disulfide bond | 334↔367 | |||||
Sequence: CDTGYKVLKDNEVMDTFQIECLKDGAWSNKIPTC | ||||||
Disulfide bond | 372↔419 | |||||
Sequence: CGAPAGLKHGLVTFSTRNNLTTYKSEIRYSCQQPYYKMLHNTTGVYTC | ||||||
Glycosylation | 390 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 402↔437 | |||||
Sequence: CQQPYYKMLHNTTGVYTCSAHGTWTNEVLKRSLPTC | ||||||
Glycosylation | 412 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 441↔577 | Interchain (between heavy and light chains) | ||||
Sequence: CGVPKFSRKQISRIFNGRPAQKGTMPWIAMLSHLNGQPFCGGSLLGSNWVLTAAHCLHQSLDPEEPTLHSSYLLSPSDFKIIMGKHWRRRSDEDEQHLHVKRTTLHPLYNPSTFENDLGLVELSESPRLNDFVMPVC | ||||||
Chain | PRO_0000027597 | 454-704 | Mannan-binding lectin serine protease 1 light chain | |||
Sequence: IFNGRPAQKGTMPWIAMLSHLNGQPFCGGSLLGSNWVLTAAHCLHQSLDPEEPTLHSSYLLSPSDFKIIMGKHWRRRSDEDEQHLHVKRTTLHPLYNPSTFENDLGLVELSESPRLNDFVMPVCLPEQPSTEGTMVIVSGWGKQFLQRFPENLMEIEIPIVNSDTCQEAYTPLKKKVTKDMICAGEKEGGKDACAGDSGGPMVTKDAERDQWYLVGVVSWGEDCGKKDRYGVYSYIYPNKDWIQRITGVRN | ||||||
Disulfide bond | 480↔496 | |||||
Sequence: CGGSLLGSNWVLTAAHC | ||||||
Disulfide bond | 619↔636 | |||||
Sequence: CQEAYTPLKKKVTKDMIC | ||||||
Disulfide bond | 647↔677 | |||||
Sequence: CAGDSGGPMVTKDAERDQWYLVGVVSWGEDC |
Post-translational modification
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
N-glycosylated. Some N-linked glycan are of the complex-type (By similarity).
Autoproteolytic processing of the proenzyme produces the active enzyme composed on the heavy and the light chain held together by a disulfide bond. Isoform 1 but not isoform 2 is activated through autoproteolytic processing (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Protein of the plasma which is primarily expressed by liver.
Gene expression databases
Interaction
Subunit
Homodimer. Interacts with the oligomeric lectins MBL2, FCN2 and FCN3; triggers the lectin pathway of complement through activation of C3. Interacts with SERPING1. Interacts with COLEC11; probably triggers the lectin pathway of complement.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-143 | CUB 1 | ||||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGTFMSVTFRSDFSNEERFTGFDAHYMAV | ||||||
Region | 25-189 | Homodimerization | ||||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGTFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVE | ||||||
Region | 25-189 | Interaction with MBL2 | ||||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGTFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVE | ||||||
Region | 25-283 | Interaction with FCN2 | ||||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGTFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVSLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQTHSVQIL | ||||||
Region | 25-305 | Interaction with MBL1 | ||||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGTFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVSLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQTHSVQILFRSDNSGENRGWRLSYRAAGNE | ||||||
Domain | 144-187 | EGF-like; calcium-binding | ||||
Sequence: DVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCR | ||||||
Domain | 190-302 | CUB 2 | ||||
Sequence: CSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVSLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQTHSVQILFRSDNSGENRGWRLSYRAA | ||||||
Domain | 304-369 | Sushi 1 | ||||
Sequence: NECPKLQPPVYGKIEPSQAVYSFKDQVLVSCDTGYKVLKDNEVMDTFQIECLKDGAWSNKIPTCKI | ||||||
Domain | 370-439 | Sushi 2 | ||||
Sequence: VDCGAPAGLKHGLVTFSTRNNLTTYKSEIRYSCQQPYYKMLHNTTGVYTCSAHGTWTNEVLKRSLPTCLP | ||||||
Domain | 454-701 | Peptidase S1 | ||||
Sequence: IFNGRPAQKGTMPWIAMLSHLNGQPFCGGSLLGSNWVLTAAHCLHQSLDPEEPTLHSSYLLSPSDFKIIMGKHWRRRSDEDEQHLHVKRTTLHPLYNPSTFENDLGLVELSESPRLNDFVMPVCLPEQPSTEGTMVIVSGWGKQFLQRFPENLMEIEIPIVNSDTCQEAYTPLKKKVTKDMICAGEKEGGKDACAGDSGGPMVTKDAERDQWYLVGVVSWGEDCGKKDRYGVYSYIYPNKDWIQRITG |
Sequence similarities
Belongs to the peptidase S1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P98064-1
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
- SynonymsMASP-1
- Length704
- Mass (Da)79,968
- Last updated2009-04-14 v2
- Checksum4CF0B17916C10961
P98064-2
- Name2
- SynonymsMASP-3
- NoteContains a N-linked (GlcNAc...) asparagine at position 538 Contains a N-linked (GlcNAc...) asparagine at position 604.
- Differences from canonical
- 443-443: V → QPSRALPNLVKRIIGGRNAELGLFPWQALIVVEDTSRVPNDKWFGSGALLSESWILTAAHVLRSQRRDNTVIPVSKEHVTVYLGLHDVRDKSGAVNSSAARVILHPDFNIQNYNHDIALVQLQKPVPLGAHVMPICLPRPEPEGPAPHMLGLVAGWGISNPNVTVDEIILSGTRTLSDVLQYVKLPVVSHAECKASYESRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDEMSQHWVAQGLVSWGGPEECGSKQVYGVYTKVSNYVDWLWEEMNSPRAVRDLQVER
- 444-704: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8VHR3 | A0A2R8VHR3_MOUSE | Masp1 | 385 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 257 | in Ref. 5; AAI31638 | ||||
Sequence: G → A | ||||||
Sequence conflict | 345 | in Ref. 1; BAA03944 and 2; BAB69688 | ||||
Sequence: E → G | ||||||
Sequence conflict | 428 | in Ref. 1; BAA03944 | ||||
Sequence: E → K | ||||||
Alternative sequence | VSP_036814 | 443 | in isoform 2 | |||
Sequence: V → QPSRALPNLVKRIIGGRNAELGLFPWQALIVVEDTSRVPNDKWFGSGALLSESWILTAAHVLRSQRRDNTVIPVSKEHVTVYLGLHDVRDKSGAVNSSAARVILHPDFNIQNYNHDIALVQLQKPVPLGAHVMPICLPRPEPEGPAPHMLGLVAGWGISNPNVTVDEIILSGTRTLSDVLQYVKLPVVSHAECKASYESRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDEMSQHWVAQGLVSWGGPEECGSKQVYGVYTKVSNYVDWLWEEMNSPRAVRDLQVER | ||||||
Alternative sequence | VSP_036815 | 444-704 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 465 | in Ref. 2; AAN39850 | ||||
Sequence: M → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D16492 EMBL· GenBank· DDBJ | BAA03944.1 EMBL· GenBank· DDBJ | mRNA | ||
AB049755 EMBL· GenBank· DDBJ | BAB69688.1 EMBL· GenBank· DDBJ | mRNA | ||
AY135527 EMBL· GenBank· DDBJ | AAN39850.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY135525 EMBL· GenBank· DDBJ | AAN39850.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK031598 EMBL· GenBank· DDBJ | BAC27469.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466521 EMBL· GenBank· DDBJ | EDK97670.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH466521 EMBL· GenBank· DDBJ | EDK97671.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC131637 EMBL· GenBank· DDBJ | AAI31638.1 EMBL· GenBank· DDBJ | mRNA | ||
BC131638 EMBL· GenBank· DDBJ | AAI31639.1 EMBL· GenBank· DDBJ | mRNA |