Q8CHN8 · MASP1_RAT
- 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.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
13 μM | C2 | 37 |
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
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent protein binding | |
Molecular Function | peptidase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | complement activation | |
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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ8CHN8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 651 | Prevents protease self-activation through proteolytic cleavage into heavy and light chain. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant 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: MRFLSFRRLLLYHVLCLTLTEVSA | ||||||
Chain | PRO_0000369243 | 25-453 | Mannan-binding lectin serine protease 1 heavy chain | |||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRVQLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVTLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQSHSIQILFRSDNSGENRGWRLSYRAAGNECPKLQPPVYGKIEPSQAVYSFKDQVLISCDTGYKVLKDNEVMDTFQIECLKDGAWSNKIPTCKIVDCGVPAVLKHGLVTFSTRNNLTTYKSEIRYSCQQPYYKMLHNTTGVYTCSAHGTWTNEVLKRSLPTCLPVCGLPKFSRKHISR | ||||||
Chain | PRO_0000369242 | 25-704 | Mannan-binding lectin serine protease 1 | |||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRVQLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVTLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQSHSIQILFRSDNSGENRGWRLSYRAAGNECPKLQPPVYGKIEPSQAVYSFKDQVLISCDTGYKVLKDNEVMDTFQIECLKDGAWSNKIPTCKIVDCGVPAVLKHGLVTFSTRNNLTTYKSEIRYSCQQPYYKMLHNTTGVYTCSAHGTWTNEVLKRSLPTCLPVCGLPKFSRKHISRIFNGRPAQKGTTPWIAMLSQLNGQPFCGGSLLGSNWVLTAAHCLHHPLDPEEPILHNSHLLSPSDFKIIMGKHWRRRSDEDEQHLHVKHIMLHPLYNPSTFENDLGLVELSESPRLNDFVMPVCLPEHPSTEGTMVIVSGWGKQFLQRLPENLMEIEIPIVNYHTCQEAYTPLGKKVTQDMICAGEKEGGKDACAGDSGGPMVTKDAERDQWYLVGVVSWGEDCGKKDRYGVYSYIYPNKDWIQRVTGVRN | ||||||
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: CPKLQPPVYGKIEPSQAVYSFKDQVLISCDTGYKVLKDNEVMDTFQIEC | ||||||
Disulfide bond | 334↔367 | |||||
Sequence: CDTGYKVLKDNEVMDTFQIECLKDGAWSNKIPTC | ||||||
Disulfide bond | 372↔419 | |||||
Sequence: CGVPAVLKHGLVTFSTRNNLTTYKSEIRYSCQQPYYKMLHNTTGVYTC | ||||||
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: CGLPKFSRKHISRIFNGRPAQKGTTPWIAMLSQLNGQPFCGGSLLGSNWVLTAAHCLHHPLDPEEPILHNSHLLSPSDFKIIMGKHWRRRSDEDEQHLHVKHIMLHPLYNPSTFENDLGLVELSESPRLNDFVMPVC | ||||||
Chain | PRO_0000369244 | 454-704 | Mannan-binding lectin serine protease 1 light chain | |||
Sequence: IFNGRPAQKGTTPWIAMLSQLNGQPFCGGSLLGSNWVLTAAHCLHHPLDPEEPILHNSHLLSPSDFKIIMGKHWRRRSDEDEQHLHVKHIMLHPLYNPSTFENDLGLVELSESPRLNDFVMPVCLPEHPSTEGTMVIVSGWGKQFLQRLPENLMEIEIPIVNYHTCQEAYTPLGKKVTQDMICAGEKEGGKDACAGDSGGPMVTKDAERDQWYLVGVVSWGEDCGKKDRYGVYSYIYPNKDWIQRVTGVRN | ||||||
Disulfide bond | 480↔496 | |||||
Sequence: CGGSLLGSNWVLTAAHC | ||||||
Glycosylation | 538 | In isoform Q8CHN8-2; N-linked (GlcNAc...) asparagine | ||||
Sequence: L | ||||||
Glycosylation | 604 | In isoform Q8CHN8-2; N-linked (GlcNAc...) asparagine | ||||
Sequence: E | ||||||
Disulfide bond | 619↔636 | |||||
Sequence: CQEAYTPLGKKVTQDMIC | ||||||
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.
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
PTM databases
Expression
Tissue specificity
Protein of the plasma which is primarily expressed by liver.
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-143 | CUB 1 | ||||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRVQLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSVTFRSDFSNEERFTGFDAHYMAV | ||||||
Region | 25-189 | Homodimerization | ||||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRVQLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVE | ||||||
Region | 25-189 | Interaction with MBL2 | ||||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRVQLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVE | ||||||
Region | 25-283 | Interaction with FCN2 | ||||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRVQLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVTLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQSHSIQIL | ||||||
Region | 25-305 | Interaction with MBL1 | ||||
Sequence: HTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRVQLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVTLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQSHSIQILFRSDNSGENRGWRLSYRAAGNE | ||||||
Domain | 144-187 | EGF-like; calcium-binding | ||||
Sequence: DVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCR | ||||||
Domain | 190-302 | CUB 2 | ||||
Sequence: CSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVTLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQSHSIQILFRSDNSGENRGWRLSYRAA | ||||||
Domain | 304-369 | Sushi 1 | ||||
Sequence: NECPKLQPPVYGKIEPSQAVYSFKDQVLISCDTGYKVLKDNEVMDTFQIECLKDGAWSNKIPTCKI | ||||||
Domain | 370-439 | Sushi 2 | ||||
Sequence: VDCGVPAVLKHGLVTFSTRNNLTTYKSEIRYSCQQPYYKMLHNTTGVYTCSAHGTWTNEVLKRSLPTCLP | ||||||
Domain | 454-701 | Peptidase S1 | ||||
Sequence: IFNGRPAQKGTTPWIAMLSQLNGQPFCGGSLLGSNWVLTAAHCLHHPLDPEEPILHNSHLLSPSDFKIIMGKHWRRRSDEDEQHLHVKHIMLHPLYNPSTFENDLGLVELSESPRLNDFVMPVCLPEHPSTEGTMVIVSGWGKQFLQRLPENLMEIEIPIVNYHTCQEAYTPLGKKVTQDMICAGEKEGGKDACAGDSGGPMVTKDAERDQWYLVGVVSWGEDCGKKDRYGVYSYIYPNKDWIQRVTG |
Sequence similarities
Belongs to the peptidase S1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 3 isoforms produced by Alternative splicing.
Q8CHN8-1
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)80,097
- Last updated2009-04-14 v2
- Checksum3CB61ED661967127
Q8CHN8-2
- Name2
- SynonymsMASP-3
- Differences from canonical
- 443-443: L → QPSRALPNLVKRIIGGRNAELGLFPWQALIVVEDTSRIPNDKWFGSGALLSESWILTAAHVLRSQRRDNTVIPVSKDHVTVYLGLHDVRDKSGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGAHVMPICLPRPEPEGPAPHMLGLVAGWGISNPNVTVDEIIISGTRTLSDVLQYVKLPVVSHAECKASYESRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDEMSQRWVAQGLVSWGGPEECGSKQVYGVYTKVSNYVDWLLEEMNSPRGVRELQVER
- 444-704: Missing
Q8CHN8-3
- Name3
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5ZL57 | A0A8I5ZL57_RAT | Masp1 | 731 | ||
A0A0H2UHA1 | A0A0H2UHA1_RAT | Masp1 | 690 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 60 | in Ref. 1; CAD29746 | ||||
Sequence: Missing | ||||||
Sequence conflict | 232 | in Ref. 1; CAD29746 | ||||
Sequence: Q → H | ||||||
Alternative sequence | VSP_036816 | 369-385 | in isoform 3 | |||
Sequence: IVDCGVPAVLKHGLVTF → KSEIDLEEELESEQVAE | ||||||
Alternative sequence | VSP_036817 | 386-704 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_036818 | 443 | in isoform 2 | |||
Sequence: L → QPSRALPNLVKRIIGGRNAELGLFPWQALIVVEDTSRIPNDKWFGSGALLSESWILTAAHVLRSQRRDNTVIPVSKDHVTVYLGLHDVRDKSGAVNSSAARVVLHPDFNIQNYNHDIALVQLQEPVPLGAHVMPICLPRPEPEGPAPHMLGLVAGWGISNPNVTVDEIIISGTRTLSDVLQYVKLPVVSHAECKASYESRSGNYSVTENMFCAGYYEGGKDTCLGDSGGAFVIFDEMSQRWVAQGLVSWGGPEECGSKQVYGVYTKVSNYVDWLLEEMNSPRGVRELQVER | ||||||
Alternative sequence | VSP_036819 | 444-704 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ457084 EMBL· GenBank· DDBJ | CAD29746.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ487624 EMBL· GenBank· DDBJ | CAD32173.1 EMBL· GenBank· DDBJ | mRNA | ||
BC085685 EMBL· GenBank· DDBJ | AAH85685.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ277423 EMBL· GenBank· DDBJ | CAB89695.1 EMBL· GenBank· DDBJ | mRNA | ||
AF004661 EMBL· GenBank· DDBJ | AAB65832.1 EMBL· GenBank· DDBJ | mRNA |