Q9JJS8 · MASP2_RAT
- ProteinMannan-binding lectin serine protease 2
- GeneMasp2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids685 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase.
Miscellaneous
Dimerization and MBL2 binding requires calcium ions.
Catalytic activity
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 67 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 75 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 120 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 122 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 123 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 138 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 139 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 159 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 162 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Site | 443-444 | Cleavage | ||||
Sequence: RI | ||||||
Active site | 482 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 531 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 632 | 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 | extracellular space | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent protein binding | |
Molecular Function | complement component C4b binding | |
Molecular Function | peptidase activity | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | complement activation | |
Biological Process | complement activation, classical pathway | |
Biological Process | complement activation, lectin pathway | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMannan-binding lectin serine protease 2
- 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 accessionQ9JJS8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MRLLIVLGLLWSLVATLLG | ||||||
Chain | PRO_0000027605 | 20-443 | Mannan-binding lectin serine protease 2 A chain | |||
Sequence: SKWPEPVFGRLVSLGFPEKYGNHQDRSWTLTAPPGFRLRLYFTHFNLELSYRCEYDFVKLTSGTKVLATLCGQESTDTERAPGNDTFYSLGPSLKVTFHSDYSNEKPFTGFEAFYAAEDVDECRTSLGDSVPCDHYCHNYLGGYYCSCRVGYILHQNKHTCSALCSGQVFTGRSGFLSSPEYPQPYPKLSSCAYNIRLEEGFSITLDFVESFDVEMHPEAQCPYDSLKIQTDKREYGPFCGKTLPPRIETDSNKVTITFTTDESGNHTGWKIHYTSTAQPCPDPTAPPNGHISPVQATYVLKDSFSVFCKTGFELLQGSVPLKSFTAVCQKDGSWDRPIPECSIIDCGPPDDLPNGHVDYITGPEVTTYKAVIQYSCEETFYTMSSNGKYVCEADGFWTSSKGEKSLPVCKPVCGLSTHTSGGR | ||||||
Chain | PRO_0000027604 | 20-685 | Mannan-binding lectin serine protease 2 | |||
Sequence: SKWPEPVFGRLVSLGFPEKYGNHQDRSWTLTAPPGFRLRLYFTHFNLELSYRCEYDFVKLTSGTKVLATLCGQESTDTERAPGNDTFYSLGPSLKVTFHSDYSNEKPFTGFEAFYAAEDVDECRTSLGDSVPCDHYCHNYLGGYYCSCRVGYILHQNKHTCSALCSGQVFTGRSGFLSSPEYPQPYPKLSSCAYNIRLEEGFSITLDFVESFDVEMHPEAQCPYDSLKIQTDKREYGPFCGKTLPPRIETDSNKVTITFTTDESGNHTGWKIHYTSTAQPCPDPTAPPNGHISPVQATYVLKDSFSVFCKTGFELLQGSVPLKSFTAVCQKDGSWDRPIPECSIIDCGPPDDLPNGHVDYITGPEVTTYKAVIQYSCEETFYTMSSNGKYVCEADGFWTSSKGEKSLPVCKPVCGLSTHTSGGRIIGGQPAKPGDFPWQVLLLGETTAAGALIHDDWVLTAAHAVYGKTEAMSSLDIRMGILKRLSLIYTQAWPEAVFIHEGYTHGAGFDNDIALIKLKNKVTINRNIMPICLPRKEAASLMKTDFVGTVAGWGLTQKGFLARNLMFVDIPIVDHQKCATAYTKQPYPGAKVTVNMLCAGLDRGGKDSCRGDSGGALVFLDNETQRWFVGGIVSWGSINCGGSEQYGVYTKVTNYIPWIENIINNF | ||||||
Disulfide bond | 72↔90 | |||||
Sequence: CEYDFVKLTSGTKVLATLC | ||||||
Glycosylation | 103 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 152↔165 | |||||
Sequence: CDHYCHNYLGGYYC | ||||||
Modified residue | 158 | (3R)-3-hydroxyasparagine | ||||
Sequence: N | ||||||
Disulfide bond | 167↔180 | |||||
Sequence: CRVGYILHQNKHTC | ||||||
Disulfide bond | 184↔211 | |||||
Sequence: CSGQVFTGRSGFLSSPEYPQPYPKLSSC | ||||||
Disulfide bond | 241↔259 | |||||
Sequence: CPYDSLKIQTDKREYGPFC | ||||||
Glycosylation | 285 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 300↔348 | |||||
Sequence: CPDPTAPPNGHISPVQATYVLKDSFSVFCKTGFELLQGSVPLKSFTAVC | ||||||
Disulfide bond | 328↔361 | |||||
Sequence: CKTGFELLQGSVPLKSFTAVCQKDGSWDRPIPEC | ||||||
Disulfide bond | 366↔411 | |||||
Sequence: CGPPDDLPNGHVDYITGPEVTTYKAVIQYSCEETFYTMSSNGKYVC | ||||||
Disulfide bond | 396↔429 | |||||
Sequence: CEETFYTMSSNGKYVCEADGFWTSSKGEKSLPVC | ||||||
Disulfide bond | 433↔551 | Interchain (between A and B chains) | ||||
Sequence: CGLSTHTSGGRIIGGQPAKPGDFPWQVLLLGETTAAGALIHDDWVLTAAHAVYGKTEAMSSLDIRMGILKRLSLIYTQAWPEAVFIHEGYTHGAGFDNDIALIKLKNKVTINRNIMPIC | ||||||
Chain | PRO_0000027606 | 444-685 | Mannan-binding lectin serine protease 2 B chain | |||
Sequence: IIGGQPAKPGDFPWQVLLLGETTAAGALIHDDWVLTAAHAVYGKTEAMSSLDIRMGILKRLSLIYTQAWPEAVFIHEGYTHGAGFDNDIALIKLKNKVTINRNIMPICLPRKEAASLMKTDFVGTVAGWGLTQKGFLARNLMFVDIPIVDHQKCATAYTKQPYPGAKVTVNMLCAGLDRGGKDSCRGDSGGALVFLDNETQRWFVGGIVSWGSINCGGSEQYGVYTKVTNYIPWIENIINNF | ||||||
Disulfide bond | 597↔617 | |||||
Sequence: CATAYTKQPYPGAKVTVNMLC | ||||||
Disulfide bond | 628↔659 | |||||
Sequence: CRGDSGGALVFLDNETQRWFVGGIVSWGSINC | ||||||
Glycosylation | 641 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in liver. Secreted in plasma.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-137 | CUB 1 | ||||
Sequence: SKWPEPVFGRLVSLGFPEKYGNHQDRSWTLTAPPGFRLRLYFTHFNLELSYRCEYDFVKLTSGTKVLATLCGQESTDTERAPGNDTFYSLGPSLKVTFHSDYSNEKPFTGFEAFYAAE | ||||||
Domain | 138-181 | EGF-like; calcium-binding | ||||
Sequence: DVDECRTSLGDSVPCDHYCHNYLGGYYCSCRVGYILHQNKHTCS | ||||||
Domain | 184-296 | CUB 2 | ||||
Sequence: CSGQVFTGRSGFLSSPEYPQPYPKLSSCAYNIRLEEGFSITLDFVESFDVEMHPEAQCPYDSLKIQTDKREYGPFCGKTLPPRIETDSNKVTITFTTDESGNHTGWKIHYTST | ||||||
Domain | 298-363 | Sushi 1 | ||||
Sequence: QPCPDPTAPPNGHISPVQATYVLKDSFSVFCKTGFELLQGSVPLKSFTAVCQKDGSWDRPIPECSI | ||||||
Domain | 364-431 | Sushi 2 | ||||
Sequence: IDCGPPDDLPNGHVDYITGPEVTTYKAVIQYSCEETFYTMSSNGKYVCEADGFWTSSKGEKSLPVCKP | ||||||
Domain | 444-683 | Peptidase S1 | ||||
Sequence: IIGGQPAKPGDFPWQVLLLGETTAAGALIHDDWVLTAAHAVYGKTEAMSSLDIRMGILKRLSLIYTQAWPEAVFIHEGYTHGAGFDNDIALIKLKNKVTINRNIMPICLPRKEAASLMKTDFVGTVAGWGLTQKGFLARNLMFVDIPIVDHQKCATAYTKQPYPGAKVTVNMLCAGLDRGGKDSCRGDSGGALVFLDNETQRWFVGGIVSWGSINCGGSEQYGVYTKVTNYIPWIENIIN |
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.
Q9JJS8-1
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
- Length685
- Mass (Da)75,667
- Last updated2005-07-19 v2
- Checksum0086154934509C64
Q9JJS8-2
- Name2
- SynonymsMAp19
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2K392 | A0A0G2K392_RAT | Masp2 | 185 | ||
A2VCV7 | A2VCV7_RAT | Masp2 | 685 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 33 | in Ref. 1; CAB90832 | ||||
Sequence: L → P | ||||||
Sequence conflict | 34 | in Ref. 1; CAB65385/CAB65387/CAB65390 | ||||
Sequence: G → A | ||||||
Alternative sequence | VSP_014638 | 182-185 | in isoform 2 | |||
Sequence: ALCS → EQSL | ||||||
Alternative sequence | VSP_014639 | 186-685 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 506-507 | in Ref. 1; CAB90832 | ||||
Sequence: LI → PH | ||||||
Sequence conflict | 622 | in Ref. 1; CAB90832 | ||||
Sequence: R → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y19161 EMBL· GenBank· DDBJ | CAB65248.1 EMBL· GenBank· DDBJ | mRNA | ||
Y18565 EMBL· GenBank· DDBJ | CAB65382.1 EMBL· GenBank· DDBJ | mRNA | ||
Y18566 EMBL· GenBank· DDBJ | CAB65383.1 EMBL· GenBank· DDBJ | mRNA | ||
Y18567 EMBL· GenBank· DDBJ | CAB65384.1 EMBL· GenBank· DDBJ | mRNA | ||
Y18568 EMBL· GenBank· DDBJ | CAB65385.1 EMBL· GenBank· DDBJ | mRNA | ||
Y18569 EMBL· GenBank· DDBJ | CAB65386.1 EMBL· GenBank· DDBJ | mRNA | ||
Y18570 EMBL· GenBank· DDBJ | CAB65387.1 EMBL· GenBank· DDBJ | mRNA | ||
Y18571 EMBL· GenBank· DDBJ | CAB65388.1 EMBL· GenBank· DDBJ | mRNA | ||
Y18572 EMBL· GenBank· DDBJ | CAB65389.1 EMBL· GenBank· DDBJ | mRNA | ||
Y18573 EMBL· GenBank· DDBJ | CAB65390.1 EMBL· GenBank· DDBJ | mRNA | ||
Y18564 EMBL· GenBank· DDBJ | CAB70973.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ277747 EMBL· GenBank· DDBJ | CAB90832.1 EMBL· GenBank· DDBJ | mRNA | ||
Y18285 EMBL· GenBank· DDBJ | CAB50738.1 EMBL· GenBank· DDBJ | mRNA |