Q9JJS8 · MASP2_RAT

  • Protein
    Mannan-binding lectin serine protease 2
  • Gene
    Masp2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

  • Selective cleavage after Arg-223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).
    EC:3.4.21.104 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site, site, active site.

168550100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site67Ca2+ 1 (UniProtKB | ChEBI)
Binding site75Ca2+ 1 (UniProtKB | ChEBI)
Binding site120Ca2+ 1 (UniProtKB | ChEBI)
Binding site122Ca2+ 1 (UniProtKB | ChEBI)
Binding site123Ca2+ 1 (UniProtKB | ChEBI)
Binding site138Ca2+ 2 (UniProtKB | ChEBI)
Binding site139Ca2+ 2 (UniProtKB | ChEBI)
Binding site159Ca2+ 2 (UniProtKB | ChEBI)
Binding site162Ca2+ 2 (UniProtKB | ChEBI)
Site443-444Cleavage
Active site482Charge relay system
Active site531Charge relay system
Active site632Charge relay system

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular space
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent protein binding
Molecular Functioncomplement component C4b binding
Molecular Functionpeptidase activity
Molecular Functionserine-type endopeptidase activity
Biological Processcomplement activation
Biological Processcomplement activation, classical pathway
Biological Processcomplement activation, lectin pathway
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Name
      Masp2

Organism names

  • Taxonomic identifier
  • Strain
    • Fischer 344
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q9JJS8
  • Secondary accessions
    • Q9JJP3
    • Q9QX83
    • Q9QX84
    • Q9QX85
    • Q9QX86

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000002760520-443Mannan-binding lectin serine protease 2 A chain
ChainPRO_000002760420-685Mannan-binding lectin serine protease 2
Disulfide bond72↔90
Glycosylation103N-linked (GlcNAc...) asparagine
Disulfide bond152↔165
Modified residue158(3R)-3-hydroxyasparagine
Disulfide bond167↔180
Disulfide bond184↔211
Disulfide bond241↔259
Glycosylation285N-linked (GlcNAc...) asparagine
Disulfide bond300↔348
Disulfide bond328↔361
Disulfide bond366↔411
Disulfide bond396↔429
Disulfide bond433↔551Interchain (between A and B chains)
ChainPRO_0000027606444-685Mannan-binding lectin serine protease 2 B chain
Disulfide bond597↔617
Disulfide bond628↔659
Glycosylation641N-linked (GlcNAc...) asparagine

Post-translational modification

N-glycosylated.
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in liver. Secreted in plasma.

Interaction

Subunit

Homodimer; disulfide-linked. Binds MBL2. Isoform 2 binds to MASP1. Binds SERPING1 (By similarity).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain20-137CUB 1
Domain138-181EGF-like; calcium-binding
Domain184-296CUB 2
Domain298-363Sushi 1
Domain364-431Sushi 2
Domain444-683Peptidase S1

Sequence similarities

Belongs to the peptidase S1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The 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.

  • Length
    685
  • Mass (Da)
    75,667
  • Last updated
    2005-07-19 v2
  • Checksum
    0086154934509C64
MRLLIVLGLLWSLVATLLGSKWPEPVFGRLVSLGFPEKYGNHQDRSWTLTAPPGFRLRLYFTHFNLELSYRCEYDFVKLTSGTKVLATLCGQESTDTERAPGNDTFYSLGPSLKVTFHSDYSNEKPFTGFEAFYAAEDVDECRTSLGDSVPCDHYCHNYLGGYYCSCRVGYILHQNKHTCSALCSGQVFTGRSGFLSSPEYPQPYPKLSSCAYNIRLEEGFSITLDFVESFDVEMHPEAQCPYDSLKIQTDKREYGPFCGKTLPPRIETDSNKVTITFTTDESGNHTGWKIHYTSTAQPCPDPTAPPNGHISPVQATYVLKDSFSVFCKTGFELLQGSVPLKSFTAVCQKDGSWDRPIPECSIIDCGPPDDLPNGHVDYITGPEVTTYKAVIQYSCEETFYTMSSNGKYVCEADGFWTSSKGEKSLPVCKPVCGLSTHTSGGRIIGGQPAKPGDFPWQVLLLGETTAAGALIHDDWVLTAAHAVYGKTEAMSSLDIRMGILKRLSLIYTQAWPEAVFIHEGYTHGAGFDNDIALIKLKNKVTINRNIMPICLPRKEAASLMKTDFVGTVAGWGLTQKGFLARNLMFVDIPIVDHQKCATAYTKQPYPGAKVTVNMLCAGLDRGGKDSCRGDSGGALVFLDNETQRWFVGGIVSWGSINCGGSEQYGVYTKVTNYIPWIENIINNF

Q9JJS8-2

  • Name
    2
  • Synonyms
    MAp19
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0G2K392A0A0G2K392_RATMasp2185
A2VCV7A2VCV7_RATMasp2685

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict33in Ref. 1; CAB90832
Sequence conflict34in Ref. 1; CAB65385/CAB65387/CAB65390
Alternative sequenceVSP_014638182-185in isoform 2
Alternative sequenceVSP_014639186-685in isoform 2
Sequence conflict506-507in Ref. 1; CAB90832
Sequence conflict622in Ref. 1; CAB90832

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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