MASP2
entrez
10747
canonical
uniprot
O00187
canonical
ensembl
ENSG00000009724
resolver
ensp
ENSP00000383690
resolver
ensp
ENSP00000383691
resolver
ensp
ENSP00000514788
resolver
ensp
ENSP00000514789
resolver
ensp
ENSP00000514795
resolver
ensp
ENSP00000662266
resolver
enst
ENST00000700089
resolver
enst
ENST00000700090
resolver
enst
ENST00000700096
resolver
genesymbol
MASP2
resolver
hgnc
HGNC:6902
resolver
uniprot
A0A8V8TPN9
resolver
uniprot
A0A8V8TQY3
resolver
uniprot
A8K458
resolver
uniprot
A8MWJ2
resolver
uniprot
O75754
resolver
uniprot
Q5TEQ5
resolver
uniprot
Q5TER0
resolver
uniprot
Q96QG4
resolver
uniprot
Q9BZH0
resolver
uniprot
Q9H498
resolver
uniprot
Q9H499
resolver
uniprot
Q9UBP3
resolver
uniprot
Q9UC48
resolver
uniprot
Q9ULC7
resolver
uniprot
Q9UMV3
resolver
uniprot
Q9Y270
resolver
uniprot_entry
A0A8V8TPN9_HUMAN
resolver
uniprot_entry
A0A8V8TQY3_HUMAN
resolver
uniprot_entry
MASP2_HUMAN
resolver
uniprot_sec
A8K458
resolver
uniprot_sec
A8MWJ2
resolver
uniprot_sec
O75754
resolver
uniprot_sec
Q5TEQ5
resolver
uniprot_sec
Q5TER0
resolver
uniprot_sec
Q96QG4
resolver
uniprot_sec
Q9BZH0
resolver
uniprot_sec
Q9H498
resolver
uniprot_sec
Q9H499
resolver
uniprot_sec
Q9UBP3
resolver
uniprot_sec
Q9UC48
resolver
uniprot_sec
Q9ULC7
resolver
uniprot_sec
Q9UMV3
resolver
uniprot_sec
Q9Y270
resolver
activity_regulation
ACTIVITY REGULATION: The protease activity is specifically inhibited by SGMI-2 small protein inhibitor. {ECO:0000269|PubMed:22511776, ECO:0000269|PubMed:22691502}.; ACTIVITY REGULATION: (Microbial infection) Serine protease activity is inhibited by E.Coli ecotin (eco). {ECO:0000269|PubMed:35483450}.
uniprot
proteins
amino_acid_sequence
MRLLTLLGLLCGSVATPLGPKWPEPVFGRLASPGFPGEYANDQERRWTLTAPPGYRLRLYFTHFDLELSHLCEYDFVKLSSGAKVLATLCGQESTDTERAPGKDTFYSLGSSLDITFRSDYSNEKPFTGFEAFYAAEDIDECQVAPGEAPTCDHHCHNHLGGFYCSCRAGYVLHRNKRTCSALCSGQVFTQRSGELSSPEYPRPYPKLSSCTYSISLEEGFSVILDFVESFDVETHPETLCPYDFLKIQTDREEHGPFCGKTLPHRIETKSNTVTITFVTDESGDHTGWKIHYTSTAQPCPYPMAPPNGHVSPVQAKYILKDSFSIFCETGYELLQGHLPLKSFTAVCQKDGSWDRPMPACSIVDCGPPDDLPSGRVEYITGPGVTTYKAVIQYSCEETFYTMKVNDGKYVCEADGFWTSSKGEKSLPVCEPVCGLSARTTGGRIYGGQKAKPGDFPWQVLILGGTTAAGALLYDNWVLTAAHAVYEQKHDASALDIRMGTLKRLSPHYTQAWSEAVFIHEGYTHDAGFDNDIALIKLNNKVVINSNITPICLPRKEAESFMRTDDIGTASGWGLTQRGFLARNLMYVDIPIVDHQKCTAAYEKPPYPRGSVTANMLCAGLESGGKDSCRGDSGGALVFLDSETERWFVGGIVSWGSMNCGEAGQYGVYTKVINYIPWIENIISDF
uniprot
proteins
disease_involvement
DISEASE: MASP2 deficiency (MASPD) [MIM:613791]: A disorder that results in autoimmune manifestations, recurrent severe infections, and chronic inflammatory disease. {ECO:0000269|PubMed:12904520, ECO:0000269|PubMed:17252003}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.104
uniprot
proteins
function
FUNCTION: Precursor of a serum protease that activates the lectin pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:11527969, PubMed:22691502). The lectin complement system is activated following association of lectins, such as MBL2, FCN1, FCN2 or FCN3, to carbohydrates on the pathogen surface (PubMed:22691502, PubMed:22966085). MASP2 is cleaved and activated by MASP1 in response to lectin-binding to pathogen carbohydrates (PubMed:10946292, PubMed:22949645, PubMed:22966085, PubMed:9087411). Can activate prothrombin to thrombin (PubMed:39924859). {ECO:0000269|PubMed:10946292, ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:22691502, ECO:0000269|PubMed:22949645, ECO:0000269|PubMed:22966085, ECO:0000269|PubMed:39924859, ECO:0000269|PubMed:9087411}.; FUNCTION: [Mannan-binding lectin serine protease 2 B chain]: Serine protease component of the lectin complement pathway, which catalyzes cleavage and activation of C2 and C4, the next components of the complement pathway. {ECO:0000269|PubMed:10946292, ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:22691502, ECO:0000269|PubMed:22949645, ECO:0000269|PubMed:22966085, ECO:0000269|PubMed:9087411}.
uniprot
proteins
mass_dalton
75702
uniprot
proteins
mutagenesis
MUTAGEN 74; /note="Y->A: Strongly decreases affinity for MBL2. Decreases affinity for FCN2."; /evidence="ECO:0000269|PubMed:15117939"; MUTAGEN 121; /note="Y->A: Strongly decreases affinity for MBL2, but not for FCN2."; /evidence="ECO:0000269|PubMed:15117939"; MUTAGEN 124; /note="E->A: Decreases affinity for MBL2. Slight decrease in affinity for FCN2."; /evidence="ECO:0000269|PubMed:15117939"; MUTAGEN 333; /note="E->R: Reduced ability to cleave complement C4."; /evidence="ECO:0000269|PubMed:22949645"; MUTAGEN 340; /note="P->R: Reduced ability to cleave complement C4."; /evidence="ECO:0000269|PubMed:22949645"; MUTAGEN 365; /note="D->R: Reduced ability to cleave complement C4."; /evidence="ECO:0000269|PubMed:22949645"; MUTAGEN 368; /note="P->R: Reduced ability to cleave complement C4."; /evidence="ECO:0000269|PubMed:22949645"; MUTAGEN 444; /note="R->Q: Abolishes cleavage."; /evidence="ECO:0000269|PubMed:16040602, ECO:0000269|PubMed:23386610"; MUTAGEN 633; /note="S->A: Abolished serine protease activity."; /evidence="ECO:0000269|PubMed:23386610
uniprot
proteins
post_translational_modification
PTM: Activated by cleavage after Arg-444 by MASP1. The uncleaved zymogen is inactive towards synthetic substrates, but has sufficient activity to effect autocatalytic cleavage. {ECO:0000269|PubMed:10092804, ECO:0000269|PubMed:16040602, ECO:0000269|PubMed:23386610}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250|UniProtKB:Q9JJS8}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10092804
uniprot
proteins
pubmed
10330290
uniprot
proteins
pubmed
10946292
uniprot
proteins
pubmed
11426320
uniprot
proteins
pubmed
11527969
uniprot
proteins
pubmed
12904520
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15117939
uniprot
proteins
pubmed
15364579
uniprot
proteins
pubmed
16029433
uniprot
proteins
pubmed
16040602
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17252003
uniprot
proteins
pubmed
22511776
uniprot
proteins
pubmed
22691502
uniprot
proteins
pubmed
22949645
uniprot
proteins
pubmed
22966085
uniprot
proteins
pubmed
23386610
uniprot
proteins
pubmed
25911760
uniprot
proteins
pubmed
25930971
uniprot
proteins
pubmed
27599733
uniprot
proteins
pubmed
35483450
uniprot
proteins
pubmed
39924859
uniprot
proteins
pubmed
8618346
uniprot
proteins
pubmed
9087411
uniprot
proteins
sequence_length
686
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9087411}.; SUBCELLULAR LOCATION: [Mannan-binding lectin serine protease 2 B chain]: Secreted {ECO:0000269|PubMed:22966085}. Cell surface {ECO:0000269|PubMed:22966085}. Note=Recruited to the surface of pathogens by the mannose-binding proteins, such as MBL2. {ECO:0000269|PubMed:22966085}.
uniprot
proteins