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Mannan-binding lectin-associated serine protease-2

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Mannan-binding lectin-associated serine protease-2 (EC 3.4.21.104, MASP-2, MASP2, MBP-associated serine protease-2, mannose-binding lectin-associated serine protease-2, p100, mannan-binding lectin-associated serine peptidase 2) is an enzyme[5][6][7][8][9][10][11] that in humans is encoded by the MASP2 gene.[12][13][14]

AliasesMASP2, MAP19, MASP-2, MASP1P1, sMAP, mannan binding lectin serine peptidase 2, Mannan-binding lectin serine protease 2, MBL associated serine protease 2, MAP-2
PDBOrtholog search: PDBe RCSB
Quick facts MASP2, Identifiers ...
MASP2
Identifiers
AliasesMASP2, MAP19, MASP-2, MASP1P1, sMAP, mannan binding lectin serine peptidase 2, Mannan-binding lectin serine protease 2, MBL associated serine protease 2, MAP-2
External IDsOMIM: 605102; MGI: 1330832; GeneCards: MASP2
Available structures
PDBOrtholog search: PDBe RCSB
Enzyme activity
EC #BRENDAExPASyKEGGMetaCyc
3.4.21.104↗↗↗↗
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_139208
NM_006610

NM_001003893
NM_010767

RefSeq (protein)

NP_006601
NP_631947

NP_001003893
NP_034897

Location (UCSC)Chr 1: 11.03 – 11.05 MbChr 4: 148.69 – 148.7 Mb
PubMed search[3][4]
Wikidata
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Function

This enzyme catalyses the following chemical reaction

Selective cleavage after Arg223 in complement component C2 (-Ser-Leu-Gly-Arg-Lys-Ile-Gln-Ile) and after Arg76 in complement component C4 (-Gly-Leu-Gln-Arg-Ala-Leu-Glu-Ile)

This mannan-binding lectin (MBL) recognizes patterns of neutral carbohydrates, such as mannose and N-acetylglucosamine.

The Ra-reactive factor (RARF) is a complement-dependent bactericidal factor that binds to the Ra and R2 polysaccharides expressed by certain enterobacteria. Alternate splicing of this gene results in two transcript variants encoding two RARF components that are involved in the mannan-binding lectin pathway of complement activation. The longer isoform is cleaved into two chains which form a heterodimer linked by a disulfide bond. The encoded proteins are members of the trypsin family of peptidases.[12][citation needed]

MASP-2 is involved in the complement system. MASP-2 is very similar to the C1s molecule, of the classical complement pathway, and they are thought to have a common evolutionary ancestor. When the carbohydrate-recognising heads of MBL bind to specifically arranged mannose residues on the surface of a pathogen, MASP-2 is activated to cleave complement components C4 and C2 into C4a, C4b, C2a, and C2b.

See also

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