Mannan-binding lectin-associated serine protease-2

(Redirected from MASP2 (gene))

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]

Mannan-binding lectin-associated serine protease-2
Identifiers
EC no.3.4.21.104
CAS no.214915-16-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
MASP2
Available structures
PDBOrtholog search: PDBe RCSB
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; HomoloGene: 4819; GeneCards: MASP2; OMA:MASP2 - orthologs
Orthologs
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
View/Edit HumanView/Edit Mouse

Function

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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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References

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  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000009724 Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028979 Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Matsushita M, Fujita T (December 1992). "Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine protease". The Journal of Experimental Medicine. 176 (6): 1497–502. doi:10.1084/jem.176.6.1497. PMC 2119445. PMID 1460414.
  6. Thiel S, Vorup-Jensen T, Stover CM, Schwaeble W, Laursen SB, Poulsen K, Willis AC, Eggleton P, Hansen S, Holmskov U, Reid KB, Jensenius JC (April 1997). "A second serine protease associated with mannan-binding lectin that activates complement". Nature. 386 (6624): 506–10. Bibcode:1997Natur.386..506T. doi:10.1038/386506a0. PMID 9087411.
  7. Rossi V, Cseh S, Bally I, Thielens NM, Jensenius JC, Arlaud GJ (November 2001). "Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2". The Journal of Biological Chemistry. 276 (44): 40880–7. doi:10.1074/jbc.M105934200. PMID 11527969.
  8. Ambrus G, Gál P, Kojima M, Szilágyi K, Balczer J, Antal J, Gráf L, Laich A, Moffatt BE, Schwaeble W, Sim RB, Závodszky P (February 2003). "Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments". Journal of Immunology. 170 (3): 1374–82. doi:10.4049/jimmunol.170.3.1374. PMID 12538697.
  9. Harmat V, Gál P, Kardos J, Szilágyi K, Ambrus G, Végh B, Náray-Szabó G, Závodszky P (October 2004). "The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions". Journal of Molecular Biology. 342 (5): 1533–46. doi:10.1016/j.jmb.2004.07.014. PMID 15364579.
  10. Chen CB, Wallis R (June 2004). "Two mechanisms for mannose-binding protein modulation of the activity of its associated serine proteases". The Journal of Biological Chemistry. 279 (25): 26058–65. doi:10.1074/jbc.M401318200. PMID 15060079.
  11. Teillet F, Dublet B, Andrieu JP, Gaboriaud C, Arlaud GJ, Thielens NM (March 2005). "The two major oligomeric forms of human mannan-binding lectin: chemical characterization, carbohydrate-binding properties, and interaction with MBL-associated serine proteases". Journal of Immunology. 174 (5): 2870–7. doi:10.4049/jimmunol.174.5.2870. PMID 15728497.
  12. 1 2 "Entrez Gene: mannan-binding lectin serine peptidase 2".
  13. Thiel S, Vorup-Jensen T, Stover CM, Schwaeble W, Laursen SB, Poulsen K, Willis AC, Eggleton P, Hansen S, Holmskov U, Reid KB, Jensenius JC (April 1997). "A second serine protease associated with mannan-binding lectin that activates complement". Nature. 386 (6624): 506–10. Bibcode:1997Natur.386..506T. doi:10.1038/386506a0. PMID 9087411. S2CID 4261967.
  14. Vorup-Jensen T, Jensenius JC, Thiel S (August 1998). "MASP-2, the C3 convertase generating protease of the MBLectin complement activating pathway". Immunobiology. 199 (2): 348–57. doi:10.1016/S0171-2985(98)80039-9. PMID 9777418.

Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.