MASP2 (protein)

MASP2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
4FXG, 1Q3X, 1SZB, 1ZJK, 3TVJ

Identifiers

Aliases

MASP2, MAP19, MASP-2, MASP1P1, sMAP, mannan binding lectin serine peptidase 2

External IDs

OMIM: 605102 MGI: 1330832 HomoloGene: 4819 GeneCards: MASP2

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	No data available	Start	11,026,523 bp^[1]
Band	No data available	End	11,047,233 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	No data available	Start	148,602,554 bp^[2]
Band	No data available	End	148,615,499 bp^[2]

Gene ontology
Molecular function	• calcium ion binding • peptidase activity • serine-type peptidase activity • protein binding • hydrolase activity • calcium-dependent protein binding • metal ion binding • complement component C4b binding • serine-type endopeptidase activity
Cellular component	• extracellular region • extracellular exosome • extracellular space
Biological process	• complement activation, lectin pathway • proteolysis • complement activation, classical pathway • immune system process • innate immune response • complement activation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


10747


17175

Ensembl


ENSG00000009724


ENSMUSG00000028979

UniProt


O00187


Q91WP0

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 Mb

Chr 1: 148.6 – 148.62 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Mannan-binding lectin serine protease 2 also known as mannose-binding protein-associated serine protease 2 (MASP-2) is an enzyme that in humans is encoded by the MASP2 gene.^[5]^[6]^[7]

Function

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.^[5]

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.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000009724 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028979 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 "Entrez Gene: mannan-binding lectin serine peptidase 2".
↑ 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. PMID 9087411. doi:10.1038/386506a0.
↑ 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. PMID 9777418. doi:10.1016/S0171-2985(98)80039-9.

Petersen SV, Thiel S, Jensenius JC (2001). "The mannan-binding lectin pathway of complement activation: biology and disease association". Mol. Immunol. 38 (2–3): 133–49. PMID 11532276. doi:10.1016/S0161-5890(01)00038-4.
Rajaraman P, Brenner AV, Butler MA, Wang SS, Pfeiffer RM, Ruder AM, Linet MS, Yeager M, Wang Z, Orr N, Fine HA, Kwon D, Thomas G, Rothman N, Inskip PD, Chanock SJ (2009). "Common variation in genes related to innate immunity and risk of adult glioma.". Cancer Epidemiol. Biomarkers Prev. 18 (5): 1651–8. PMC 2771723 . PMID 19423540. doi:10.1158/1055-9965.EPI-08-1041.
McGeachie M, Ramoni RL, Mychaleckyj JC, Furie KL, Dreyfuss JM, Liu Y, Herrington D, Guo X, Lima JA, Post W, Rotter JI, Rich S, Sale M, Ramoni MF (2009). "Integrative predictive model of coronary artery calcification in atherosclerosis.". Circulation. 120 (24): 2448–54. PMC 2810344 . PMID 19948975. doi:10.1161/CIRCULATIONAHA.109.865501.
Gulla KC, Gupta K, Krarup A, Gal P, Schwaeble WJ, Sim RB, O'Connor CD, Hajela K (2010). "Activation of mannan-binding lectin-associated serine proteases leads to generation of a fibrin clot.". Immunology. 129 (4): 482–95. PMC 2842495 . PMID 20002787. doi:10.1111/j.1365-2567.2009.03200.x.
Cerhan JR, Novak AJ, Fredericksen ZS, Wang AH, Liebow M, Call TG, Dogan A, Witzig TE, Ansell SM, Habermann TM, Kay NE, Slager SL (2009). "Risk of non-Hodgkin lymphoma in association with germline variation in complement genes.". Br. J. Haematol. 145 (5): 614–23. PMC 2820509 . PMID 19344414. doi:10.1111/j.1365-2141.2009.07675.x.
Wang Y, Yan J, Shi Y, Li P, Liu C, Ma Q, Yang R, Wang X, Zhu L, Yang X, Cao C (2009). "Lack of association between polymorphisms of MASP2 and susceptibility to SARS coronavirus infection.". BMC Infect. Dis. 9: 51. PMC 2683852 . PMID 19405982. doi:10.1186/1471-2334-9-51.
Han S, Lan Q, Park AK, Lee KM, Park SK, Ahn HS, Shin HY, Kang HJ, Koo HH, Seo JJ, Choi JE, Ahn YO, Chanock SJ, Kim H, Rothman N, Kang D (2010). "Polymorphisms in innate immunity genes and risk of childhood leukemia.". Hum. Immunol. 71 (7): 727–30. PMC 2967770 . PMID 20438785. doi:10.1016/j.humimm.2010.04.004.
Kocsis A, Kékesi KA, Szász R, Végh BM, Balczer J, Dobó J, Závodszky P, Gál P, Pál G (2010). "Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 and -2: significant contribution of MASP-1 to lectin pathway activation.". J. Immunol. 185 (7): 4169–78. PMID 20817870. doi:10.4049/jimmunol.1001819.
Segat L, Milanese M, Pirulli D, Trevisiol C, Lupo F, Salizzoni M, Amoroso A, Crovella S (2009). "Secreted protein acidic and rich in cysteine (SPARC) gene polymorphism association with hepatocellular carcinoma in Italian patients.". J. Gastroenterol. Hepatol. 24 (12): 1840–6. PMID 19817957. doi:10.1111/j.1440-1746.2009.06009.x.
Smithson A, Perello R, Aibar J, Espinosa G, Tassies D, Freire C, Castro P, Suarez B, Lozano F, Nicolas JM (2010). "Genotypes coding for low serum levels of mannose-binding lectin are underrepresented among individuals suffering from noninfectious systemic inflammatory response syndrome.". Clin. Vaccine Immunol. 17 (3): 447–53. PMC 2837953 . PMID 20042521. doi:10.1128/CVI.00375-09.
Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD (2009). "Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.". Am. J. Hum. Genet. 85 (5): 628–42. PMC 2775832 . PMID 19913121. doi:10.1016/j.ajhg.2009.10.014.
Ytting H, Christensen IJ, Steffensen R, Alsner J, Thiel S, Jensenius JC, Hansen U, Nielsen HJ (2011). "Mannan-binding lectin (MBL) and MBL-associated serine protease 2 (MASP-2) genotypes in colorectal cancer.". Scand. J. Immunol. 73 (2): 122–7. PMID 21198752. doi:10.1111/j.1365-3083.2010.02480.x.
Vallès X, Roca A, Lozano F, Morais L, Suárez B, Casals F, Mandomando I, Sigaúque B, Nhalungo D, Esquinas C, Quintó L, Alonso PL, Torres A (2010). "Serotype-specific pneumococcal disease may be influenced by mannose-binding lectin deficiency.". Eur. Respir. J. 36 (4): 856–63. PMID 20150204. doi:10.1183/09031936.00171409.
de Rooij BJ, van Hoek B, ten Hove WR, Roos A, Bouwman LH, Schaapherder AF, Porte RJ, Daha MR, van der Reijden JJ, Coenraad MJ, Ringers J, Baranski AG, Hepkema BG, Hommes DW, Verspaget HW (2010). "Lectin complement pathway gene profile of donor and recipient determine the risk of bacterial infections after orthotopic liver transplantation.". Hepatology. 52 (3): 1100–10. PMID 20593422. doi:10.1002/hep.23782.
Rajaraman P, Brenner AV, Neta G, Pfeiffer R, Wang SS, Yeager M, Thomas G, Fine HA, Linet MS, Rothman N, Chanock SJ, Inskip PD (2010). "Risk of meningioma and common variation in genes related to innate immunity.". Cancer Epidemiol. Biomarkers Prev. 19 (5): 1356–61. PMC 3169167 . PMID 20406964. doi:10.1158/1055-9965.EPI-09-1151.
Liu JL, Cao C, Ma QJ (2009). "[Study on interaction between SARS-CoV N and MAP19].". Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi. 25 (9): 777–9. PMID 19737459.
St Swierzko A, Cedzynski M, Domzalska-Popadiuk I, MacDonald SL, Borkowska-Klos M, Atkinson AP, Szala A, Jopek A, Jensenius JC, Kawakami M, Szczapa J, Matsushita M, Szemraj J, Turner ML, Kilpatrick DC (2009). "Mannan-binding lectin-associated serine protease-2 (MASP-2) in a large cohort of neonates and its clinical associations". Mol. Immunol. 46 (8–9): 1696–701. PMID 19307021. doi:10.1016/j.molimm.2009.02.022.
Vallès X, Sarrias MR, Casals F, Farnós M, Piñer R, Suárez B, Morais L, Mandomando I, Sigaúque B, Roca A, Alonso PL, Torres A, Thielens NM, Lozano F (2009). "Genetic and structural analysis of MBL2 and MASP2 polymorphisms in south-eastern African children.". Tissue Antigens. 74 (4): 298–307. PMID 19775369. doi:10.1111/j.1399-0039.2009.01328.x.
Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S (2010). "Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.". Diabetes Care. 33 (10): 2250–3. PMC 2945168 . PMID 20628086. doi:10.2337/dc10-0452.

External links

MASP Proteases at the US National Library of Medicine Medical Subject Headings (MeSH)

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

PDB gallery
1q3x: Crystal structure of the catalytic region of human MASP-2 1szb: Crystal structure of the human MBL-associated protein 19 (MAp19) 1zjk: Crystal structure of the zymogen catalytic region of human MASP-2

Proteins: complement system (C, L, A)

Activators/enzymes

Early	C: C1Q/C1R/C1S C4 C4a C4b C2 L: MASP1/MASP2 MBL A: Factor B Factor D Factor P/Properdin
Middle	C3 C3a C3b/iC3b C5 C5a C3-convertase C5-convertase
Late	MAC C6 C7 C8 C9

Inhibitors

CL: C4BP

A: Factor H

Complement receptors

Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin Streptokinase S1P Cathepsin A G

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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MASP2 (protein)

Function

See also

References

Further reading

External links