MASP1 (protein)

MASP1
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	3DEM, 3GOV, 4AQB, 4DJZ, 4IGD, 4IW4, 4KKD
Identifiers
Aliases	MASP1, 3MC1, CRARF, CRARF1, MAP1, MASP, MASP3, MAp44, PRSS5, RaRF, mannan binding lectin serine peptidase 1, Mannan-binding lectin serine protease 1, MBL associated serine protease 1, MASP-3, MAP-1
External IDs	OMIM: 600521 HomoloGene: 89143 GeneCards: MASP1
Gene location (Human)
Chr.	Chromosome 3 (human)
End	187,291,980 bp
Gene ontology
Molecular function	• calcium ion binding; • peptidase activity; • serine-type peptidase activity; • GO:0001948 protein binding; • hydrolase activity; • protein homodimerization activity; • calcium-dependent protein binding; • metal ion binding; • serine-type endopeptidase activity;
Cellular component	• extracellular region; • extracellular space; • nucleoplasm; • cytosol;
Biological process	• complement activation, lectin pathway; • receptor-mediated endocytosis; • proteolysis; • negative regulation of complement activation; • immune system process; • innate immune response; • complement activation;
	Sources:Amigo / QuickGO
Orthologs
	5648
	n/a
	ENSG00000127241
	n/a
	P48740
	n/a
	NM_001031849; NM_001879; NM_139125
	n/a
	NP_001027019; NP_001870; NP_624302
	n/a
	Wikidata
View/Edit Human

Mannan-binding lectin serine protease 1 also known as mannose-associated serine protease 1 (MASP-1) is an enzyme that in humans is encoded by the MASP1 gene.^[3]^[4]^[5]

MASP-1 is involved in the lectin pathway of the complement system and is responsible for cleaving C4 and C2 into fragments to form a C3-convertase.^[6]

Function[]

MASP-1 is a serine protease that functions as a component of the lectin pathway of complement activation. The complement pathway plays an essential role in the innate and adaptive immune response.^[7] MASP-1 is synthesized as a zymogen and is activated when it complexes with the pathogen recognition molecules of lectin pathway, the mannose-binding lectin and the ficolins. This protein is not directly involved in complement activation but may play a role as an amplifier of complement activation by cleaving complement C2 or by activating another complement serine protease, MASP-2. MASP-1 is also able to cleave fibrinogen and factor XIII and may be involved in coagulation. A splice variant of this gene which lacks the serine protease domain functions as an inhibitor of the complement pathway.^[5]

References[]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000127241 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Takada F, Takayama Y, Hatsuse H, Kawakami M (Oct 1993). "A new member of the C1s family of complement proteins found in a bactericidal factor, Ra-reactive factor, in human serum". Biochemical and Biophysical Research Communications. 196 (2): 1003–9. doi:10.1006/bbrc.1993.2349. PMID 8240317.
^ Sato T, Endo Y, Matsushita M, Fujita T (Apr 1994). "Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein". International Immunology. 6 (4): 665–9. doi:10.1093/intimm/6.4.665. PMID 8018603.
^ ^a ^b "Entrez Gene: mannan-binding lectin serine peptidase 1 (C4/C2 activating component of Ra-reactive factor)".
^ Matsushita M, Thiel S, Jensenius JC, Terai I, Fujita T (Sep 2000). "Proteolytic activities of two types of mannose-binding lectin-associated serine protease". Journal of Immunology. 165 (5): 2637–42. doi:10.4049/jimmunol.165.5.2637. PMID 10946292.
^ Andrade, Fabiana A.; Lidani, Kárita C. F.; Catarino, Sandra J.; Messias-Reason, Iara J. (2017-06-10). "Serine Proteases in the Lectin Pathway of the Complement System". Proteases in Physiology and Pathology: 397–420. doi:10.1007/978-981-10-2513-6_18. ISBN 978-981-10-2512-9. PMC 7120406.

Further reading[]

Guey LT, García-Closas M, Murta-Nascimento C, Lloreta J, Palencia L, Kogevinas M, Rothman N, Vellalta G, Calle ML, Marenne G, Tardón A, Carrato A, García-Closas R, Serra C, Silverman DT, Chanock S, Real FX, Malats N (Feb 2010). "Genetic susceptibility to distinct bladder cancer subphenotypes". European Urology. 57 (2): 283–92. doi:10.1016/j.eururo.2009.08.001. PMC 3220186. PMID 19692168.
Petersen SV, Thiel S, Jensenius JC (Aug 2001). "The mannan-binding lectin pathway of complement activation: biology and disease association". Molecular Immunology. 38 (2–3): 133–49. doi:10.1016/S0161-5890(01)00038-4. PMID 11532276.
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 (May 2009). "Common variation in genes related to innate immunity and risk of adult glioma". Cancer Epidemiology, Biomarkers & Prevention. 18 (5): 1651–8. doi:10.1158/1055-9965.EPI-08-1041. PMC 2771723. PMID 19423540.
Dobó J, Harmat V, Beinrohr L, Sebestyén E, Závodszky P, Gál P (Jul 2009). "MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity". Journal of Immunology. 183 (2): 1207–14. doi:10.4049/jimmunol.0901141. PMID 19564340.
Skjoedt MO, Hummelshoj T, Palarasah Y, Honore C, Koch C, Skjodt K, Garred P (Mar 2010). "A novel mannose-binding lectin/ficolin-associated protein is highly expressed in heart and skeletal muscle tissues and inhibits complement activation". The Journal of Biological Chemistry. 285 (11): 8234–43. doi:10.1074/jbc.M109.065805. PMC 2832975. PMID 20053996.
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 (Jul 2010). "Polymorphisms in innate immunity genes and risk of childhood leukemia". Human Immunology. 71 (7): 727–30. doi:10.1016/j.humimm.2010.04.004. PMC 2967770. PMID 20438785.
Kocsis A, Kékesi KA, Szász R, Végh BM, Balczer J, Dobó J, Závodszky P, Gál P, Pál G (Oct 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". Journal of Immunology. 185 (7): 4169–78. doi:10.4049/jimmunol.1001819. PMID 20817870.
Rooryck C, Diaz-Font A, Osborn DP, Chabchoub E, Hernandez-Hernandez V, Shamseldin H, Kenny J, Waters A, Jenkins D, Kaissi AA, Leal GF, Dallapiccola B, Carnevale F, Bitner-Glindzicz M, Lees M, Hennekam R, Stanier P, Burns AJ, Peeters H, Alkuraya FS, Beales PL (Mar 2011). "Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC syndrome". Nature Genetics. 43 (3): 197–203. doi:10.1038/ng.757. PMC 3045628. PMID 21258343.
Megyeri M, Makó V, Beinrohr L, Doleschall Z, Prohászka Z, Cervenak L, Závodszky P, Gál P (Sep 2009). "Complement protease MASP-1 activates human endothelial cells: PAR4 activation is a link between complement and endothelial function". Journal of Immunology. 183 (5): 3409–16. doi:10.4049/jimmunol.0900879. PMID 19667088.
Sirmaci A, Walsh T, Akay H, Spiliopoulos M, Sakalar YB, Hasanefendioğlu-Bayrak A, Duman D, Farooq A, King MC, Tekin M (Nov 2010). "MASP1 mutations in patients with facial, umbilical, coccygeal, and auditory findings of Carnevale, Malpuech, OSA, and Michels syndromes". American Journal of Human Genetics. 87 (5): 679–86. doi:10.1016/j.ajhg.2010.09.018. PMC 2978960. PMID 21035106.
Hosgood HD, Menashe I, He X, Chanock S, Lan Q (Dec 2009). "PTEN identified as important risk factor of chronic obstructive pulmonary disease". Respiratory Medicine. 103 (12): 1866–70. doi:10.1016/j.rmed.2009.06.016. PMC 2783799. PMID 19625176.
Hosgood HD, Menashe I, Shen M, Yeager M, Yuenger J, Rajaraman P, He X, Chatterjee N, Caporaso NE, Zhu Y, Chanock SJ, Zheng T, Lan Q (Oct 2008). "Pathway-based evaluation of 380 candidate genes and lung cancer susceptibility suggests the importance of the cell cycle pathway". Carcinogenesis. 29 (10): 1938–43. doi:10.1093/carcin/bgn178. PMC 2722857. PMID 18676680.
Kang JU, Koo SH, Kwon KC, Park JW, Kim JM (2009). "Identification of novel candidate target genes, including EPHB3, MASP1 and SST at 3q26.2-q29 in squamous cell carcinoma of the lung". BMC Cancer. 9: 237. doi:10.1186/1471-2407-9-237. PMC 2716371. PMID 19607727.
Skjoedt MO, Palarasah Y, Munthe-Fog L, Jie Ma Y, Weiss G, Skjodt K, Koch C, Garred P (Nov 2010). "MBL-associated serine protease-3 circulates in high serum concentrations predominantly in complex with Ficolin-3 and regulates Ficolin-3 mediated complement activation". Immunobiology. 215 (11): 921–31. doi:10.1016/j.imbio.2009.10.006. PMID 19939495.
Degn SE, Hansen AG, Steffensen R, Jacobsen C, Jensenius JC, Thiel S (Dec 2009). "MAp44, a human protein associated with pattern recognition molecules of the complement system and regulating the lectin pathway of complement activation". Journal of Immunology. 183 (11): 7371–8. doi:10.4049/jimmunol.0902388. PMID 19917686.
Rajaraman P, Brenner AV, Neta G, Pfeiffer R, Wang SS, Yeager M, Thomas G, Fine HA, Linet MS, Rothman N, Chanock SJ, Inskip PD (May 2010). "Risk of meningioma and common variation in genes related to innate immunity". Cancer Epidemiology, Biomarkers & Prevention. 19 (5): 1356–61. doi:10.1158/1055-9965.EPI-09-1151. PMC 3169167. PMID 20406964.
Ennis S, Jomary C, Mullins R, Cree A, Chen X, Macleod A, Jones S, Collins A, Stone E, Lotery A (Nov 2008). "Association between the SERPING1 gene and age-related macular degeneration: a two-stage case-control study". Lancet. 372 (9652): 1828–34. doi:10.1016/S0140-6736(08)61348-3. PMC 5983350. PMID 18842294.
Shen M, Vermeulen R, Rajaraman P, Menashe I, He X, Chapman RS, Yeager M, Thomas G, Burdett L, Hutchinson A, Yuenger J, Chanock S, Lan Q (May 2009). "Polymorphisms in innate immunity genes and lung cancer risk in Xuanwei, China". Environmental and Molecular Mutagenesis. 50 (4): 285–90. doi:10.1002/em.20452. PMC 2666781. PMID 19170196.
Duus K, Thielens NM, Lacroix M, Tacnet P, Frachet P, Holmskov U, Houen G (Dec 2010). "CD91 interacts with mannan-binding lectin (MBL) through the MBL-associated serine protease-binding site". The FEBS Journal. 277 (23): 4956–64. doi:10.1111/j.1742-4658.2010.07901.x. PMID 21054788. S2CID 31526986.
Degn SE, Jensen L, Gál P, Dobó J, Holmvad SH, Jensenius JC, Thiel S (Sep 2010). "Biological variations of MASP-3 and MAp44, two splice products of the MASP1 gene involved in regulation of the complement system". Journal of Immunological Methods. 361 (1–2): 37–50. doi:10.1016/j.jim.2010.07.006. PMID 20673767.

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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000127241 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8240317-3] Takada F, Takayama Y, Hatsuse H, Kawakami M (Oct 1993). "A new member of the C1s family of complement proteins found in a bactericidal factor, Ra-reactive factor, in human serum". Biochemical and Biophysical Research Communications. 196 (2): 1003–9. doi:10.1006/bbrc.1993.2349. PMID 8240317.

[pmid8018603-4] Sato T, Endo Y, Matsushita M, Fujita T (Apr 1994). "Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein". International Immunology. 6 (4): 665–9. doi:10.1093/intimm/6.4.665. PMID 8018603.

[entrez-5] "Entrez Gene: mannan-binding lectin serine peptidase 1 (C4/C2 activating component of Ra-reactive factor)".

[pmid10946292-6] Matsushita M, Thiel S, Jensenius JC, Terai I, Fujita T (Sep 2000). "Proteolytic activities of two types of mannose-binding lectin-associated serine protease". Journal of Immunology. 165 (5): 2637–42. doi:10.4049/jimmunol.165.5.2637. PMID 10946292.

[7] Andrade, Fabiana A.; Lidani, Kárita C. F.; Catarino, Sandra J.; Messias-Reason, Iara J. (2017-06-10). "Serine Proteases in the Lectin Pathway of the Complement System". Proteases in Physiology and Pathology: 397–420. doi:10.1007/978-981-10-2513-6_18. ISBN 978-981-10-2512-9. PMC 7120406.

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v t 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/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
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) EC7 Translocases (list)

MASP1 (protein)

Contents

Function[]

See also[]

References[]

Further reading[]

External links[]