MASP1 (protein)

MASP1
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
Aliases MASP1, 3MC1, CRARF, CRARF1, MAP1, MASP, MASP3, MAp44, PRSS5, RaRF, mannan binding lectin serine peptidase 1
External IDs OMIM: 600521 HomoloGene: 89143 GeneCards: MASP1
Genetically Related Diseases
amyotrophic lateral sclerosis[1]
Orthologs
Species Human Mouse
Entrez

5648

n/a

Ensembl

ENSG00000127241

n/a

UniProt

P48740

n/a

RefSeq (mRNA)

NM_001031849
NM_001879
NM_139125

n/a

RefSeq (protein)

NP_001027019.1
NP_001870.3
NP_624302.1

n/a

Location (UCSC) Chr 3: 187.22 – 187.29 Mb n/a
PubMed search [2] 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 to form C4b2a, 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. 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]

See also

References

  1. "Diseases that are genetically associated with MASP1 view/edit references on wikidata".
  2. "Human PubMed Reference:".
  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.
  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.
  5. 1 2 "Entrez Gene: mannan-binding lectin serine peptidase 1 (C4/C2 activating component of Ra-reactive factor)".
  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.

Further reading

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

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