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MASP2 (protein)

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Protein-coding gene in the species Homo sapiens
MASP2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4FXG, 1Q3X, 1SZB, 1ZJK, 3TVJ

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
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)
Chromosome 1 (human)Genomic location for MASP2Genomic location for MASP2
Band1p36.22Start11,026,523 bp
End11,047,239 bp
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)
Chromosome 4 (mouse)Genomic location for MASP2Genomic location for MASP2
Band4|4 E2Start148,687,011 bp
End148,699,956 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of liver

  • cerebellar hemisphere

  • right hemisphere of cerebellum

  • pancreatic ductal cell

  • left uterine tube

  • monocyte

  • muscle of leg

  • gastrocnemius muscle

  • skin of leg

  • tibial nerve
Top expressed in
  • left lobe of liver

  • gallbladder

  • superior surface of tongue

  • morula

  • superior frontal gyrus

  • primary visual cortex

  • muscle of thigh

  • ascending aorta

  • embryo

  • lumbar spinal ganglion
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
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 MbChr 4: 148.69 – 148.7 Mb
PubMed search
Wikidata
View/Edit HumanView/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.

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.

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

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000009724Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000028979Ensembl, 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. ^ "Entrez Gene: mannan-binding lectin serine peptidase 2".
  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. S2CID 4261967.
  7. 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

External links

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 1q3x: Crystal structure of the catalytic region of human MASP-2
  • 1szb: Crystal structure of the human MBL-associated protein 19 (MAp19) 1szb: Crystal structure of the human MBL-associated protein 19 (MAp19)
  • 1zjk: Crystal structure of the zymogen catalytic region of human MASP-2 1zjk: Crystal structure of the zymogen catalytic region of human MASP-2
Complement system
Pathways
Activators/enzymes
Early
Middle
Late
Inhibitors
Complement receptors
Function
Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes
Coagulation
Complement system
Other immune system
Venombin
Other
Enzymes
Activity
Regulation
Classification
Kinetics
Types
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