XB-FEAT-984452

masp1

This is the community wiki page for the gene masp1 please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase

nomenclature changes

NB: Xenopus gene names follow human nomenclature.

date unknown

Xenopus gene name changed from mannan-binding lectin serine peptidase 1 (C4/C2 activating component of Ra-reactive factor), to mannan-binding lectin serine peptidase 1

date unknown

Xenopus name has changed for Entrez Gene: 5648. From mannan-binding lectin serine peptidase 1 to mannan binding lectin serine peptidase 1 ( removed the hyphen!) opus

2.17.2021

Xenopus name has changed for Entrez Gene: 5648. From mannan binding lectin serine peptidase 1 to MBL associated serine protease 1

annotation corrections

20SEPT2023

The X. laevis masp1.L gene [Gene ID: 398414] was misannotated in the v10 genome release as ovch2l.L ovochymase 2 like [provisional] L homeolog [ Xenopus laevis (African clawed frog) ]

After consultation with domain experts, Dr Heather Ray at ISU, this gene has been placed on the Xenbase masp1 gene page.

Please note that it make take several cycles of data synchronization for the corrected gene name to cascade through to NCBI and back to Xenbase. The last update occurred on 7-Sep-2023. We hope the name change will be reflected accurately by Oct 7th, 2023. Similarly, associated accession will populate the XB-GEN-17335616 (masp1.L) column on the gene page on next Xenbase<->NCBI data refresh.

Summary for human MASP1 from NCBI

This gene encodes 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. The encoded protein 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. The encoded protein is also able to cleave fibrinogen and factor XIII and may 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. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Apr 2010]