SLPI report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0045071Biological processnegative regulation of viral genome replication
GO_0045087Biological processinnate immune response
GO_0019731Biological processantibacterial humoral response
GO_0006955Biological processimmune response
GO_0035821Biological processmodulation of process of another organism
GO_0032091Biological processnegative regulation of protein binding
GO_0032496Biological processresponse to lipopolysaccharide
GO_0005615Cellular componentextracellular space
GO_0005576Cellular componentextracellular region
GO_0035580Cellular componentspecific granule lumen
GO_0070062Cellular componentextracellular exosome
GO_0005794Cellular componentGolgi apparatus
GO_0062023Cellular componentcollagen-containing extracellular matrix
GO_0003677Molecular functionDNA binding
GO_0019899Molecular functionenzyme binding
GO_0004866Molecular functionendopeptidase inhibitor activity
GO_0004867Molecular functionserine-type endopeptidase inhibitor activity
GO_0003729Molecular functionmRNA binding
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameSLPI
Protein nameSecretory leukoprotease inhibitor protein
Antileukoproteinase (ALP) (BLPI) (HUSI-1) (Mucus proteinase inhibitor) (MPI) (Protease inhibitor WAP4) (Secretory leukocyte protease inhibitor) (Seminal proteinase inhibitor) (WAP four-disulfide core domain protein 4)
SynonymsWAP4
WFDC4
DescriptionFUNCTION: Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G . Modulates the inflammatory and immune responses after bacterial infection, and after infection by the intracellular parasite L.major. Down-regulates responses to bacterial lipopolysaccharide (LPS) (By similarity). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses . Has antimicrobial activity against mycobacteria, but not against salmonella. Contributes to normal resistance against infection by M.tuberculosis. Required for normal resistance to infection by L.major. Required for normal wound healing, probably by preventing tissue damage by limiting protease activity (By similarity). Together with ELANE, required for normal differentiation and proliferation of bone marrow myeloid cells . .

AccessionsP03973
Q6LDI0
ENST00000338380.2