P97430 · SLPI_MOUSE

  • Protein
    Antileukoproteinase
  • Gene
    Slpi
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G (PubMed:9126337).
Modulates the innate immune response after bacterial infection (PubMed:12615907).
Contributes to regulate the inflammatory and immune responses to the intracellular parasite L.major (PubMed:25030421).
Down-regulates responses to bacterial lipopolysaccharide (LPS) (PubMed:12615907, PubMed:25030421, PubMed:9039268).
Plays a role in regulating the activation of NF-kappa-B and inflammatory responses (PubMed:11017147, PubMed:12615907).
Has antimicrobial activity against mycobacteria, but not against salmonella (PubMed:18322212).
Contributes to normal resistance against infection by M.tuberculosis (PubMed:18322212).
Required for normal resistance to L.major (PubMed:25030421).
Required for normal wound healing, probably by preventing tissue damage by limiting protease activity (PubMed:11017147, PubMed:25030421).
Together with ELANE, required for normal differentiation and proliferation of bone marrow myeloid cells (By similarity).

Features

Showing features for site.

1131102030405060708090100110120130
TypeIDPosition(s)Description
Site98-99Reactive bond for chymotrypsin, trypsin and elastase

GO annotations

AspectTerm
Cellular Componentextracellular space
Cellular ComponentGolgi apparatus
Molecular FunctionDNA binding
Molecular Functionendopeptidase inhibitor activity
Molecular Functionenzyme binding
Molecular FunctionmRNA binding
Molecular Functionserine-type endopeptidase inhibitor activity
Biological Processantibacterial humoral response
Biological Processimmune response
Biological Processinnate immune response
Biological Processmodulation of process of another organism
Biological Processnegative regulation of viral genome replication
Biological Processresponse to lipopolysaccharide

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Antileukoproteinase
  • Short names
    ALP
  • Alternative names
    • Secretory leukocyte protease inhibitor

Gene names

    • Name
      Slpi

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6 X CBA
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P97430
  • Secondary accessions
    • O09081
    • O09082

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Mutant mice show delayed epithelial wound healing and an increased inflammatory response at the site of wounding, possibly due to increased elastase activity (PubMed:11017147, PubMed:25030421).
Mutant mice show an increased tendency to die from toxic shock after exposure to bacterial lipopolysaccharide (LPS) (PubMed:12615907).
Mutant mice are highly susceptible to M.tuberculosis; all die within 50 days after infection (PubMed:18322212).
Mutant mice are highly susceptible infection by L.major. Contrary to what is observed with wild-type, the parasites are not restricted to the initial site of infection, but spread to spleen, liver and bone morrow. The skin lesions at the initial site of infection do not heal normally, but become bigger over time, in parallel with the spread of the parasites. The inflammatory response at the site of infection is more intense and persists longer than normal. Increased protease activity is observed in these lesions and may be the cause of the extensive tissue damage and necrosis (PubMed:25030421).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis39-40Loss of antimicrobial activity.
Mutagenesis92Loss of antimicrobial activity; when associated with A-96.
Mutagenesis96Loss of antimicrobial activity; when associated with A-92.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 8 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-25
ChainPRO_000004135626-131Antileukoproteinase
Disulfide bond36↔65
Disulfide bond44↔69
Disulfide bond52↔64
Disulfide bond58↔73
Disulfide bond90↔119
Disulfide bond97↔123
Disulfide bond106↔118
Disulfide bond112↔127

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in bronchial epithelial cells (PubMed:18322212).
Detected in bronchoalveolar fluid after infection with M.tuberculosis (at protein level) (PubMed:18322212).
Highest expression in lung, spleen, intestine and epididymis with lower levels in liver and seminal vesicle. No expression in brain, heart, kidney and muscle

Induction

Up-regulated by bacterial lipopolysaccharide (PubMed:25030421, PubMed:9039268).
Up-regulated in lung after infection with M.tuberculosis (PubMed:18322212).
Down-regulated by IFNG (PubMed:9039268).
Up-regulated in lung in response to bacterial pneumonia (PubMed:9351627).
Up-regulated in macrophages after exposure to L.major (PubMed:25030421).
Not up-regulated in spleen in response to bacterial pneumonia (PubMed:9351627).
Up-regulated in wounded skin (PubMed:11017147).

Gene expression databases

Interaction

Subunit

Interacts with GRN; interaction protects progranulin from proteolysis.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain29-77WAP 1
Domain83-131WAP 2
Region85-131Elastase inhibitory domain

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    131
  • Mass (Da)
    14,308
  • Last updated
    1997-05-01 v1
  • Checksum
    A57C9E30FE711B8F
MKSCGLLPFTVLLALGILAPWTVEGGKNDAIKIGACPAKKPAQCLKLEKPQCRTDWECPGKQRCCQDACGSKCVNPVPIRKPVWRKPGRCVKTQARCMMLNPPNVCQRDGQCDGKYKCCEGICGKVCLPPM

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E9Q748E9Q748_MOUSESlpi107
E9Q4A3E9Q4A3_MOUSESlpi34

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U73004
EMBL· GenBank· DDBJ
AAC53047.1
EMBL· GenBank· DDBJ
mRNA
U88093
EMBL· GenBank· DDBJ
AAC53140.1
EMBL· GenBank· DDBJ
mRNA
U94341
EMBL· GenBank· DDBJ
AAC53394.1
EMBL· GenBank· DDBJ
mRNA
BC028509
EMBL· GenBank· DDBJ
AAH28509.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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