P97430 · SLPI_MOUSE
- ProteinAntileukoproteinase
- GeneSlpi
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids131 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 98-99 | Reactive bond for chymotrypsin, trypsin and elastase | ||||
Sequence: MM |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | Golgi apparatus | |
Molecular Function | DNA binding | |
Molecular Function | endopeptidase inhibitor activity | |
Molecular Function | enzyme binding | |
Molecular Function | mRNA binding | |
Molecular Function | serine-type endopeptidase inhibitor activity | |
Biological Process | antibacterial humoral response | |
Biological Process | immune response | |
Biological Process | innate immune response | |
Biological Process | modulation of process of another organism | |
Biological Process | negative regulation of viral genome replication | |
Biological Process | response to lipopolysaccharide |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAntileukoproteinase
- Short namesALP
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP97430
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 39-40 | Loss of antimicrobial activity. | ||||
Sequence: KK → DD | ||||||
Mutagenesis | 92 | Loss of antimicrobial activity; when associated with A-96. | ||||
Sequence: K → D | ||||||
Mutagenesis | 96 | Loss of antimicrobial activity; when associated with A-92. | ||||
Sequence: R → D |
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.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MKSCGLLPFTVLLALGILAPWTVEG | ||||||
Chain | PRO_0000041356 | 26-131 | Antileukoproteinase | |||
Sequence: GKNDAIKIGACPAKKPAQCLKLEKPQCRTDWECPGKQRCCQDACGSKCVNPVPIRKPVWRKPGRCVKTQARCMMLNPPNVCQRDGQCDGKYKCCEGICGKVCLPPM | ||||||
Disulfide bond | 36↔65 | |||||
Sequence: CPAKKPAQCLKLEKPQCRTDWECPGKQRCC | ||||||
Disulfide bond | 44↔69 | |||||
Sequence: CLKLEKPQCRTDWECPGKQRCCQDAC | ||||||
Disulfide bond | 52↔64 | |||||
Sequence: CRTDWECPGKQRC | ||||||
Disulfide bond | 58↔73 | |||||
Sequence: CPGKQRCCQDACGSKC | ||||||
Disulfide bond | 90↔119 | |||||
Sequence: CVKTQARCMMLNPPNVCQRDGQCDGKYKCC | ||||||
Disulfide bond | 97↔123 | |||||
Sequence: CMMLNPPNVCQRDGQCDGKYKCCEGIC | ||||||
Disulfide bond | 106↔118 | |||||
Sequence: CQRDGQCDGKYKC | ||||||
Disulfide bond | 112↔127 | |||||
Sequence: CDGKYKCCEGICGKVC |
Keywords
- PTM
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
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).
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
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 29-77 | WAP 1 | ||||
Sequence: DAIKIGACPAKKPAQCLKLEKPQCRTDWECPGKQRCCQDACGSKCVNPV | ||||||
Domain | 83-131 | WAP 2 | ||||
Sequence: VWRKPGRCVKTQARCMMLNPPNVCQRDGQCDGKYKCCEGICGKVCLPPM | ||||||
Region | 85-131 | Elastase inhibitory domain | ||||
Sequence: RKPGRCVKTQARCMMLNPPNVCQRDGQCDGKYKCCEGICGKVCLPPM |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length131
- Mass (Da)14,308
- Last updated1997-05-01 v1
- ChecksumA57C9E30FE711B8F
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |