Secretory leukocyte protease inhibitor

SLPI
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2Z7F, 4DOQ
Identifiers
Aliases	SLPI, ALK1, ALP, BLPI, HUSI, HUSI-I, MPI, WAP4, WFDC4, secretory leukocyte peptidase inhibitor
External IDs	HomoloGene: 2305 GeneCards: SLPI
Gene location (Human) Chr. Chromosome 20 (human) Band 20q13.12 Start 45,252,239 bp End 45,254,564 bp
RNA expression pattern More reference expression data
Gene ontology Molecular function • peptidase inhibitor activity • enzyme binding • protein binding • serine-type endopeptidase inhibitor activity • DNA binding • mRNA binding • endopeptidase inhibitor activity Cellular component • extracellular matrix • extracellular exosome • extracellular region • extracellular space • Golgi apparatus • specific granule lumen Biological process • antibacterial humoral response • response to lipopolysaccharide • negative regulation of viral genome replication • negative regulation of peptidase activity • innate immune response • negative regulation of protein binding • defense response to bacterium • immune response • negative regulation of endopeptidase activity • immune system process • neutrophil degranulation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6590	n/a
Ensembl	ENSG00000124107	n/a
UniProt	P03973	n/a
RefSeq (mRNA)	NM_003064	n/a
RefSeq (protein)	NP_003055	n/a
Location (UCSC)	Chr 20: 45.25 – 45.25 Mb	n/a
PubMed search		n/a

2Z7F, 4DOQ

6590

n/a

ENSG00000124107

n/a

P03973

n/a

NM_003064

n/a

NP_003055

n/a

Antileukoproteinase, also known as secretory leukocyte protease inhibitor (SLPI), is an enzyme that in humans is encoded by the SLPI gene. SLPI is a highly cationic single-chain protein with eight intramolecular disulfide bonds. It is found in large quantities in bronchial, cervical, and nasal mucosa, saliva, and seminal fluids. SLPI inhibits human leukocyte elastase, human cathepsin G, human trypsin, neutrophil elastase, and mast cell chymase. X-ray crystallography has shown that SLPI has two homologous domains of 53 and 54 amino acids, one of which exhibits anti-protease activity (C-terminal domain). The other domain (N-terminal domain) is not known to have any function.

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