ID   SLPI_SHEEP              Reviewed;         132 AA.
AC   Q6V9X0;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Antileukoproteinase;
DE            Short=ALP;
DE   AltName: Full=Secretory leukocyte protease inhibitor;
DE   Flags: Precursor;
GN   Name=SLPI;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION BY BACTERIAL LIPOPOLYSACCHARIDE.
RX   PubMed=15292488; DOI=10.1152/physiolgenomics.00113.2004;
RA   Brown T.I., Mistry R., Collie D.D., Tate S., Sallenave J.-M.;
RT   "Trappin ovine molecule (TOM), the ovine ortholog of elafin, is an acute
RT   phase reactant in the lung.";
RL   Physiol. Genomics 19:11-21(2004).
CC   -!- FUNCTION: Acid-stable proteinase inhibitor with strong affinities for
CC       trypsin, chymotrypsin, elastase, and cathepsin G. Modulates the
CC       inflammatory and immune responses after bacterial infection, and after
CC       infection by the intracellular parasite L.major. Down-regulates
CC       responses to bacterial lipopolysaccharide (LPS). Plays a role in
CC       regulating the activation of NF-kappa-B and inflammatory responses. Has
CC       antimicrobial activity against mycobacteria, but not against
CC       salmonella. Contributes to normal resistance against infection by
CC       M.tuberculosis. Required for normal resistance to infection by L.major.
CC       Required for normal wound healing, probably by preventing tissue damage
CC       by limiting protease activity (By similarity). Together with ELANE,
CC       required for normal differentiation and proliferation of bone marrow
CC       myeloid cells (By similarity). {ECO:0000250|UniProtKB:P03973,
CC       ECO:0000250|UniProtKB:P97430}.
CC   -!- SUBUNIT: Interacts with GRN; interaction protects progranulin from
CC       proteolysis. {ECO:0000250|UniProtKB:P03973}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15292488}.
CC   -!- TISSUE SPECIFICITY: Detected in bronchoalveolar fluid (at protein
CC       level). Detected in large and small intestine, trachea, skin, lung and
CC       tongue. {ECO:0000269|PubMed:15292488}.
CC   -!- INDUCTION: Up-regulated in response to bacterial lipopolysaccharide
CC       (LPS) in bronchoalveolar fluid (at protein level).
CC       {ECO:0000269|PubMed:15292488}.
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DR   EMBL; AY346135; AAQ23185.1; -; Genomic_DNA.
DR   RefSeq; NP_001030302.1; NM_001035225.1.
DR   AlphaFoldDB; Q6V9X0; -.
DR   SMR; Q6V9X0; -.
DR   STRING; 9940.ENSOARP00000005324; -.
DR   MEROPS; I17.001; -.
DR   MEROPS; I17.950; -.
DR   GeneID; 641306; -.
DR   KEGG; oas:641306; -.
DR   CTD; 6590; -.
DR   eggNOG; ENOG502SWIR; Eukaryota.
DR   OrthoDB; 1560605at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0019731; P:antibacterial humoral response; ISS:UniProtKB.
DR   GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR   Gene3D; 4.10.75.10; -; 2.
DR   InterPro; IPR036645; Elafin-like_sf.
DR   InterPro; IPR008197; WAP_dom.
DR   Pfam; PF00095; WAP; 2.
DR   PRINTS; PR00003; 4DISULPHCORE.
DR   SMART; SM00217; WAP; 2.
DR   SUPFAM; SSF57256; SSF57256; 2.
DR   PROSITE; PS51390; WAP; 2.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Disulfide bond; Glycoprotein; Immunity;
KW   Innate immunity; Protease inhibitor; Reference proteome; Repeat; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..132
FT                   /note="Antileukoproteinase"
FT                   /id="PRO_0000279743"
FT   DOMAIN          28..76
FT                   /note="WAP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DOMAIN          82..130
FT                   /note="WAP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   SITE            97..98
FT                   /note="Reactive bond for chymotrypsin, trypsin and
FT                   elastase"
FT                   /evidence="ECO:0000250|UniProtKB:P03973"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        43..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        51..63
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        57..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        89..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        96..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        105..117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        111..126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
SQ   SEQUENCE   132 AA;  14197 MW;  A8D2A39A1A1DE901 CRC64;
     MKFSGLFPFL LLALGTLALW AVEGAENEAL KAGACPPRKS AQCFGNEKPR CSSDWQCPHK
     KKCCLDTCGT ECLDPVNITN PVKKKPGTCP VIHGQCLMLK PLNHCETDDQ CIGALKCCKA
     MCGKVCLSPV KA