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Antileukoproteinase (ALP) (Secretory leukocyte protease inhibitor)

 SLPI_MOUSE              Reviewed;         131 AA.
P97430; O09081; O09082;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
12-SEP-2018, entry version 141.
RecName: Full=Antileukoproteinase;
Short=ALP;
AltName: Full=Secretory leukocyte protease inhibitor {ECO:0000303|PubMed:9039268};
Flags: Precursor;
Name=Slpi;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY BACTERIAL
LIPOPOLYSACCHARIDE, AND TISSUE SPECIFICITY.
PubMed=9039268; DOI=10.1016/S0092-8674(00)81880-2;
Jin F.-Y., Nathan C.F., Radzioch D., Ding A.;
"Secretory leukocyte protease inhibitor: a macrophage product induced
by and antagonistic to bacterial lipopolysaccharide.";
Cell 88:417-426(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-51, FUNCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9126337; DOI=10.1006/bbrc.1997.6358;
Zitnik R.J., Zhang J., Kashem M.A., Kohno T., Lyons D.E., Wright C.D.,
Rosen E., Goldberg I., Hayday A.C.;
"The cloning and characterization of a murine secretory leukocyte
protease inhibitor cDNA.";
Biochem. Biophys. Res. Commun. 232:687-697(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY
PNEUMONIA.
STRAIN=C57BL/6 X CBA; TISSUE=Lung;
PubMed=9351627; DOI=10.1164/ajrccm.156.4.9701075;
Abe T., Tominaga Y., Kikuchi T., Watanabe A., Satoh K., Watanabe Y.,
Nukiwa T.;
"Bacterial pneumonia causes augmented expression of the secretory
leukoprotease inhibitor gene in the murine lung.";
Am. J. Respir. Crit. Care Med. 156:1235-1240(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DISRUPTION PHENOTYPE, FUNCTION, AND INDUCTION BY WOUNDING.
PubMed=11017147; DOI=10.1038/80489;
Ashcroft G.S., Lei K., Jin W., Longenecker G., Kulkarni A.B.,
Greenwell-Wild T., Hale-Donze H., McGrady G., Song X.Y., Wahl S.M.;
"Secretory leukocyte protease inhibitor mediates non-redundant
functions necessary for normal wound healing.";
Nat. Med. 6:1147-1153(2000).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=12615907; DOI=10.1084/jem.20021824;
Nakamura A., Mori Y., Hagiwara K., Suzuki T., Sakakibara T.,
Kikuchi T., Igarashi T., Ebina M., Abe T., Miyazaki J., Takai T.,
Nukiwa T.;
"Increased susceptibility to LPS-induced endotoxin shock in secretory
leukoprotease inhibitor (SLPI)-deficient mice.";
J. Exp. Med. 197:669-674(2003).
[7]
DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF 39-LYS-LYS-40; LYS-92 AND ARG-96.
PubMed=18322212; DOI=10.4049/jimmunol.180.6.4032;
Nishimura J., Saiga H., Sato S., Okuyama M., Kayama H., Kuwata H.,
Matsumoto S., Nishida T., Sawa Y., Akira S., Yoshikai Y., Yamamoto M.,
Takeda K.;
"Potent antimycobacterial activity of mouse secretory leukocyte
protease inhibitor.";
J. Immunol. 180:4032-4039(2008).
[8]
DISRUPTION PHENOTYPE, FUNCTION, AND INDUCTION.
PubMed=25030421; DOI=10.1189/jlb.4A0612-295RR;
McCartney-Francis N., Jin W., Belkaid Y., McGrady G., Wahl S.M.;
"Aberrant host defense against Leishmania major in the absence of
SLPI.";
J. Leukoc. Biol. 96:917-929(2014).
-!- 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:9039268, PubMed:12615907,
PubMed:25030421). 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). {ECO:0000250|UniProtKB:P03973,
ECO:0000269|PubMed:11017147, ECO:0000269|PubMed:12615907,
ECO:0000269|PubMed:18322212, ECO:0000269|PubMed:25030421,
ECO:0000269|PubMed:9039268, ECO:0000269|PubMed:9126337,
ECO:0000269|PubMed:9351627, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18322212,
ECO:0000269|PubMed:9126337}.
-!- 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.
{ECO:0000269|PubMed:18322212, ECO:0000269|PubMed:9039268,
ECO:0000269|PubMed:9126337, ECO:0000269|PubMed:9351627}.
-!- INDUCTION: Up-regulated by bacterial lipopolysaccharide
(PubMed:9039268, PubMed:25030421). 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).
{ECO:0000269|PubMed:11017147, ECO:0000269|PubMed:18322212,
ECO:0000269|PubMed:25030421, ECO:0000269|PubMed:9039268,
ECO:0000269|PubMed:9351627}.
-!- 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).
{ECO:0000269|PubMed:11017147, ECO:0000269|PubMed:12615907,
ECO:0000269|PubMed:18322212, ECO:0000269|PubMed:25030421}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U73004; AAC53047.1; -; mRNA.
EMBL; U88093; AAC53140.1; -; mRNA.
EMBL; U94341; AAC53394.1; -; mRNA.
EMBL; BC028509; AAH28509.1; -; mRNA.
CCDS; CCDS17033.1; -.
RefSeq; NP_035544.1; NM_011414.3.
UniGene; Mm.371583; -.
ProteinModelPortal; P97430; -.
SMR; P97430; -.
BioGrid; 203333; 1.
STRING; 10090.ENSMUSP00000104992; -.
MEROPS; I17.001; -.
PhosphoSitePlus; P97430; -.
PaxDb; P97430; -.
PRIDE; P97430; -.
Ensembl; ENSMUST00000109367; ENSMUSP00000104992; ENSMUSG00000017002.
GeneID; 20568; -.
KEGG; mmu:20568; -.
UCSC; uc008nuj.1; mouse.
CTD; 6590; -.
MGI; MGI:109297; Slpi.
eggNOG; ENOG410J417; Eukaryota.
eggNOG; ENOG41116TS; LUCA.
GeneTree; ENSGT00730000111217; -.
HOGENOM; HOG000115819; -.
HOVERGEN; HBG018073; -.
InParanoid; P97430; -.
OMA; SDWQCPG; -.
OrthoDB; EOG091G0S8U; -.
PhylomeDB; P97430; -.
TreeFam; TF338375; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
PRO; PR:P97430; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000017002; Expressed in 169 organ(s), highest expression level in esophagus.
CleanEx; MM_SLPI; -.
ExpressionAtlas; P97430; baseline and differential.
Genevisible; P97430; MM.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0003729; F:mRNA binding; ISO:MGI.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISS:UniProtKB.
GO; GO:0019731; P:antibacterial humoral response; IMP:UniProtKB.
GO; GO:0006955; P:immune response; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0035821; P:modification of morphology or physiology of other organism; ISO:MGI.
GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
Gene3D; 4.10.75.10; -; 2.
InterPro; IPR036645; Elafin-like_sf.
InterPro; IPR008197; WAP_dom.
Pfam; PF00095; WAP; 2.
PRINTS; PR00003; 4DISULPHCORE.
SMART; SM00217; WAP; 2.
SUPFAM; SSF57256; SSF57256; 2.
PROSITE; PS51390; WAP; 2.
1: Evidence at protein level;
Antibiotic; Antimicrobial; Complete proteome;
Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
Protease inhibitor; Reference proteome; Repeat; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 25 {ECO:0000269|PubMed:9126337}.
CHAIN 26 131 Antileukoproteinase.
/FTId=PRO_0000041356.
DOMAIN 29 77 WAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00722}.
DOMAIN 83 131 WAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00722}.
REGION 85 131 Elastase inhibitory domain.
SITE 98 99 Reactive bond for chymotrypsin, trypsin
and elastase.
{ECO:0000250|UniProtKB:P03973}.
DISULFID 36 65 {ECO:0000255|PROSITE-ProRule:PRU00722}.
DISULFID 44 69 {ECO:0000255|PROSITE-ProRule:PRU00722}.
DISULFID 52 64 {ECO:0000255|PROSITE-ProRule:PRU00722}.
DISULFID 58 73 {ECO:0000255|PROSITE-ProRule:PRU00722}.
DISULFID 90 119 {ECO:0000255|PROSITE-ProRule:PRU00722}.
DISULFID 97 123 {ECO:0000255|PROSITE-ProRule:PRU00722}.
DISULFID 106 118 {ECO:0000255|PROSITE-ProRule:PRU00722}.
DISULFID 112 127 {ECO:0000255|PROSITE-ProRule:PRU00722}.
MUTAGEN 39 40 KK->DD: Loss of antimicrobial activity.
{ECO:0000269|PubMed:18322212}.
MUTAGEN 92 92 K->D: Loss of antimicrobial activity;
when associated with A-96.
{ECO:0000269|PubMed:18322212}.
MUTAGEN 96 96 R->D: Loss of antimicrobial activity;
when associated with A-92.
{ECO:0000269|PubMed:18322212}.
SEQUENCE 131 AA; 14308 MW; A57C9E30FE711B8F CRC64;
MKSCGLLPFT VLLALGILAP WTVEGGKNDA IKIGACPAKK PAQCLKLEKP QCRTDWECPG
KQRCCQDACG SKCVNPVPIR KPVWRKPGRC VKTQARCMML NPPNVCQRDG QCDGKYKCCE
GICGKVCLPP M


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