SLPI_PIG
ID SLPI_PIG Reviewed; 129 AA.
AC P22298;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Antileukoproteinase;
DE Short=ALP;
DE AltName: Full=Secretory leukocyte protease inhibitor;
DE Flags: Precursor; Fragment;
GN Name=SLPI; Synonyms=ALP {ECO:0000303|PubMed:1547723};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Uterus;
RX PubMed=2293019; DOI=10.1210/mend-4-8-1095;
RA Farmer S.J., Fliss A.E., Simmen R.C.M.;
RT "Complementary DNA cloning and regulation of expression of the messenger
RT RNA encoding a pregnancy-associated porcine uterine protein related to
RT human antileukoproteinase.";
RL Mol. Endocrinol. 4:1095-1104(1990).
RN [2]
RP PROTEIN SEQUENCE OF 23-40, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=1547723; DOI=10.1210/endo.130.4.1547723;
RA Simmen R.C., Michel F.J., Fliss A.E., Smith L.C., Fliss M.F.;
RT "Ontogeny, immunocytochemical localization, and biochemical properties of
RT the pregnancy-associated uterine elastase/cathepsin-G protease inhibitor,
RT antileukoproteinase (ALP): monospecific antibodies to a synthetic peptide
RT recognize native ALP.";
RL Endocrinology 130:1957-1965(1992).
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:1547723}.
CC -!- TISSUE SPECIFICITY: Found in pregnant endometrium and myometrium,
CC placenta, allantoic fluids, fetal cord blood, and fetal liver. Also
CC found in uterus and lung. {ECO:0000269|PubMed:1547723}.
CC -!- DEVELOPMENTAL STAGE: Levels in endometrium, allantoic fluids, and fetal
CC cord blood change with the stage of pregnancy. Maximal expression found
CC at mid- and late gestation (at protein level).
CC {ECO:0000269|PubMed:1547723}.
CC -!- INDUCTION: By estrogen and progesterone; in uterus.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA63446.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M57446; AAA63446.1; ALT_SEQ; mRNA.
DR PIR; A36113; A36113.
DR RefSeq; NP_999035.1; NM_213870.1.
DR STRING; 9823.ENSSSCP00000024994; -.
DR MEROPS; I17.001; -.
DR MEROPS; I17.950; -.
DR PaxDb; P22298; -.
DR PeptideAtlas; P22298; -.
DR GeneID; 396886; -.
DR KEGG; ssc:396886; -.
DR CTD; 6590; -.
DR eggNOG; ENOG502SWIR; Eukaryota.
DR InParanoid; P22298; -.
DR OrthoDB; 1560605at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; 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; Direct protein sequencing; Disulfide bond;
KW Immunity; Innate immunity; Protease inhibitor; Reference proteome; Repeat;
KW Secreted; Serine protease inhibitor; Signal.
FT SIGNAL <1..22
FT /evidence="ECO:0000269|PubMed:1547723"
FT CHAIN 23..129
FT /note="Antileukoproteinase"
FT /id="PRO_0000188985"
FT DOMAIN 25..73
FT /note="WAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 79..127
FT /note="WAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT REGION 81..129
FT /note="Elastase inhibitory domain"
FT SITE 94..95
FT /note="Reactive bond for chymotrypsin, trypsin and
FT elastase"
FT /evidence="ECO:0000250|UniProtKB:P03973"
FT DISULFID 32..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 40..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 48..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 54..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 86..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 93..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 102..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DISULFID 108..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT NON_TER 1
SQ SEQUENCE 129 AA; 13919 MW; 0390D3DE28A9655C CRC64;
GRGLLPFVLL ALGIXAPWAV EGAENALKGG ACPPRKIVQC LRYEKPKCTS DWQCPDKKKC
CRDTCAIKCL NPVAITNPVK VKPGKCPVVY GQCMMLNPPN HCKTDSQCLG DLKCCKSMCG
KVCLTPVKA
