ILEU_BOVIN
ID ILEU_BOVIN Reviewed; 377 AA.
AC Q1JPB0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Leukocyte elastase inhibitor;
DE Short=LEI;
DE AltName: Full=Serpin B1;
GN Name=SERPINB1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-330.
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Neutrophil serine protease inhibitor that plays an essential
CC role in the regulation of the innate immune response, inflammation and
CC cellular homeostasis. Acts primarily to protect the cell from proteases
CC released in the cytoplasm during stress or infection. These proteases
CC are important in killing microbes but when released from granules,
CC these potent enzymes also destroy host proteins and contribute to
CC mortality. Regulates the activity of the neutrophil proteases elastase,
CC cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3.
CC Acts also as a potent intracellular inhibitor of GZMH by directly
CC blocking its proteolytic activity. During inflammation, limits the
CC activity of inflammatory caspases CASP1, CASP4 and CASP5 by suppressing
CC their caspase-recruitment domain (CARD) oligomerization and enzymatic
CC activation. When secreted, promotes the proliferation of beta-cells via
CC its protease inhibitory function. {ECO:0000250|UniProtKB:P30740}.
CC -!- SUBUNIT: Monomer. Interacts (via C-terminus) with CASP1; CASP4 (via
CC CARD domain) and CASP5; these interactions regulate the activity of
CC inflammatory caspases. Interacts with PRTN3. Interacts with GZMH.
CC {ECO:0000250|UniProtKB:P30740}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P30740}.
CC Cytoplasm {ECO:0000250|UniProtKB:P30740}. Cytolytic granule
CC {ECO:0000250|UniProtKB:P30740}. Early endosome
CC {ECO:0000250|UniProtKB:P30740}.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
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DR EMBL; BT025443; ABF57399.1; -; mRNA.
DR RefSeq; NP_001193539.1; NM_001206610.1.
DR AlphaFoldDB; Q1JPB0; -.
DR SMR; Q1JPB0; -.
DR STRING; 9913.ENSBTAP00000015889; -.
DR MEROPS; I04.006; -.
DR PaxDb; Q1JPB0; -.
DR PeptideAtlas; Q1JPB0; -.
DR PRIDE; Q1JPB0; -.
DR Ensembl; ENSBTAT00000015889; ENSBTAP00000015889; ENSBTAG00000011975.
DR GeneID; 507264; -.
DR KEGG; bta:507264; -.
DR CTD; 1992; -.
DR VEuPathDB; HostDB:ENSBTAG00000011975; -.
DR VGNC; VGNC:34470; SERPINB1.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154573; -.
DR InParanoid; Q1JPB0; -.
DR OrthoDB; 1124079at2759; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000011975; Expressed in olfactory segment of nasal mucosa and 101 other tissues.
DR ExpressionAtlas; Q1JPB0; baseline and differential.
DR GO; GO:0044194; C:cytolytic granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IBA:GO_Central.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR015557; Serpin_B1.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR PANTHER; PTHR11461:SF180; PTHR11461:SF180; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Disulfide bond; Endosome; Lysosome; Phosphoprotein;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor.
FT CHAIN 1..377
FT /note="Leukocyte elastase inhibitor"
FT /id="PRO_0000289119"
FT REGION 349..377
FT /note="CARD-binding motif (CBM)"
FT /evidence="ECO:0000250|UniProtKB:P30740"
FT SITE 342..343
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P30740"
FT MOD_RES 136
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30740"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30740"
FT DISULFID 79
FT /note="Interchain"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 42236 MW; 91EBD2E4FBA7D329 CRC64;
MEQLSAANTR FAVDLFLTLT EHNPAGNIFI SPFSISSALA MVFLGARGDT AAQMSKALHF
EGVEIHSGFQ SLNADINKCG APYTLKLANR LFGEKSYDFL PEFLASTQEM YSAELASVDF
LRAPEDARKT INAWVKEQTG GKIPELLASG MVDSLTKLVL VNAIYFKGKW QEKFMVEATK
DAPFRLNKKE TKTVKMMYQK KKFPFGYIKD LKCRVLELPY EGKDLSMVIL LPDDIQDEAT
GLKKIEQQLT LEKLREWTRP ESLDLLEVRV QLPRFKLEES YDLQEPLARL GVRDLFSSKA
DLSGMSGAKD LFISKVVHKS VVDVNEEGTE AAAATGAIAE FAMLVPEEEF VADHPFIFFI
RHKPSSNILF LGRLSSP
