ILEU_PIG
ID ILEU_PIG Reviewed; 378 AA.
AC P80229;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Leukocyte elastase inhibitor;
DE Short=LEI;
DE AltName: Full=Leukocyte neutral proteinase inhibitor;
DE Short=LNPI;
DE AltName: Full=Serpin B1;
GN Name=SERPINB1; Synonyms=ELANH2;
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 PROTEIN SEQUENCE.
RC TISSUE=Leukocyte;
RX PubMed=7901009; DOI=10.1111/j.1432-1033.1993.tb18272.x;
RA Teschauer W.F., Mentele R., Sommerhoff C.P.;
RT "Primary structure of a porcine leukocyte serpin.";
RL Eur. J. Biochem. 217:519-526(1993).
RN [2]
RP PROTEIN SEQUENCE OF 57-65; 66-74; 97-107; 111-123; 291-301 AND 311-316, AND
RP FUNCTION.
RX PubMed=9584202; DOI=10.1128/mcb.18.6.3612;
RA Torriglia A., Perani P., Brossas J.Y., Chaudun E., Treton J., Courtois Y.,
RA Counis M.F.;
RT "L-DNase II, a molecule that links proteases and endonucleases in
RT apoptosis, derives from the ubiquitous serpin leukocyte elastase
RT inhibitor.";
RL Mol. Cell. Biol. 18:3612-3619(1998).
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 -!- FUNCTION: May be cleaved leading to a loss of its anti-protease
CC activity and to the appearance of an endonuclease activity. However no
CC catalytic site was identified. {ECO:0000269|PubMed:9584202}.
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 PIR; S38962; S38962.
DR AlphaFoldDB; P80229; -.
DR SMR; P80229; -.
DR STRING; 9823.ENSSSCP00000001081; -.
DR MEROPS; I04.006; -.
DR PaxDb; P80229; -.
DR PeptideAtlas; P80229; -.
DR PRIDE; P80229; -.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; P80229; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Endosome; Lysosome; Phosphoprotein; Protease inhibitor; Reference proteome;
KW Secreted; Serine protease inhibitor.
FT CHAIN 1..378
FT /note="Leukocyte elastase inhibitor"
FT /id="PRO_0000094102"
FT REGION 350..378
FT /note="CARD-binding motif (CBM)"
FT /evidence="ECO:0000250|UniProtKB:P30740"
FT SITE 343..344
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 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30740"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30740"
FT DISULFID 80
FT /note="Interchain"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42513 MW; 3CA7C65F11E508CA CRC64;
MEQLSAANTR FALDLFRALN ESNPAGNIFI SPFSISSALA MILLGTRGNT EAQMSKALHF
DTVKDIHSRF QSLNADINKC GASYILKLAN RLFGEKTYHF LPEFLASTQK TYGAELASVD
FLRASEEARK AINEWVKEQT EGKIPELLAS GVVDSATKLV LVNAIYFKGS WQEKFMTEAT
KDAPFRLNKK DSKTVKMMYQ KKKFPFGYIK ELKCRVLELP YQGKDLSMVI LLPDSIEDES
TGLRKIEQHL TLEKLNEWTK PDNLELLEVN VHLPRFRLEE SYDLNAPLAR LGVQDLFGSR
ADLTGMSEAR DLFISKVVHK AFVEVNEEGT EAAAATAGIA VFAMLMPEED FIADHPFIFF
IRHNPSSNIL FLGRLSSP
