ID   ILEU_XENLA              Reviewed;         377 AA.
AC   Q52L45;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Leukocyte elastase inhibitor;
DE   AltName: Full=Serpin B1;
GN   Name=serpinb1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates the activity of the neutrophil proteases.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC094073; AAH94073.1; -; mRNA.
DR   RefSeq; NP_001089382.1; NM_001095913.1.
DR   RefSeq; XP_018122179.1; XM_018266690.1.
DR   AlphaFoldDB; Q52L45; -.
DR   SMR; Q52L45; -.
DR   BioGRID; 592213; 1.
DR   MEROPS; I04.006; -.
DR   DNASU; 734432; -.
DR   GeneID; 734432; -.
DR   KEGG; xla:734432; -.
DR   CTD; 734432; -.
DR   Xenbase; XB-GENE-1217270; serpinb1.L.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 734432; Expressed in intestine and 20 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor.
FT   CHAIN           1..377
FT                   /note="Leukocyte elastase inhibitor"
FT                   /id="PRO_0000289124"
FT   SITE            344..345
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   377 AA;  42698 MW;  8DFBEFB1E69517A7 CRC64;
     MENLSSACTH FCFDLFKKIN ENNSTGNLFF SPISLSTALA MVFLGTKGKT AEQMSKTLHF
     DAVKDLHSNF QTLNAEINKK DVSTYALNLA NRLFGEKTFN FLPNFLSSVK KQYSADLGTV
     DFISALEDAR KEINKWVSEQ TKGKIPEVLS TGTVDRSTKL VLVNAIYFKG DWAKKFNAEH
     TTDMPFQLNK KEQKTVKMMY QKEKLPFNYI PDINCRILEL PYVDYELSMI IILPDNINDD
     TTGLQQLEKE LSLEKIHEWT ENMMPTDVHI HLPKFKLEDS YKLKSQLAGM GMVDLFNSGS
     ADLSGMSGSN NLFLSEVIHK SFVEVNEEGT EAAAASAGIA MMCMMREEEF NADHPFLFLI
     RHNATKSILF FGRYSSP