ID   ILEUA_RAT               Reviewed;         379 AA.
AC   Q4G075;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Leukocyte elastase inhibitor A;
DE   AltName: Full=Serine protease inhibitor EIA;
DE   AltName: Full=Serpin B1a;
GN   Name=Serpinb1a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Regulates the activity of the neutrophil proteases.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
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; BC098686; AAH98686.1; -; mRNA.
DR   RefSeq; NP_001026812.1; NM_001031642.1.
DR   AlphaFoldDB; Q4G075; -.
DR   SMR; Q4G075; -.
DR   STRING; 10116.ENSRNOP00000056600; -.
DR   MEROPS; I04.049; -.
DR   iPTMnet; Q4G075; -.
DR   PhosphoSitePlus; Q4G075; -.
DR   jPOST; Q4G075; -.
DR   PaxDb; Q4G075; -.
DR   PRIDE; Q4G075; -.
DR   Ensembl; ENSRNOT00000059854; ENSRNOP00000056600; ENSRNOG00000016581.
DR   GeneID; 291091; -.
DR   KEGG; rno:291091; -.
DR   UCSC; RGD:1306203; rat.
DR   CTD; 66222; -.
DR   RGD; 1306203; Serpinb1a.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000154573; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; Q4G075; -.
DR   OMA; CMAIEED; -.
DR   OrthoDB; 1124079at2759; -.
DR   PhylomeDB; Q4G075; -.
DR   TreeFam; TF352619; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q4G075; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   Bgee; ENSRNOG00000016581; Expressed in duodenum and 20 other tissues.
DR   Genevisible; Q4G075; RN.
DR   GO; GO:0044194; C:cytolytic granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030414; F:peptidase inhibitor activity; ISO:RGD.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0019725; P:cellular homeostasis; ISO:RGD.
DR   GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:RGD.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:RGD.
DR   GO; GO:0045088; P:regulation of innate immune response; ISO:RGD.
DR   GO; GO:0042176; P:regulation of protein catabolic process; ISO:RGD.
DR   GO; GO:0044342; P:type B pancreatic cell proliferation; ISO:RGD.
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   Cytoplasm; Endosome; Lysosome; Phosphoprotein; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor.
FT   CHAIN           1..379
FT                   /note="Leukocyte elastase inhibitor A"
FT                   /id="PRO_0000289123"
FT   SITE            344..345
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   379 AA;  42727 MW;  2335D7C019FF849C CRC64;
     MEQLSSANSL FALELFHTLS ESSPTGNIFF SPFSISSALA MVFLGTKGTT AAQLSKTFHF
     DSVEDVHSRF QSLNAEVSKR GASHTLKLAN RLYGEKTYNF LPEFLTSTQK MYGADLAPVD
     FQHASEDARK EINQWVKGQT EGKIPELLAV GVVDSMTKLV LVNAIYFKGM WEEKFMKQDT
     TDAPFRLNKK NTKSVKMMYQ KKKFFFGYIS DLKCKVLEMP YQGGELSMVI LLPEDIEDES
     TGLKKIEEQI TLEKLREWTK RENLENIDVH VKLPRFKIEE SYILNSNLGR LGLQDLFNSS
     KADLSGMSGS RDLFISKIVH KAFVEVNEEG TEAAAATAGI ATFCMLLPEE EFTADHPFIF
     FIRHNPTANV LFLGRVCSP