ILEUB_MOUSE
ID ILEUB_MOUSE Reviewed; 382 AA.
AC Q8VHP7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Leukocyte elastase inhibitor B;
DE AltName: Full=Serine protease inhibitor EIB;
DE AltName: Full=Serpin B1b;
GN Name=Serpinb1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129S6/SvEvTac, and BALB/cJ; TISSUE=Lung, and Spleen;
RX PubMed=11863365; DOI=10.1006/geno.2002.6716;
RA Kaiserman D., Knaggs S., Scarff K.L., Gillard A., Mirza G., Cadman M.,
RA McKeone R., Denny P., Cooley J., Benarafa C., Remold-O'Donnell E.,
RA Ragoussis J., Bird P.I.;
RT "Comparison of human chromosome 6p25 with mouse chromosome 13 reveals a
RT greatly expanded ov-serpin gene repertoire in the mouse.";
RL Genomics 79:349-362(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH CTSG, AND
RP TISSUE SPECIFICITY.
RC STRAIN=129S6/SvEvTac; TISSUE=Spleen;
RX PubMed=12189154; DOI=10.1074/jbc.m207080200;
RA Benarafa C., Cooley J., Zeng W., Bird P.I., Remold-O'Donnell E.;
RT "Characterization of four murine homologs of the human ov-serpin monocyte
RT neutrophil elastase inhibitor MNEI (SERPINB1).";
RL J. Biol. Chem. 277:42028-42033(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND INTERACTION WITH CASP1 AND CASP4.
RX PubMed=30692621; DOI=10.1038/s41590-018-0303-z;
RA Choi Y.J., Kim S., Choi Y., Nielsen T.B., Yan J., Lu A., Ruan J., Lee H.R.,
RA Wu H., Spellberg B., Jung J.U.;
RT "SERPINB1-mediated checkpoint of inflammatory caspase activation.";
RL Nat. Immunol. 20:276-287(2019).
CC -!- FUNCTION: Regulates the activity of the neutrophil proteases. Forms
CC only a stable complex with CTSG/Cathepsin G (PubMed:12189154). During
CC inflammation, limits the activity of inflammatory caspases CASP1 and
CC CASP4 by suppressing their caspase-recruitment domain (CARD)
CC oligomerization and enzymatic activation (PubMed:30692621).
CC {ECO:0000269|PubMed:12189154, ECO:0000269|PubMed:30692621}.
CC -!- SUBUNIT: Monomer. Interacts (via C-terminus) with CASP1 and CASP4 (via
CC CARD domain); these interactions regulate the activity of inflammatory
CC caspases. {ECO:0000269|PubMed:30692621}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain with lower expression in lung,
CC spleen and testis. {ECO:0000269|PubMed:12189154}.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
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DR EMBL; AF426025; AAL57487.1; -; mRNA.
DR EMBL; AF521698; AAM95934.1; -; Genomic_DNA.
DR EMBL; AL589871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030354; AAH30354.1; -; mRNA.
DR CCDS; CCDS26433.1; -.
DR RefSeq; NP_766640.1; NM_173052.2.
DR RefSeq; XP_006516747.1; XM_006516684.1.
DR AlphaFoldDB; Q8VHP7; -.
DR SMR; Q8VHP7; -.
DR STRING; 10090.ENSMUSP00000016951; -.
DR MEROPS; I04.006; -.
DR iPTMnet; Q8VHP7; -.
DR PhosphoSitePlus; Q8VHP7; -.
DR UCD-2DPAGE; Q8VHP7; -.
DR MaxQB; Q8VHP7; -.
DR PaxDb; Q8VHP7; -.
DR PeptideAtlas; Q8VHP7; -.
DR PRIDE; Q8VHP7; -.
DR ProteomicsDB; 267238; -.
DR DNASU; 282663; -.
DR Ensembl; ENSMUST00000016951; ENSMUSP00000016951; ENSMUSG00000051029.
DR GeneID; 282663; -.
DR KEGG; mmu:282663; -.
DR UCSC; uc007qab.2; mouse.
DR CTD; 282663; -.
DR MGI; MGI:2445361; Serpinb1b.
DR VEuPathDB; HostDB:ENSMUSG00000051029; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154573; -.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; Q8VHP7; -.
DR OMA; RKNINAW; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q8VHP7; -.
DR TreeFam; TF352619; -.
DR BioGRID-ORCS; 282663; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8VHP7; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8VHP7; protein.
DR Bgee; ENSMUSG00000051029; Expressed in choroid plexus epithelium and 88 other tissues.
DR Genevisible; Q8VHP7; MM.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030414; F:peptidase inhibitor activity; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:MGI.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:MGI.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IMP:UniProtKB.
DR GO; GO:0042176; P:regulation of protein catabolic process; IPI:MGI.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; ISO:MGI.
DR Gene3D; 2.30.39.10; -; 2.
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; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor.
FT CHAIN 1..382
FT /note="Leukocyte elastase inhibitor B"
FT /id="PRO_0000289121"
FT REGION 352..382
FT /note="CARD-binding motif (CBM)"
FT /evidence="ECO:0000250|UniProtKB:P30740"
FT SITE 347..348
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
SQ SEQUENCE 382 AA; 42887 MW; 35CBB6ADF677C8DB CRC64;
MEQLSSANTL FTLELFHTLK ESSPTGNIFF SPFSISSSLA MVFLGAKGST AAQLSKTLHF
DSVEDIHSCF QSLTAEVSKL GASHTLKLAN RLYGEKTYNF LPEFLASTQK MYSADLAAVD
FQHASEDARK EINQWVKGQT EGKIPELLAK GVVDSMTKLV LVNAIYFKGI WEEQFMTRET
INAPFRLNKK DTKTVKMMYQ KKKFPFGYIS DLKCKVLEMP YQGGELSMVI LLPEDIEDES
TGLKKIEEQL TLGKLHEWTK HENLRNIDVH VKLPRFKMEE SYILNSNLCC LGVQDLFSSG
KADLSGMSGS RDLFVSKIVH KSFVDVNEQG TEAAAATGGI IQVLCEKMPT PQEVFTVDHP
FLFFIRHNPT ANMIFFGRVC SP
