ID   SPB6_MOUSE              Reviewed;         378 AA.
AC   Q60854;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=Serpin B6;
DE   AltName: Full=Placental thrombin inhibitor;
DE   AltName: Full=Proteinase inhibitor 6;
DE            Short=PI-6;
GN   Name=Serpinb6; Synonyms=Serpinb6a, Spi3;
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=BALB/cJ;
RX   PubMed=7608171; DOI=10.1074/jbc.270.27.16089;
RA   Sun J., Rose J.B., Bird P.;
RT   "Gene structure, chromosomal localization, and expression of the murine
RT   homologue of human proteinase inhibitor 6 (PI-6) suggests divergence of PI-
RT   6 from the ovalbumin serpins.";
RL   J. Biol. Chem. 270:16089-16096(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
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   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17761692; DOI=10.1093/jb/mvm156;
RA   Scott F.L., Sun J., Whisstock J.C., Kato K., Bird P.I.;
RT   "SerpinB6 is an inhibitor of kallikrein-8 in keratinocytes.";
RL   J. Biochem. 142:435-442(2007).
RN   [4]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=20451170; DOI=10.1016/j.ajhg.2010.04.004;
RA   Sirmaci A., Erbek S., Price J., Huang M., Duman D., Cengiz F.B.,
RA   Bademci G., Tokgoz-Yilmaz S., Hismi B., Ozdag H., Ozturk B.,
RA   Kulaksizoglu S., Yildirim E., Kokotas H., Grigoriadou M., Petersen M.B.,
RA   Shahin H., Kanaan M., King M.C., Chen Z.Y., Blanton S.H., Liu X.Z.,
RA   Zuchner S., Akar N., Tekin M.;
RT   "A truncating mutation in SERPINB6 is associated with autosomal-recessive
RT   nonsyndromic sensorineural hearing loss.";
RL   Am. J. Hum. Genet. 86:797-804(2010).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play
CC       an important role in the inner ear in the protection against leakage of
CC       lysosomal content during stress. May be involved in the regulation of
CC       serine proteinases present in the brain or extravasated from the blood.
CC       {ECO:0000269|PubMed:17761692}.
CC   -!- SUBUNIT: Forms a complex with the monomeric form of beta-tryptase.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17761692,
CC       ECO:0000269|PubMed:20451170}.
CC   -!- TISSUE SPECIFICITY: Expressed in the inner ear hair cells,
CC       keratinocytes of hair follicles and epidermis in abdominal skin.
CC       {ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:20451170}.
CC   -!- DEVELOPMENTAL STAGE: At 13.5 dpc, weakly detected in utricle sensory
CC       epithelium but not in hair cells. At 16.5 dpc, more prominently
CC       detected in crista hair cells. Hair cell expression is sustained in
CC       postnatal mice. In cochlea, detected in cochlear hair cells in embryo
CC       and in hair cells and the greater epithelial ridge (GER) region in
CC       early postnatal age. {ECO:0000269|PubMed:20451170}.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U25844; AAA79684.1; -; mRNA.
DR   EMBL; BC006766; AAH06766.1; -; mRNA.
DR   EMBL; BC057950; AAH57950.1; -; mRNA.
DR   CCDS; CCDS26441.1; -.
DR   PIR; A57488; A57488.
DR   RefSeq; NP_001157590.1; NM_001164118.1.
DR   RefSeq; NP_001230121.1; NM_001243192.1.
DR   RefSeq; NP_033280.1; NM_009254.3.
DR   RefSeq; XP_006516686.1; XM_006516623.1.
DR   RefSeq; XP_011242601.1; XM_011244299.1.
DR   RefSeq; XP_011242602.1; XM_011244300.2.
DR   RefSeq; XP_011242603.1; XM_011244301.1.
DR   AlphaFoldDB; Q60854; -.
DR   SMR; Q60854; -.
DR   BioGRID; 203444; 6.
DR   IntAct; Q60854; 1.
DR   STRING; 10090.ENSMUSP00000017188; -.
DR   MEROPS; I04.030; -.
DR   GlyGen; Q60854; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q60854; -.
DR   MetOSite; Q60854; -.
DR   PhosphoSitePlus; Q60854; -.
DR   SwissPalm; Q60854; -.
DR   EPD; Q60854; -.
DR   jPOST; Q60854; -.
DR   MaxQB; Q60854; -.
DR   PaxDb; 10090-ENSMUSP00000017188; -.
DR   ProteomicsDB; 263312; -.
DR   Pumba; Q60854; -.
DR   DNASU; 20719; -.
DR   Ensembl; ENSMUST00000043552.17; ENSMUSP00000041016.11; ENSMUSG00000060147.16.
DR   Ensembl; ENSMUST00000076532.14; ENSMUSP00000075848.8; ENSMUSG00000060147.16.
DR   Ensembl; ENSMUST00000167163.8; ENSMUSP00000131115.2; ENSMUSG00000060147.16.
DR   GeneID; 20719; -.
DR   KEGG; mmu:20719; -.
DR   UCSC; uc007qap.2; mouse.
DR   AGR; MGI:103123; -.
DR   CTD; 20719; -.
DR   MGI; MGI:103123; Serpinb6a.
DR   VEuPathDB; HostDB:ENSMUSG00000060147; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000154519; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; Q60854; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; Q60854; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-75205; Dissolution of Fibrin Clot.
DR   BioGRID-ORCS; 20719; 0 hits in 75 CRISPR screens.
DR   ChiTaRS; Serpinb6a; mouse.
DR   PRO; PR:Q60854; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q60854; Protein.
DR   Bgee; ENSMUSG00000060147; Expressed in stroma of bone marrow and 268 other cell types or tissues.
DR   ExpressionAtlas; Q60854; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0097180; C:serine protease inhibitor complex; ISO:MGI.
DR   GO; GO:0002020; F:protease binding; ISO:MGI.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
DR   GO; GO:0071470; P:cellular response to osmotic stress; ISO:MGI.
DR   GO; GO:0008406; P:gonad development; NAS:BHF-UCL.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; NAS:BHF-UCL.
DR   GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR   CDD; cd19565; serpinB6_CAP; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
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; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   PANTHER; PTHR11461:SF204; SERPIN B6; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
DR   Genevisible; Q60854; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Phosphoprotein; Protease inhibitor;
KW   Reference proteome; Serine protease inhibitor.
FT   CHAIN           1..378
FT                   /note="Serpin B6"
FT                   /id="PRO_0000094107"
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:P35237"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35237"
FT   MOD_RES         197
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
SQ   SEQUENCE   378 AA;  42599 MW;  4B0F5E1A030BBDF6 CRC64;
     MDPLQEANGT FALNLLKILG EDSSKNVFLS PMSISSALAM VFMGAKGTTA SQMAQALALD
     KCSGNGGGDV HQGFQSLLTE VNKTGTQYLL RTANRLFGDK TCDLLASFKD SCLKFYEAEL
     EELDFQGATE ESRQHINTWV AKKTEDKIKE VLSPGTVNSD TSLVLVNAIY FKGNWEKQFN
     KEHTREMPFK VSKNEEKPVQ MMFKKSTFKM TYIGEIFTKI LLLPYVSSEL NMIIMLPDEH
     VELSTVEKEV TYEKFIEWTR LDKMDEEEVE VFLPKFKLEE NYNMNDALYK LGMTDAFGGR
     ADFSGMSSKQ GLFLSKVVHK AFVEVNEEGT EAAAATAGMM TVRCMRFTPR FCADHPFLFF
     IHHVKTNGIL FCGRFSSP
//