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 14-OCT-2015, entry version 137. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; 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 RT murine homologue of human proteinase inhibitor 6 (PI-6) suggests RT divergence of PI-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 RT project: 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., RA Petersen M.B., Shahin H., Kanaan M., King M.C., Chen Z.Y., RA Blanton S.H., Liu X.Z., Zuchner S., Akar N., Tekin M.; RT "A truncating mutation in SERPINB6 is associated with autosomal- RT recessive 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 RT expression."; RL Cell 143:1174-1189(2010). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197, AND IDENTIFICATION BY RP MASS 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., RA Zhang Y., 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 CC play an important role in the inner ear in the protection against CC leakage of lysosomal content during stress. May be involved in the CC regulation of serine proteinases present in the brain or CC extravasated from the blood. {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 E13.5, weakly detected in utricle sensory CC epithelium but not in hair cells. At E16.5, more prominently CC detected in crista hair cells. Hair cell expression is sustained CC in postnatal mice. In cochlea, detected in cochlear hair cells in CC embryo and in hair cells and the greater epithelial ridge (GER) CC region in early postnatal age. {ECO:0000269|PubMed:20451170}. 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; 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_011244300.1. DR RefSeq; XP_011242603.1; XM_011244301.1. DR UniGene; Mm.252210; -. DR UniGene; Mm.374799; -. DR UniGene; Mm.486427; -. DR PDB; 1M37; Model; -; A=1-378. DR PDBsum; 1M37; -. DR ProteinModelPortal; Q60854; -. DR SMR; Q60854; 1-378. DR BioGrid; 203444; 1. DR IntAct; Q60854; 2. DR MINT; MINT-1855884; -. DR STRING; 10090.ENSMUSP00000017188; -. DR MEROPS; I04.030; -. DR PhosphoSite; Q60854; -. DR MaxQB; Q60854; -. DR PaxDb; Q60854; -. DR PRIDE; Q60854; -. DR GeneID; 20719; -. DR UCSC; uc007qap.2; mouse. DR CTD; 20719; -. DR MGI; MGI:103123; Serpinb6a. DR eggNOG; COG4826; -. DR HOGENOM; HOG000238519; -. DR HOVERGEN; HBG005957; -. DR InParanoid; Q60854; -. DR OrthoDB; EOG7327PB; -. DR PhylomeDB; Q60854; -. DR NextBio; 299313; -. DR PRO; PR:Q60854; -. DR Proteomes; UP000000589; Unplaced. DR Bgee; Q60854; -. DR ExpressionAtlas; Q60854; baseline and differential. DR Genevisible; Q60854; MM. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005622; C:intracellular; IDA:BHF-UCL. DR GO; GO:0043234; C:protein complex; ISO:MGI. DR GO; GO:0002020; F:protease binding; ISO:MGI. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:BHF-UCL. 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 InterPro; IPR023795; Serpin_CS. DR InterPro; IPR023796; Serpin_dom. DR InterPro; IPR000215; Serpin_fam. DR PANTHER; PTHR11461; PTHR11461; 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 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Protease inhibitor; Reference proteome; Serine protease inhibitor. FT CHAIN 1 378 Serpin B6. FT /FTId=PRO_0000094107. FT SITE 343 344 Reactive bond. {ECO:0000250}. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000250|UniProtKB:P35237}. FT MOD_RES 197 197 N6-acetyllysine. FT {ECO:0000244|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 //