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 21-SEP-2011, entry version 99. 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 MEDLINE=95332310; 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). 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. CC -!- SUBUNIT: Forms a complex with the monomeric form of beta-tryptase CC (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in the inner ear hair cells, CC keratinocytes of hair follicles and epidermis in abdominal skin. 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. CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily. 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 IPI; IPI00121471; -. DR PIR; A57488; A57488. DR RefSeq; NP_001157590.1; NM_001164118.1. DR RefSeq; NP_033280.1; NM_009254.3. DR UniGene; Mm.252210; -. DR PDB; 1M37; Model; -; A=1-378. DR PDBsum; 1M37; -. DR ProteinModelPortal; Q60854; -. DR SMR; Q60854; 1-378. DR IntAct; Q60854; 1. DR STRING; Q60854; -. DR MEROPS; I04.030; -. DR PhosphoSite; Q60854; -. DR PRIDE; Q60854; -. DR Ensembl; ENSMUST00000043552; ENSMUSP00000041016; ENSMUSG00000060147. DR Ensembl; ENSMUST00000167163; ENSMUSP00000131115; ENSMUSG00000060147. DR GeneID; 20719; -. DR KEGG; mmu:20719; -. DR CTD; 20719; -. DR MGI; MGI:103123; Serpinb6a. DR HOGENOM; HBG714743; -. DR HOVERGEN; HBG005957; -. DR InParanoid; Q60854; -. DR OMA; KMTYIGE; -. DR OrthoDB; EOG412M5X; -. DR PhylomeDB; Q60854; -. DR NextBio; 299313; -. DR ArrayExpress; Q60854; -. DR Bgee; Q60854; -. DR Genevestigator; Q60854; -. DR GermOnline; ENSMUSG00000060147; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:BHF-UCL. DR GO; GO:0008406; P:gonad development; NAS:BHF-UCL. DR InterPro; IPR000215; Protease_inhib_I4_serpin. DR InterPro; IPR023795; Protease_inhib_I4_serpin_CS. DR InterPro; IPR023796; Sepin_dom. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; Prot_inh_serpin; 1. DR PROSITE; PS00284; SERPIN; 1. PE 2: Evidence at transcript level; KW 3D-structure; Complete proteome; Cytoplasm; Protease inhibitor; KW Reference proteome; Serine protease inhibitor. FT CHAIN 1 378 Serpin B6. FT /FTId=PRO_0000094107. FT SITE 343 344 Reactive bond (By similarity). FT HELIX 2 21 FT HELIX 31 44 FT HELIX 47 57 FT HELIX 59 61 FT HELIX 65 77 FT STRAND 82 97 FT HELIX 101 111 FT STRAND 114 118 FT TURN 120 122 FT HELIX 124 139 FT STRAND 157 172 FT HELIX 176 178 FT STRAND 180 189 FT STRAND 191 208 FT TURN 209 212 FT STRAND 213 234 FT STRAND 236 238 FT HELIX 241 244 FT HELIX 247 254 FT HELIX 256 258 FT STRAND 260 269 FT STRAND 271 273 FT STRAND 276 278 FT HELIX 281 284 FT TURN 285 287 FT TURN 290 292 FT TURN 294 296 FT TURN 300 302 FT STRAND 312 320 FT STRAND 322 336 FT STRAND 350 354 FT TURN 355 358 FT STRAND 359 363 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 //