SPB6_MOUSE
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 03-AUG-2022, entry version 173.
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, Pancreas,
RC 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; 4.
DR IntAct; Q60854; 1.
DR STRING; 10090.ENSMUSP00000017188; -.
DR MEROPS; I04.030; -.
DR iPTMnet; Q60854; -.
DR PhosphoSitePlus; Q60854; -.
DR SwissPalm; Q60854; -.
DR EPD; Q60854; -.
DR jPOST; Q60854; -.
DR MaxQB; Q60854; -.
DR PaxDb; Q60854; -.
DR PRIDE; Q60854; -.
DR DNASU; 20719; -.
DR Ensembl; ENSMUST00000043552; ENSMUSP00000041016; ENSMUSG00000060147.
DR Ensembl; ENSMUST00000076532; ENSMUSP00000075848; ENSMUSG00000060147.
DR Ensembl; ENSMUST00000167163; ENSMUSP00000131115; ENSMUSG00000060147.
DR GeneID; 20719; -.
DR KEGG; mmu:20719; -.
DR UCSC; uc007qap.2; mouse.
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 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 70 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 264 other tissues.
DR ExpressionAtlas; Q60854; baseline and differential.
DR Genevisible; Q60854; MM.
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; ISO:MGI.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 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; 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 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
