SPB6_HUMAN
ID SPB6_HUMAN Reviewed; 376 AA.
AC P35237; B2RBA8; Q59F97; Q5TD06; Q7Z2Y7; Q96J44; Q9UDI7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Serpin B6;
DE AltName: Full=Cytoplasmic antiproteinase;
DE Short=CAP;
DE AltName: Full=Peptidase inhibitor 6;
DE Short=PI-6;
DE AltName: Full=Placental thrombin inhibitor;
GN Name=SERPINB6; Synonyms=PI6, PTI;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-90, AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=8415716; DOI=10.1073/pnas.90.20.9417;
RA Coughlin P., Sun J., Cerruti L., Salem H.H., Bird P.;
RT "Cloning and molecular characterization of a human intracellular serine
RT proteinase inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9417-9421(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 67-73 AND 144-149, VARIANT
RP VAL-90, AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=8136380; DOI=10.1021/bi00177a037;
RA Morgenstern K.A., Sprecher C.A., Holth L., Foster D., Grant F.J., Ching A.,
RA Kisiel W.;
RT "Complementary DNA cloning and kinetic characterization of a novel
RT intracellular serine proteinase inhibitor: mechanism of action with trypsin
RT and factor Xa as model proteinases.";
RL Biochemistry 33:3432-3441(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-90.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-90.
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Chondrosarcoma, and Colon;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-372.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 47-60; 63-81 AND 91-98, AND SUBCELLULAR LOCATION.
RC TISSUE=Leukemia;
RX PubMed=8486644; DOI=10.1016/s0021-9258(18)98385-7;
RA Coughlin P.B., Tetaz T., Salem H.H.;
RT "Identification and purification of a novel serine proteinase inhibitor.";
RL J. Biol. Chem. 268:9541-9547(1993).
RN [10]
RP FUNCTION.
RX PubMed=10068683;
RA Scott F.L., Hirst C.E., Sun J., Bird C.H., Bottomley S.P., Bird P.I.;
RT "The intracellular serpin proteinase inhibitor 6 is expressed in monocytes
RT and granulocytes and is a potent inhibitor of the azurophilic granule
RT protease, cathepsin G.";
RL Blood 93:2089-2097(1999).
RN [11]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND COMPLEX FORMATION WITH
RP BETA-TRYPTASE.
RX PubMed=14670919; DOI=10.1182/blood-2003-08-2981;
RA Strik M.C., Wolbink A., Wouters D., Bladergroen B.A., Verlaan A.R.,
RA van Houdt I.S., Hijlkema S., Hack C.E., Kummer J.A.;
RT "Intracellular serpin SERPINB6 (PI6) is abundantly expressed by human mast
RT cells and forms complexes with beta-tryptase monomers.";
RL Blood 103:2710-2717(2004).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP INVOLVEMENT IN DFNB91, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May be involved in the regulation of serine proteinases
CC present in the brain or extravasated from the blood (By similarity).
CC Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play an
CC important role in the inner ear in the protection against leakage of
CC lysosomal content during stress and loss of this protection results in
CC cell death and sensorineural hearing loss. {ECO:0000250,
CC ECO:0000269|PubMed:10068683, ECO:0000269|PubMed:17761692,
CC ECO:0000269|PubMed:20451170, ECO:0000269|PubMed:8136380,
CC ECO:0000269|PubMed:8415716}.
CC -!- SUBUNIT: Forms a complex with the monomeric form of beta-tryptase.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14670919,
CC ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:20451170,
CC ECO:0000269|PubMed:8486644}.
CC -!- TISSUE SPECIFICITY: Expressed in keratinocytes (at protein level).
CC Highest levels in skeletal muscle. Also found in placenta, cardiac
CC muscle, lung, liver, kidney and pancreas. Expressed in the inner ear
CC hair cells. Expressed abundantly by normal mast cells in different
CC tissues and by mast cells in mastocytoma lesions.
CC {ECO:0000269|PubMed:14670919, ECO:0000269|PubMed:17761692,
CC ECO:0000269|PubMed:20451170}.
CC -!- DISEASE: Deafness, autosomal recessive, 91 (DFNB91) [MIM:613453]: A
CC form of non-syndromic deafness characterized by progressive and age-
CC dependent sensorineural hearing loss. Vestibular function is normal.
CC {ECO:0000269|PubMed:20451170}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92800.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD98106.1; Type=Erroneous initiation; Evidence={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; Z22658; CAA80373.1; -; mRNA.
DR EMBL; S69272; AAB30320.1; -; mRNA.
DR EMBL; AK314578; BAG37155.1; -; mRNA.
DR EMBL; BX538343; CAD98106.1; ALT_INIT; mRNA.
DR EMBL; AL133351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55097.1; -; Genomic_DNA.
DR EMBL; BC001394; AAH01394.1; -; mRNA.
DR EMBL; BC098564; AAH98564.1; -; mRNA.
DR EMBL; AB209563; BAD92800.1; ALT_INIT; mRNA.
DR CCDS; CCDS4479.1; -.
DR PIR; A48681; A48681.
DR RefSeq; NP_001182220.2; NM_001195291.2.
DR RefSeq; NP_001258751.1; NM_001271822.1.
DR RefSeq; NP_001258752.1; NM_001271823.1.
DR RefSeq; NP_001258753.1; NM_001271824.1.
DR RefSeq; NP_001258754.1; NM_001271825.1.
DR RefSeq; NP_001284628.1; NM_001297699.1.
DR RefSeq; NP_001284629.1; NM_001297700.1.
DR RefSeq; NP_004559.4; NM_004568.5.
DR RefSeq; XP_011512975.1; XM_011514673.1.
DR RefSeq; XP_011512976.1; XM_011514674.2.
DR AlphaFoldDB; P35237; -.
DR SMR; P35237; -.
DR BioGRID; 111287; 33.
DR IntAct; P35237; 7.
DR MINT; P35237; -.
DR STRING; 9606.ENSP00000484343; -.
DR DrugBank; DB00055; Drotrecogin alfa.
DR MEROPS; I04.011; -.
DR iPTMnet; P35237; -.
DR MetOSite; P35237; -.
DR PhosphoSitePlus; P35237; -.
DR SwissPalm; P35237; -.
DR BioMuta; SERPINB6; -.
DR DMDM; 161784343; -.
DR OGP; P35237; -.
DR EPD; P35237; -.
DR jPOST; P35237; -.
DR MassIVE; P35237; -.
DR MaxQB; P35237; -.
DR PaxDb; P35237; -.
DR PeptideAtlas; P35237; -.
DR PRIDE; P35237; -.
DR ProteomicsDB; 54998; -.
DR Antibodypedia; 1702; 313 antibodies from 39 providers.
DR DNASU; 5269; -.
DR Ensembl; ENST00000380520.6; ENSP00000369891.1; ENSG00000124570.21.
DR Ensembl; ENST00000380524.5; ENSP00000369896.1; ENSG00000124570.21.
DR Ensembl; ENST00000380529.5; ENSP00000369901.1; ENSG00000124570.21.
DR Ensembl; ENST00000380539.7; ENSP00000369912.2; ENSG00000124570.21.
DR Ensembl; ENST00000380546.7; ENSP00000369919.3; ENSG00000124570.21.
DR Ensembl; ENST00000643098.1; ENSP00000493936.1; ENSG00000124570.21.
DR Ensembl; ENST00000644178.1; ENSP00000496073.1; ENSG00000124570.21.
DR Ensembl; ENST00000644388.1; ENSP00000494650.1; ENSG00000124570.21.
DR GeneID; 5269; -.
DR KEGG; hsa:5269; -.
DR MANE-Select; ENST00000380539.7; ENSP00000369912.2; NM_004568.6; NP_004559.4.
DR UCSC; uc003muk.3; human.
DR CTD; 5269; -.
DR DisGeNET; 5269; -.
DR GeneCards; SERPINB6; -.
DR HGNC; HGNC:8950; SERPINB6.
DR HPA; ENSG00000124570; Low tissue specificity.
DR MalaCards; SERPINB6; -.
DR MIM; 173321; gene.
DR MIM; 613453; phenotype.
DR neXtProt; NX_P35237; -.
DR OpenTargets; ENSG00000124570; -.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR PharmGKB; PA35516; -.
DR VEuPathDB; HostDB:ENSG00000124570; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154519; -.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; P35237; -.
DR OMA; MRCARIT; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P35237; -.
DR TreeFam; TF352619; -.
DR PathwayCommons; P35237; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
DR SignaLink; P35237; -.
DR BioGRID-ORCS; 5269; 24 hits in 1079 CRISPR screens.
DR ChiTaRS; SERPINB6; human.
DR GeneWiki; SERPINB6; -.
DR GenomeRNAi; 5269; -.
DR Pharos; P35237; Tbio.
DR PRO; PR:P35237; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P35237; protein.
DR Bgee; ENSG00000124570; Expressed in right testis and 204 other tissues.
DR ExpressionAtlas; P35237; baseline and differential.
DR Genevisible; P35237; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0097180; C:serine protease inhibitor complex; IDA:BHF-UCL.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
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; Deafness; Direct protein sequencing;
KW Non-syndromic deafness; Phosphoprotein; Protease inhibitor;
KW Reference proteome; Serine protease inhibitor.
FT CHAIN 1..376
FT /note="Serpin B6"
FT /id="PRO_0000094106"
FT SITE 341..342
FT /note="Reactive bond"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 195
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60854"
FT VARIANT 90
FT /note="M -> V (in dbSNP:rs2295769)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:8136380,
FT ECO:0000269|PubMed:8415716"
FT /id="VAR_037295"
FT VARIANT 153
FT /note="G -> S (in dbSNP:rs2295766)"
FT /id="VAR_037296"
FT CONFLICT 175
FT /note="E -> G (in Ref. 1; CAA80373)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="M -> V (in Ref. 3; BAG37155)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="S -> R (in Ref. 1; CAA80373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 42622 MW; 3A06BC26A7510E1A CRC64;
MDVLAEANGT FALNLLKTLG KDNSKNVFFS PMSMSCALAM VYMGAKGNTA AQMAQILSFN
KSGGGGDIHQ GFQSLLTEVN KTGTQYLLRM ANRLFGEKSC DFLSSFRDSC QKFYQAEMEE
LDFISAVEKS RKHINTWVAE KTEGKIAELL SPGSVDPLTR LVLVNAVYFR GNWDEQFDKE
NTEERLFKVS KNEEKPVQMM FKQSTFKKTY IGEIFTQILV LPYVGKELNM IIMLPDETTD
LRTVEKELTY EKFVEWTRLD MMDEEEVEVS LPRFKLEESY DMESVLRNLG MTDAFELGKA
DFSGMSQTDL SLSKVVHKSF VEVNEEGTEA AAATAAIMMM RCARFVPRFC ADHPFLFFIQ
HSKTNGILFC GRFSSP
