SPB3_HUMAN
ID SPB3_HUMAN Reviewed; 390 AA.
AC P29508; A6NDM2; B2RBT5; B3W5Y6; Q53H28; Q53YB5; Q86VF3; Q86W04; Q8IWL4;
AC Q8IXI3; Q96J21; Q9BYF8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Serpin B3;
DE AltName: Full=Protein T4-A;
DE AltName: Full=Squamous cell carcinoma antigen 1;
DE Short=SCCA-1;
GN Name=SERPINB3; Synonyms=SCCA, SCCA1;
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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP VARIANT ALA-357.
RX PubMed=1958219; DOI=10.1016/s0006-291x(05)81380-4;
RA Suminami Y., Kishi F., Sekiguchi K., Kato H.;
RT "Squamous cell carcinoma antigen is a new member of the serine protease
RT inhibitors.";
RL Biochem. Biophys. Res. Commun. 181:51-58(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=7724531; DOI=10.1073/pnas.92.8.3147;
RA Schneider S.S., Schick C., Fish K.E., Miller E., Pena J.C., Treter S.D.,
RA Hui S.M., Silverman G.A.;
RT "A serine proteinase inhibitor locus at 18q21.3 contains a tandem
RT duplication of the human squamous cell carcinoma antigen gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3147-3151(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ALA-357.
RA Suminami Y., Kishi F., Murakami A., Sakaguchi Y., Kato H.;
RT "Novel forms of SCC antigen transcripts produced by alternative splicing.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-351, AND MUTAGENESIS OF
RP ALA-341; PHE-352 AND 354-SER-SER-355.
RC TISSUE=Hepatoma;
RX PubMed=12975381; DOI=10.1074/jbc.m302842200;
RA Moore P.L., Ong S., Harrison T.J.;
RT "Squamous cell carcinoma antigen 1-mediated binding of hepatitis B virus to
RT hepatocytes does not involve the hepatic serpin clearance system.";
RL J. Biol. Chem. 278:46709-46717(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Hepatoma;
RA Tong C., Chenyu X., Jun Z., Ningshao X.;
RT "SCCA1 mRNA sequence from human hepatocellular carcinoma cell line HepG2,
RT complete cds.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-351.
RC TISSUE=Liver;
RA Turato C., Biasiolo A., Quarta S., Beneduce L., Zuin J., Fassina G.,
RA Gatta A., Pontisso P.;
RT "Characterization of the new isoform of squamous cell carcinoma antigen-1
RT (SCCA-PD) detected in hepatocellular carcinoma.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-357.
RC TISSUE=Dermoid cancer;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [11]
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 [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [13]
RP PROTEIN SEQUENCE OF 1-21; 88-94; 112-125; 147-160; 215-260; 266-300;
RP 322-331 AND 378-386, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Bensaad K., Vousden K.H.;
RL Submitted (FEB-2008) to UniProtKB.
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-390 (ISOFORM 1), VARIANT ALA-351,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver cancer;
RX PubMed=14970861; DOI=10.1038/sj.bjc.6601543;
RA Pontisso P., Calabrese F., Benvegnu L., Lise M., Belluco C.,
RA Ruvoletto M.G., De Falco S., Marino M., Valente M., Nitti D., Gatta A.,
RA Fassina G.;
RT "Overexpression of squamous cell carcinoma antigen variants in
RT hepatocellular carcinoma.";
RL Br. J. Cancer 90:833-837(2004).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=10956412;
RX DOI=10.1002/1097-0215(20000720)89:4<368::aid-ijc9>3.0.co;2-6;
RA Uemura Y., Pak S.C., Luke C., Cataltepe S., Tsu C., Schick C., Kamachi Y.,
RA Pomeroy S.L., Perlmutter D.H., Silverman G.A.;
RT "Circulating serpin tumor markers SCCA1 and SCCA2 are not actively secreted
RT but reside in the cytosol of squamous carcinoma cells.";
RL Int. J. Cancer 89:368-377(2000).
RN [16]
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 [17]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-390, FUNCTION, INDUCTION,
RP MUTAGENESIS OF PHE-352, AND INTERACTION WITH MAPK8.
RX PubMed=19166818; DOI=10.1016/j.bbrc.2009.01.057;
RA Zheng B., Matoba Y., Kumagai T., Katagiri C., Hibino T., Sugiyama M.;
RT "Crystal structure of SCCA1 and insight about the interaction with JNK1.";
RL Biochem. Biophys. Res. Commun. 380:143-147(2009).
RN [18]
RP VARIANT ALA-351.
RX PubMed=21383048; DOI=10.1258/ebm.2011.010229;
RA Turato C., Biasiolo A., Pengo P., Frecer V., Quarta S., Fasolato S.,
RA Ruvoletto M., Beneduce L., Zuin J., Fassina G., Gatta A., Pontisso P.;
RT "Increased antiprotease activity of the SERPINB3 polymorphic variant SCCA-
RT PD.";
RL Exp. Biol. Med. 236:281-290(2011).
CC -!- FUNCTION: May act as a papain-like cysteine protease inhibitor to
CC modulate the host immune response against tumor cells. Also functions
CC as an inhibitor of UV-induced apoptosis via suppression of the activity
CC of c-Jun NH(2)-terminal kinase (JNK1). {ECO:0000269|PubMed:19166818}.
CC -!- SUBUNIT: Interacts with MAPK8/JNK1. {ECO:0000269|PubMed:19166818}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10956412,
CC ECO:0000269|PubMed:14970861}. Note=Seems to also be secreted in plasma
CC by cancerous cells but at a low level.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P29508-1; Sequence=Displayed;
CC Name=2; Synonyms=SCCA1b;
CC IsoId=P29508-2; Sequence=VSP_032657;
CC -!- TISSUE SPECIFICITY: Squamous cells. Expressed in some hepatocellular
CC carcinoma (at protein level). {ECO:0000269|PubMed:14970861}.
CC -!- DEVELOPMENTAL STAGE: Its expression is closely related to cellular
CC differentiation in both normal and malignant squamous cells.
CC -!- INDUCTION: Strongly up-regulated in the upper epidermis of sun-exposed
CC skin. {ECO:0000269|PubMed:19166818}.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO11731.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S66896; AAB20405.1; -; mRNA.
DR EMBL; U19556; AAA97552.1; -; mRNA.
DR EMBL; U19568; AAA86317.1; -; Genomic_DNA.
DR EMBL; U19559; AAA86317.1; JOINED; Genomic_DNA.
DR EMBL; U19560; AAA86317.1; JOINED; Genomic_DNA.
DR EMBL; U19562; AAA86317.1; JOINED; Genomic_DNA.
DR EMBL; U19565; AAA86317.1; JOINED; Genomic_DNA.
DR EMBL; U19567; AAA86317.1; JOINED; Genomic_DNA.
DR EMBL; U19562; AAA86316.1; -; Genomic_DNA.
DR EMBL; U19559; AAA86316.1; JOINED; Genomic_DNA.
DR EMBL; U19560; AAA86316.1; JOINED; Genomic_DNA.
DR EMBL; AB046399; BAB40772.1; -; mRNA.
DR EMBL; AJ515706; CAD56658.1; -; mRNA.
DR EMBL; AY245778; AAO92269.1; -; mRNA.
DR EMBL; AY245781; AAO92272.1; -; mRNA.
DR EMBL; EU852041; ACF21012.1; -; mRNA.
DR EMBL; BT006748; AAP35394.1; -; mRNA.
DR EMBL; AK222746; BAD96466.1; -; mRNA.
DR EMBL; AK222753; BAD96473.1; -; mRNA.
DR EMBL; AK314805; BAG37332.1; -; mRNA.
DR EMBL; AC069356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471096; EAW63156.1; -; Genomic_DNA.
DR EMBL; CH471096; EAW63157.1; -; Genomic_DNA.
DR EMBL; BC005224; AAH05224.1; -; mRNA.
DR EMBL; AY190327; AAO11731.1; ALT_INIT; mRNA.
DR CCDS; CCDS11987.1; -. [P29508-1]
DR PIR; I38201; I38201.
DR RefSeq; NP_008850.1; NM_006919.2. [P29508-1]
DR PDB; 2ZV6; X-ray; 2.70 A; A/B/C=2-390.
DR PDB; 4ZK0; X-ray; 2.15 A; A=1-390.
DR PDB; 4ZK3; X-ray; 2.00 A; A=1-390.
DR PDBsum; 2ZV6; -.
DR PDBsum; 4ZK0; -.
DR PDBsum; 4ZK3; -.
DR AlphaFoldDB; P29508; -.
DR SMR; P29508; -.
DR BioGRID; 112223; 229.
DR IntAct; P29508; 52.
DR MINT; P29508; -.
DR STRING; 9606.ENSP00000283752; -.
DR DrugBank; DB03929; D-Serine.
DR DrugBank; DB04522; Dexfosfoserine.
DR MEROPS; I04.008; -.
DR GlyGen; P29508; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P29508; -.
DR PhosphoSitePlus; P29508; -.
DR BioMuta; SERPINB3; -.
DR DMDM; 20141712; -.
DR SWISS-2DPAGE; P29508; -.
DR UCD-2DPAGE; P29508; -.
DR EPD; P29508; -.
DR jPOST; P29508; -.
DR MassIVE; P29508; -.
DR MaxQB; P29508; -.
DR PaxDb; P29508; -.
DR PeptideAtlas; P29508; -.
DR PRIDE; P29508; -.
DR ProteomicsDB; 54582; -. [P29508-1]
DR ProteomicsDB; 54583; -. [P29508-2]
DR TopDownProteomics; P29508-1; -. [P29508-1]
DR TopDownProteomics; P29508-2; -. [P29508-2]
DR Antibodypedia; 4364; 720 antibodies from 38 providers.
DR CPTC; P29508; 3 antibodies.
DR DNASU; 6317; -.
DR Ensembl; ENST00000283752.10; ENSP00000283752.5; ENSG00000057149.16. [P29508-1]
DR Ensembl; ENST00000332821.8; ENSP00000329498.8; ENSG00000057149.16. [P29508-2]
DR GeneID; 6317; -.
DR KEGG; hsa:6317; -.
DR MANE-Select; ENST00000283752.10; ENSP00000283752.5; NM_006919.3; NP_008850.1.
DR UCSC; uc002lji.3; human. [P29508-1]
DR CTD; 6317; -.
DR DisGeNET; 6317; -.
DR GeneCards; SERPINB3; -.
DR HGNC; HGNC:10569; SERPINB3.
DR HPA; ENSG00000057149; Tissue enhanced (esophagus, vagina).
DR MIM; 600517; gene.
DR neXtProt; NX_P29508; -.
DR OpenTargets; ENSG00000057149; -.
DR PharmGKB; PA35538; -.
DR VEuPathDB; HostDB:ENSG00000057149; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000154520; -.
DR HOGENOM; CLU_023330_0_2_1; -.
DR InParanoid; P29508; -.
DR OMA; ATHDFTT; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P29508; -.
DR TreeFam; TF352619; -.
DR PathwayCommons; P29508; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P29508; -.
DR BioGRID-ORCS; 6317; 14 hits in 1046 CRISPR screens.
DR ChiTaRS; SERPINB3; human.
DR EvolutionaryTrace; P29508; -.
DR GeneWiki; SERPINB3; -.
DR GenomeRNAi; 6317; -.
DR Pharos; P29508; Tbio.
DR PRO; PR:P29508; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P29508; protein.
DR Bgee; ENSG00000057149; Expressed in olfactory segment of nasal mucosa and 116 other tissues.
DR Genevisible; P29508; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IMP:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0001618; F:virus receptor activity; IDA:UniProtKB.
DR GO; GO:0035425; P:autocrine signaling; IMP:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IMP:UniProtKB.
DR GO; GO:0010466; P:negative regulation of peptidase activity; IDA:UniProtKB.
DR GO; GO:0045861; P:negative regulation of proteolysis; IDA:UniProtKB.
DR GO; GO:0038001; P:paracrine signaling; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010950; P:positive regulation of endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; 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 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor.
FT CHAIN 1..390
FT /note="Serpin B3"
FT /id="PRO_0000094103"
FT SITE 354..355
FT /note="Reactive bond"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.13"
FT VAR_SEQ 205..256
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_032657"
FT VARIANT 351
FT /note="G -> A (increased antiprotease activity and
FT increased MAPK8 inhibition activity; dbSNP:rs3180227)"
FT /evidence="ECO:0000269|PubMed:12975381,
FT ECO:0000269|PubMed:14970861, ECO:0000269|PubMed:21383048,
FT ECO:0000269|Ref.6"
FT /id="VAR_024351"
FT VARIANT 357
FT /note="T -> A (in dbSNP:rs1065205)"
FT /evidence="ECO:0000269|PubMed:1958219, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.9"
FT /id="VAR_024352"
FT MUTAGEN 341
FT /note="A->R: Loss of inhibitory activity."
FT /evidence="ECO:0000269|PubMed:12975381"
FT MUTAGEN 352
FT /note="F->A: Loss of inhibitory activity."
FT /evidence="ECO:0000269|PubMed:12975381,
FT ECO:0000269|PubMed:19166818"
FT MUTAGEN 352
FT /note="F->G: Loss of inhibitory activity to papain but does
FT not decrease the suppression activity to MAPK8."
FT /evidence="ECO:0000269|PubMed:12975381,
FT ECO:0000269|PubMed:19166818"
FT MUTAGEN 354..355
FT /note="SS->PP: Loss of inhibitory activity."
FT /evidence="ECO:0000269|PubMed:12975381"
FT CONFLICT 16
FT /note="F -> S (in Ref. 4; CAD56658)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="D -> N (in Ref. 4; CAD56658)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="N -> T (in Ref. 4; CAD56658)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="Q -> R (in Ref. 5; AAO92272)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="P -> S (in Ref. 5; AAO92272)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="T -> A (in Ref. 5; AAO92269)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="V -> E (in Ref. 5; AAO92272)"
FT /evidence="ECO:0000305"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 97..110
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:4ZK3"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:4ZK3"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:4ZK3"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2ZV6"
FT STRAND 174..188
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 206..224
FT /evidence="ECO:0007829|PDB:4ZK3"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 239..250
FT /evidence="ECO:0007829|PDB:4ZK3"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4ZK3"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 324..336
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 338..352
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:4ZK3"
FT TURN 376..379
FT /evidence="ECO:0007829|PDB:4ZK3"
FT STRAND 380..387
FT /evidence="ECO:0007829|PDB:4ZK3"
SQ SEQUENCE 390 AA; 44565 MW; E5F27F986C752CFA CRC64;
MNSLSEANTK FMFDLFQQFR KSKENNIFYS PISITSALGM VLLGAKDNTA QQIKKVLHFD
QVTENTTGKA ATYHVDRSGN VHHQFQKLLT EFNKSTDAYE LKIANKLFGE KTYLFLQEYL
DAIKKFYQTS VESVDFANAP EESRKKINSW VESQTNEKIK NLIPEGNIGS NTTLVLVNAI
YFKGQWEKKF NKEDTKEEKF WPNKNTYKSI QMMRQYTSFH FASLEDVQAK VLEIPYKGKD
LSMIVLLPNE IDGLQKLEEK LTAEKLMEWT SLQNMRETRV DLHLPRFKVE ESYDLKDTLR
TMGMVDIFNG DADLSGMTGS RGLVLSGVLH KAFVEVTEEG AEAAAATAVV GFGSSPTSTN
EEFHCNHPFL FFIRQNKTNS ILFYGRFSSP
