ID   SPB10_HUMAN             Reviewed;         397 AA.
AC   P48595; Q4VAX4; Q4VAX7;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Serpin B10;
DE   AltName: Full=Bomapin;
DE   AltName: Full=Peptidase inhibitor 10;
DE            Short=PI-10;
GN   Name=SERPINB10; Synonyms=PI10;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Bone marrow;
RX   PubMed=7592909; DOI=10.1074/jbc.270.45.26754;
RA   Riewald M., Schleef R.R.;
RT   "Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin
RT   that is expressed specifically in the bone marrow.";
RL   J. Biol. Chem. 270:26754-26757(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-360.
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   SUBCELLULAR LOCATION, AND MUTAGENESIS OF 74-LYS--LYS-78.
RX   PubMed=10196205; DOI=10.1074/jbc.274.16.11194;
RA   Chuang T.L., Schleef R.R.;
RT   "Identification of a nuclear targeting domain in the insertion between
RT   helices C and D in protease inhibitor-10.";
RL   J. Biol. Chem. 274:11194-11198(1999).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10871600; DOI=10.1074/jbc.c000389200;
RA   Schleef R.R., Chuang T.L.;
RT   "Protease inhibitor 10 inhibits tumor necrosis factor alpha -induced cell
RT   death. Evidence for the formation of intracellular high M(r) protease
RT   inhibitor 10-containing complexes.";
RL   J. Biol. Chem. 275:26385-26389(2000).
RN   [5]
RP   DISULFIDE BOND, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-395, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=20433722; DOI=10.1186/1471-2121-11-30;
RA   Przygodzka P., Ramstedt B., Tengel T., Larsson G., Wilczynska M.;
RT   "Bomapin is a redox-sensitive nuclear serpin that affects responsiveness of
RT   myeloid progenitor cells to growth environment.";
RL   BMC Cell Biol. 11:30-30(2010).
CC   -!- FUNCTION: Protease inhibitor that may play a role in the regulation of
CC       protease activities during hematopoiesis and apoptosis induced by TNF.
CC       May regulate protease activities in the cytoplasm and in the nucleus.
CC       {ECO:0000269|PubMed:10871600, ECO:0000269|PubMed:7592909}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mostly found in the
CC       nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in myeloid cells and the
CC       bone marrow. {ECO:0000269|PubMed:20433722, ECO:0000269|PubMed:7592909}.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U35459; AAC50282.1; -; mRNA.
DR   EMBL; BC096217; AAH96217.1; -; mRNA.
DR   EMBL; BC096219; AAH96219.1; -; mRNA.
DR   EMBL; BC096220; AAH96220.1; -; mRNA.
DR   CCDS; CCDS11990.1; -.
DR   PIR; I39184; I39184.
DR   RefSeq; NP_005015.1; NM_005024.2.
DR   RefSeq; XP_011524329.1; XM_011526027.1.
DR   AlphaFoldDB; P48595; -.
DR   SMR; P48595; -.
DR   BioGRID; 111291; 5.
DR   IntAct; P48595; 2.
DR   MINT; P48595; -.
DR   STRING; 9606.ENSP00000238508; -.
DR   MEROPS; I04.015; -.
DR   iPTMnet; P48595; -.
DR   PhosphoSitePlus; P48595; -.
DR   SwissPalm; P48595; -.
DR   BioMuta; SERPINB10; -.
DR   DMDM; 1345616; -.
DR   EPD; P48595; -.
DR   jPOST; P48595; -.
DR   MassIVE; P48595; -.
DR   PaxDb; 9606-ENSP00000238508; -.
DR   PeptideAtlas; P48595; -.
DR   ProteomicsDB; 55912; -.
DR   Antibodypedia; 34913; 140 antibodies from 25 providers.
DR   DNASU; 5273; -.
DR   Ensembl; ENST00000238508.8; ENSP00000238508.3; ENSG00000242550.7.
DR   GeneID; 5273; -.
DR   KEGG; hsa:5273; -.
DR   MANE-Select; ENST00000238508.8; ENSP00000238508.3; NM_005024.3; NP_005015.1.
DR   UCSC; uc010xev.3; human.
DR   AGR; HGNC:8942; -.
DR   CTD; 5273; -.
DR   DisGeNET; 5273; -.
DR   GeneCards; SERPINB10; -.
DR   HGNC; HGNC:8942; SERPINB10.
DR   HPA; ENSG00000242550; Tissue enriched (bone).
DR   MIM; 602058; gene.
DR   neXtProt; NX_P48595; -.
DR   OpenTargets; ENSG00000242550; -.
DR   PharmGKB; PA35510; -.
DR   VEuPathDB; HostDB:ENSG00000242550; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000161205; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; P48595; -.
DR   OMA; QYVRAYD; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; P48595; -.
DR   TreeFam; TF352619; -.
DR   PathwayCommons; P48595; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; P48595; -.
DR   BioGRID-ORCS; 5273; 11 hits in 1150 CRISPR screens.
DR   GenomeRNAi; 5273; -.
DR   Pharos; P48595; Tbio.
DR   PRO; PR:P48595; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; P48595; Protein.
DR   Bgee; ENSG00000242550; Expressed in bone marrow and 63 other cell types or tissues.
DR   ExpressionAtlas; P48595; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
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:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   CDD; cd19569; serpinB10_bomapin; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   PANTHER; PTHR11461:SF175; SERPIN B10; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
DR   Genevisible; P48595; HS.
PE   1: Evidence at protein level;
KW   Cytoplasm; Disulfide bond; Nucleus; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor.
FT   CHAIN           1..397
FT                   /note="Serpin B10"
FT                   /id="PRO_0000094114"
FT   MOTIF           74..77
FT                   /note="Nuclear localization signal"
FT   SITE            362..363
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..395
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000269|PubMed:20433722"
FT   VARIANT         3
FT                   /note="S -> A (in dbSNP:rs17072097)"
FT                   /id="VAR_051949"
FT   VARIANT         41
FT                   /note="I -> M (in dbSNP:rs8097425)"
FT                   /id="VAR_024353"
FT   VARIANT         99
FT                   /note="I -> T (in dbSNP:rs724558)"
FT                   /id="VAR_024354"
FT   VARIANT         135
FT                   /note="G -> D (in dbSNP:rs17072146)"
FT                   /id="VAR_051950"
FT   VARIANT         140
FT                   /note="P -> S (in dbSNP:rs9967382)"
FT                   /id="VAR_024355"
FT   VARIANT         246
FT                   /note="R -> C (in dbSNP:rs963075)"
FT                   /id="VAR_022116"
FT   VARIANT         360
FT                   /note="D -> N (in dbSNP:rs35453062)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_051951"
FT   MUTAGEN         74..77
FT                   /note="KKRK->AAAA: Abolishes nuclear localization."
FT   MUTAGEN         395
FT                   /note="C->S: No effect on cell proliferation."
FT                   /evidence="ECO:0000269|PubMed:20433722"
SQ   SEQUENCE   397 AA;  45403 MW;  8CE01246867154DF CRC64;
     MDSLATSINQ FALELSKKLA ESAQGKNIFF SSWSISTSLT IVYLGAKGTT AAQMAQVLQF
     NRDQGVKCDP ESEKKRKMEF NLSNSEEIHS DFQTLISEIL KPNDDYLLKT ANAIYGEKTY
     AFHNKYLEDM KTYFGAEPQP VNFVEASDQI RKDINSWVER QTEGKIQNLL PDDSVDSTTR
     MILVNALYFK GIWEHQFLVQ NTTEKPFRIN ETTSKPVQMM FMKKKLHIFH IEKPKAVGLQ
     LYYKSRDLSL LILLPEDING LEQLEKAITY EKLNEWTSAD MMELYEVQLH LPKFKLEDSY
     DLKSTLSSMG MSDAFSQSKA DFSGMSSARN LFLSNVFHKA FVEINEQGTE AAAGSGSEID
     IRIRVPSIEF NANHPFLFFI RHNKTNTILF YGRLCSP
//