SPB10_HUMAN
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 03-AUG-2022, entry version 172.
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; 4.
DR IntAct; P48595; 1.
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; P48595; -.
DR PeptideAtlas; P48595; -.
DR PRIDE; P48595; -.
DR ProteomicsDB; 55912; -.
DR Antibodypedia; 34913; 132 antibodies from 25 providers.
DR DNASU; 5273; -.
DR Ensembl; ENST00000238508.8; ENSP00000238508.3; ENSG00000242550.6.
DR Ensembl; ENST00000619595.1; ENSP00000479385.1; ENSG00000242550.6.
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 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; QFNRDQD; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P48595; -.
DR TreeFam; TF352619; -.
DR PathwayCommons; P48595; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P48595; -.
DR BioGRID-ORCS; 5273; 10 hits in 1072 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 62 other tissues.
DR ExpressionAtlas; P48595; baseline and differential.
DR Genevisible; P48595; HS.
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 GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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 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
