ID   SPB10_MOUSE             Reviewed;         397 AA.
AC   Q8K1K6;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Serpin B10;
GN   Name=Serpinb10;
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 [LARGE SCALE MRNA].
RC   STRAIN=Czech II; 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).
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       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC029736; AAH29736.1; -; mRNA.
DR   EMBL; BC069938; AAH69938.1; -; mRNA.
DR   AlphaFoldDB; Q8K1K6; -.
DR   SMR; Q8K1K6; -.
DR   STRING; 10090.ENSMUSP00000138771; -.
DR   MEROPS; I04.015; -.
DR   PhosphoSitePlus; Q8K1K6; -.
DR   PRIDE; Q8K1K6; -.
DR   ProteomicsDB; 257551; -.
DR   MGI; MGI:2138648; Serpinb10.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; Q8K1K6; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   ChiTaRS; Serpinb10; mouse.
DR   PRO; PR:Q8K1K6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8K1K6; protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor.
FT   CHAIN           1..397
FT                   /note="Serpin B10"
FT                   /id="PRO_0000094115"
FT   MOTIF           74..77
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   SITE            362..363
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  45115 MW;  C9DE8E9A2248DA73 CRC64;
     MASLAVSINQ FALEFSKKLA ESAEGRNIFF SPWGISTALA MLYLGTKGTT ADQMAQVLQF
     SSVEDFKSCP DSEKKRKMEF NSGKFEEIQS DFQTLAAEIL KPGNSYVLKT ANRIYGEKTY
     PFHNKYLEDM KTYFGAEPQS VNFVEASGQI RKEINSWVGS QTGGKIPNLL PDDSVDTKTK
     MVLVNALYFK GTWEHQFSVK NTTERPFRVN KTTSKPVQMM SMKQSLQVFH IEELQTIGLQ
     LHYQNRDLSL LLLLPEAIDG LEQLERAITY EKLDKWTSAD MMDTYEVQLY LPKFKMEESY
     DLKSALRGMG MTDVFSQSKA DFSNMTSERN LFLSNVFHKT FLEINEEGTE AAAGTGSEIS
     VRIKAPSIEL NVDHPFLFFI RHNKTKSILF CGRFCSP