ID   SPB10_SORAR             Reviewed;         397 AA.
AC   B3RFC3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Serpin B10;
GN   Name=SERPINB10;
OS   Sorex araneus (Eurasian common shrew) (European shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Soricinae; Sorex.
OX   NCBI_TaxID=42254;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA   Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA   Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA   Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA   Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA   Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA   Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA   Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA   Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA   Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; DP000788; ACE79048.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3RFC3; -.
DR   SMR; B3RFC3; -.
DR   MEROPS; I04.015; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Protease inhibitor; Serine protease inhibitor.
FT   CHAIN           1..397
FT                   /note="Serpin B10"
FT                   /id="PRO_0000355550"
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;  45169 MW;  8A674D47D2BCE2FF CRC64;
     MDSLANSINQ FALEFSKKLA ETDEGKNIFF SPWGISTTLA MVYLGTKGTT ATQMAQVLQF
     DTDQDVKSSP ENEKKRKVDL NSDQVGEIHF GFQKLISEIN NPSNTYVLKT ANGIYGEKTY
     PFHNKYIEDI KTYFGAKPQS VNFVEDSDQI RKDINSWVES QTEGKIPNLL PDDAVDSATK
     MVLVNALYFK GLWEHQFSVQ DTTEKPFRIN KTSSKPVQMM SMKKNLEVFH IEKPQATGLR
     LDYKNRDLSL LLILPEDVCG LDQLEKAITY DQLSEWTSED MMEMYTVELH LPKFKLEQSY
     DLKTTLASMG MSDAFNQSKA DFSGMSDERN LYLSNVFHKS FVEINEQGTE AAAGSASEIS
     VRIKLPTIEI NADHPFIFFI RHNKTNSILF YGRFCSP