ID   SPB10_RHIFE             Reviewed;         397 AA.
AC   B2KI30;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Serpin B10;
DE   AltName: Full=Proteinase inhibitor 10;
GN   Name=SERPINB10;
OS   Rhinolophus ferrumequinum (Greater horseshoe bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC   Rhinolophinae; Rhinolophus.
OX   NCBI_TaxID=59479;
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 (APR-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; DP000700; ACC62105.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2KI30; -.
DR   SMR; B2KI30; -.
DR   MEROPS; I04.015; -.
DR   Proteomes; UP000472240; Unplaced.
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; Reference proteome;
KW   Serine protease inhibitor.
FT   CHAIN           1..397
FT                   /note="Serpin B10"
FT                   /id="PRO_0000355549"
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;  45401 MW;  7C227C733CFAD744 CRC64;
     MDSLTKSINQ FALEFSKKLA ESAEGKNIFF SPWGISTSLA MVYLGTRGTT AAQIAQVLQF
     NRDQDSKFFP ESEKKRKMDF NSRKVEEIRS DFQTLISEIN NPSNAYVLKT ANGIYGEKTY
     PFHNKYLEDM KTYFGVEPQS VNFLEAPDQT RNEINSWVES QTQGKILNLL PDDAVDSATR
     MVLVNAIYFK GIWEHQFSAR DTREKPFRIN KNTSKPVQMM SMKKKLQVFH IENPQAIGLQ
     LYYESRDLSL FLLLPEDVSG LDQLEKAVTY EKLSEWTSAD MMELYDVQLH LPKFKLEESY
     DLKSALSSMG MSDAFNQSKA DFSGMSVEGN LFLSNVFHKS FVEINEQGTE ASAGTGSEVS
     LRIRLPSIEF NADHPFLFFI RHNKTNSILF YGRFCSP