ID   SPB10_PLEMO             Reviewed;         397 AA.
AC   B1MTC3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Serpin B10;
GN   Name=SERPINB10;
OS   Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini;
OC   Pitheciidae; Callicebinae; Plecturocebus.
OX   NCBI_TaxID=9523;
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 (MAR-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; DP000624; ACA57868.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1MTC3; -.
DR   SMR; B1MTC3; -.
DR   MEROPS; I04.015; -.
DR   PRIDE; B1MTC3; -.
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_0000355546"
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;  45102 MW;  EAAC03853C740999 CRC64;
     MDALATSINQ FALELSKKLA ESAQGKNIFF SAWSISASLA MVHLGAKGNT AAQMAQVLQF
     KRDQGVKSDP ESEKKRKTEF NLSNSGEIHC NFQTLISEIL KPNNDYILKT ANAAYSEKTY
     PFHNKYLEDV KTYFGAEPQS VNFVEASDQI RKEINSWVER QTEGKIQNLL SDDSVGSTTR
     MVLVNALYFK GIWEHQFLVQ NTTEKPFRIN ETTSKPVQMM FMKEKLQIFH IEKPQALGLQ
     LYYKSCDLSL FILLPEDING LEQLEKAITY EKLSKWTSAD MMEVYDVQLH LPKFKLEESY
     DLKSTLSSMG MSDAFSESEA DFSGMSSARN LFLSNVFHKA FVEIDEQGTE AAAGSGSEIS
     FRIKVPSIEF NANHPFLFFI RHNKTNNILF YGRFCSP