ID   SPB10_RAT               Reviewed;         397 AA.
AC   Q8K3K4; Q6P7C1;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   RecName: Full=Serpin B10;
DE   AltName: Full=TGF-beta-repressible serine proteinase inhibitor;
DE            Short=Trespin;
DE   AltName: Full=Transforming growth factor beta repressible serpin;
GN   Name=Serpinb10;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Wistar;
RX   PubMed=11986314; DOI=10.1074/jbc.m201244200;
RA   Chipuk J.E., Stewart L.V., Ranieri A., Song K., Danielpour D.;
RT   "Identification and characterization of a novel rat ov-serpin family
RT   member, trespin.";
RL   J. Biol. Chem. 277:26412-26421(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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). Inhibits plasmin. {ECO:0000250,
CC       ECO:0000269|PubMed:11986314}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC       {ECO:0000269|PubMed:11986314}.
CC   -!- TISSUE SPECIFICITY: Expressed in many tissues, including brain, heart,
CC       kidney, liver, lung, prostate, skin, spleen and stomach.
CC       {ECO:0000269|PubMed:11986314}.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY075037; AAL78042.1; -; mRNA.
DR   EMBL; BC061735; AAH61735.1; -; mRNA.
DR   RefSeq; NP_714955.2; NM_153733.2.
DR   AlphaFoldDB; Q8K3K4; -.
DR   SMR; Q8K3K4; -.
DR   STRING; 10116.ENSRNOP00000003314; -.
DR   MEROPS; I04.015; -.
DR   PhosphoSitePlus; Q8K3K4; -.
DR   PaxDb; 10116-ENSRNOP00000003314; -.
DR   GeneID; 266775; -.
DR   KEGG; rno:266775; -.
DR   UCSC; RGD:628853; rat.
DR   AGR; RGD:628853; -.
DR   CTD; 5273; -.
DR   RGD; 628853; Serpinb10.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; Q8K3K4; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; Q8K3K4; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q8K3K4; -.
DR   Proteomes; UP000002494; Unplaced.
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:0030414; F:peptidase inhibitor activity; IDA:RGD.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IDA:RGD.
DR   CDD; cd19569; serpinB10_bomapin; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   PANTHER; PTHR11461:SF175; SERPIN B10; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 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_0000094116"
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"
FT   CONFLICT        88
FT                   /note="M -> I (in Ref. 2; AAH61735)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="D -> G (in Ref. 2; AAH61735)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        288
FT                   /note="R -> Q (in Ref. 2; AAH61735)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        391
FT                   /note="D -> Y (in Ref. 2; AAH61735)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   397 AA;  45387 MW;  19E7BF371A9D2F4C CRC64;
     MASLAVSINQ FAVEFSKKLA ESAEGRNIFF SPWGISTSLA MVYLGTKGTT AAQMSQVLHF
     GSIQDFKFGP DSEKKRKMEC HSGKSEEMQS DFQTLTAKIL KHGNSYVLKI ANRIYVEKTY
     LFHNKYLEDM KTYFGAEPQS VNFVEASGQI RKEINSWVGS QTGDKIPNLL PDDAVDNKTT
     MVLVNALYFK GTWEHQFSVQ NTTERPFRIN KTTSKPVQMM SMKQSLQVFH IEELQTIGVQ
     LHYQNREFSL LLLLPEEVEG LKQLERAITY EKLDKWTSAD MMDTYEVRLY LPKFKMEESY
     DLQSALRDMG MTDAFNQGKA NFSNMTSERN LFLSNVFHKT FLEINEEGTE AAAGTGSEVN
     FRIKAPSIEL NADHPFLFLI RHNVTNTILF DGRFYSP
//