ID   SPB8_BOVIN              Reviewed;         374 AA.
AC   Q5BIR5;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Serpin B8;
GN   Name=SERPINB8;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Has an important role in epithelial desmosome-mediated cell-
CC       cell adhesion. {ECO:0000250|UniProtKB:P50452}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BT021159; AAX31341.1; -; mRNA.
DR   RefSeq; NP_001030364.1; NM_001035287.1.
DR   RefSeq; XP_015315533.1; XM_015460047.1.
DR   AlphaFoldDB; Q5BIR5; -.
DR   SMR; Q5BIR5; -.
DR   STRING; 9913.ENSBTAP00000001597; -.
DR   MEROPS; I04.013; -.
DR   PaxDb; Q5BIR5; -.
DR   PeptideAtlas; Q5BIR5; -.
DR   PRIDE; Q5BIR5; -.
DR   Ensembl; ENSBTAT00000001597; ENSBTAP00000001597; ENSBTAG00000001207.
DR   GeneID; 513825; -.
DR   KEGG; bta:513825; -.
DR   CTD; 5271; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001207; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000154835; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; Q5BIR5; -.
DR   OMA; NCIFFCG; -.
DR   OrthoDB; 1124079at2759; -.
DR   TreeFam; TF352619; -.
DR   Proteomes; UP000009136; Chromosome 24.
DR   Bgee; ENSBTAG00000001207; Expressed in zone of skin and 104 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
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; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor.
FT   CHAIN           1..374
FT                   /note="Serpin B8"
FT                   /id="PRO_0000094110"
FT   SITE            339..340
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  42173 MW;  156506FF9023092E CRC64;
     MDALCEANGT FAINLLKMLG EEDHLRNVFF SPLSLSSVLT MVLMGAKGNT AAQMSQALCL
     NESGDVHRGF QSLLREVSTS GPKCLLRTAN RLFGEKTCDF LPAFKESCQK FYQADLEELS
     FAEDTEECRK HINDWVMEKT DGKISEILGA GTVSPLTKLV LVNAIYFKGK WNEQFDRKHT
     RGMPFKTNQE KKTVQMMFKQ AKFKMGHVEE VPAQVLELPY VGAELSMLIL LPDENTDLAV
     VEKALTYEKF RTWTSPEKLT EEKVQVFLPR LKLEASYDLE AFLRSLGMTD AFEEAKADFS
     GMSAKKNVPM SKVAHKCFVE VNEEGTEAAG ATAVVRNSRC CRMEPKFCAD HPFLFFIRHR
     ETNSILFCGR FSSP