ID SPB6_BOVIN Reviewed; 378 AA.
AC O02739; A5PK82;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 24-JAN-2024, entry version 120.
DE RecName: Full=Serpin B6;
DE AltName: Full=Proteinase inhibitor 6;
DE AltName: Full=Serine proteinase inhibitor B-43;
GN Name=SERPINB6;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=9013786; DOI=10.1016/s0169-328x(96)00133-7;
RA Nakaya N., Nishibori M., Kawabata M., Saeki K.;
RT "Cloning of a serine proteinase inhibitor from bovine brain: expression in
RT the brain and characterization of its target proteinases.";
RL Brain Res. Mol. Brain Res. 42:293-300(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inhibitor of cathepsin G, kallikrein-8 and thrombin. May play
CC an important role in the inner ear in the protection against leakage of
CC lysosomal content during stress (By similarity). May be involved in the
CC regulation of serine proteinases present in the brain or extravasated
CC from the blood. {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with the monomeric form of beta-tryptase.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain.
CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily.
CC {ECO:0000305}.
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DR EMBL; D55670; BAA19875.1; -; mRNA.
DR EMBL; BC142394; AAI42395.1; -; mRNA.
DR RefSeq; NP_777214.1; NM_174789.1.
DR AlphaFoldDB; O02739; -.
DR SMR; O02739; -.
DR STRING; 9913.ENSBTAP00000070967; -.
DR PaxDb; 9913-ENSBTAP00000026816; -.
DR PeptideAtlas; O02739; -.
DR GeneID; 286854; -.
DR KEGG; bta:286854; -.
DR CTD; 5269; -.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; O02739; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR CDD; cd19565; serpinB6_CAP; 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:SF204; SERPIN B6; 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 Acetylation; Cytoplasm; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor.
FT CHAIN 1..378
FT /note="Serpin B6"
FT /id="PRO_0000094105"
FT SITE 343..344
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P35237"
FT MOD_RES 196
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60854"
SQ SEQUENCE 378 AA; 42561 MW; 664F499CCFCE263A CRC64;
MDALSEANGT FALTLLKKLG EGNSKNVFIS PLSISSALAM VLLGAKGNTA AQMCQTLSLN
KSSGGGEDVH QGFQNLLSEV NRRDTQYLLR TANRLFGEKT YDFLSSFKDS CHKFYQAEME
ELDFVSATEQ SRKHINTWVA EKTEGKIRDL LPANSVNPMT RLVLVNAIYF KGNWDTQFNK
EHTEERPFRV SKNVEKPVQM MFKKSTCKIT YIGEISTQIL VLPYVGQELN MVILLPSEST
DLNTVEKALT YEKFIAWTKP DVMDEEEVEV FLPRFTLEES YDMEEFLQEL GMTDAFEETR
ADFSGMSSGR GLHLSKVMHK SFVEVTEEGT EAAAATGAVV MMRCLMVVPR FNANHPFLFF
IQHSKTGAIL FCGRFCSP
//
