F12AI_BOVIN
ID F12AI_BOVIN Reviewed; 468 AA.
AC P50448;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Factor XIIa inhibitor;
DE Short=XIIaINH;
DE Flags: Precursor;
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=Liver;
RA Edmeston J.E., Strumpfer A., Muldbjerg M., Halkier T., Macgillivray R.T.A.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=8457651;
RA Muldbjerg M., Markussen S., Magnusson S., Halkier T.;
RT "Bovine factor XIIa inhibitor.";
RL Blood Coagul. Fibrinolysis 4:47-54(1993).
RN [3]
RP PROTEIN SEQUENCE OF 24-33.
RC TISSUE=Serum;
RX PubMed=3814612; DOI=10.1016/0304-4165(87)90001-8;
RA van Nostrand W.E., Cunningham D.D.;
RT "Purification of a proteinase inhibitor from bovine serum with C1-inhibitor
RT activity.";
RL Biochim. Biophys. Acta 923:167-175(1987).
CC -!- FUNCTION: May play a potentially crucial role in regulating important
CC physiological pathways including complement activation, blood
CC coagulation, fibrinolysis and the generation of kinins.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: N- and O-glycosylated.
CC -!- MISCELLANEOUS: Could be the ortholog of SERPING1.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U30332; AAA73928.1; -; mRNA.
DR RefSeq; NP_777246.1; NM_174821.2.
DR AlphaFoldDB; P50448; -.
DR SMR; P50448; -.
DR MINT; P50448; -.
DR STRING; 9913.ENSBTAP00000021638; -.
DR MEROPS; I04.024; -.
DR PaxDb; P50448; -.
DR PeptideAtlas; P50448; -.
DR PRIDE; P50448; -.
DR GeneID; 281035; -.
DR KEGG; bta:281035; -.
DR CTD; 710; -.
DR eggNOG; KOG2392; Eukaryota.
DR OrthoDB; 1124079at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0045916; P:negative regulation of complement activation; IEA:InterPro.
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; IPR015553; C1-inh.
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 PANTHER; PTHR11461:SF159; PTHR11461:SF159; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Direct protein sequencing; Disulfide bond; Fibrinolysis;
KW Glycoprotein; Hemostasis; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:3814612"
FT CHAIN 24..468
FT /note="Factor XIIa inhibitor"
FT /id="PRO_0000032529"
FT REGION 27..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 434..435
FT /note="Reactive bond"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 97..396
FT /evidence="ECO:0000250"
FT DISULFID 104..179
FT /evidence="ECO:0000250"
FT CONFLICT 78
FT /note="S -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..85
FT /note="PV -> TL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="S -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="T -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="C -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="L -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="L -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="K -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="L -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="T -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="I -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="R -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 51723 MW; E5029063E199734D CRC64;
MASRLTPLTL LLLLLLAGDR VTSDMIVGPG NLQEGESEGD SQKGGILDGE SIQGNEDSPT
LPITNLTVVP ATVTKPFSQP ATEPVQSTIQ PTAEPFCLAP VTSCSDSEIR SAEAVLGEAL
TDFSLRLYQD FSVLKKRETN FIFSPFSIAS LLTQILLGAG GETRVSLEHL LSYPQNFSCV
HHALRAFMSE GFTSFSQIFH SSDLTIKDTF AEASQRLYGS SPRPLGNDST ASLELINDWV
AKKTNLRIRR LLDSLPEDTR LILLNAVALS AKWKIAFDKG RTSTKPFHLK SSAIKVPMMN
SKKYPVASFT DRTLNRPGGR LQLSHNLSFV ILVPQTVKHH LQDLEQALST AVFKAVIKKL
EMTKFHPTHL TMPRIKVQSS QDMLDYFDFI YDVNLCGLTE DPDVQVSGIR HQATLELTES
GVDATAASVV SVARNLLLFE VQQPFLFLLW DQQHKFPVFM GRVYDPKG
