ID   FTE46_BOTJA             Reviewed;         341 AA.
AC   Q9DGI0;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Antihemorrhagic factor BJ46a;
DE   AltName: Full=Metalloproteinase inhibitor;
DE   Flags: Precursor;
OS   Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8724 {ECO:0000312|EMBL:AAG09055.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-191; 212-224; 252-293
RP   AND 307-341, FUNCTION, GLYCOSYLATION AT ASN-95 AND ASN-282, SUBUNIT, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver {ECO:0000269|PubMed:11358523};
RX   PubMed=11358523; DOI=10.1046/j.1432-1327.2001.02199.x;
RA   Valente R.H., Dragulev B., Perales J., Fox J.W., Domont G.B.;
RT   "BJ46a, a snake venom metalloproteinase inhibitor. Isolation,
RT   characterization, cloning and insights into its mechanism of action.";
RL   Eur. J. Biochem. 268:3042-3052(2001).
CC   -!- FUNCTION: Potent inhibitor of hemorrhagic activity but also proteolytic
CC       activities of atrolysin C and jararhagin. Inhibition occurs by
CC       formation of a non-covalent complex between BJ46a and the proteinases
CC       at their metalloproteinase domains. {ECO:0000269|PubMed:11358523}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11358523}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC   -!- MASS SPECTROMETRY: Mass=46101; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11358523};
CC   -!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00861, 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; AF294836; AAG09055.1; -; mRNA.
DR   AlphaFoldDB; Q9DGI0; -.
DR   SMR; Q9DGI0; -.
DR   MEROPS; I25.026; -.
DR   MEROPS; I25.042; -.
DR   iPTMnet; Q9DGI0; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IDA:UniProtKB.
DR   CDD; cd00042; CY; 2.
DR   InterPro; IPR000010; Cystatin_dom.
DR   InterPro; IPR025760; Cystatin_Fetuin_A.
DR   InterPro; IPR046350; Cystatin_sf.
DR   InterPro; IPR001363; Prot_inh_fetuin_CS.
DR   Pfam; PF00031; Cystatin; 1.
DR   SMART; SM00043; CY; 2.
DR   SUPFAM; SSF54403; SSF54403; 2.
DR   PROSITE; PS51529; CYSTATIN_FETUIN_A; 2.
DR   PROSITE; PS01254; FETUIN_1; 1.
DR   PROSITE; PS01255; FETUIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:11358523"
FT   CHAIN           20..341
FT                   /note="Antihemorrhagic factor BJ46a"
FT                   /id="PRO_0000008902"
FT   DOMAIN          22..130
FT                   /note="Cystatin fetuin-A-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DOMAIN          141..254
FT                   /note="Cystatin fetuin-A-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   MOTIF           23..25
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   SITE            140..141
FT                   /note="Cleavage; by trypsin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:11358523"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:11358523"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        28..332
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        85..96
FT                   /evidence="ECO:0000250|UniProtKB:P29695,
FT                   ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        110..129
FT                   /evidence="ECO:0000250|UniProtKB:P29695,
FT                   ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        143..146
FT                   /evidence="ECO:0000250|UniProtKB:P29695,
FT                   ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        205..217
FT                   /evidence="ECO:0000250|UniProtKB:P29695,
FT                   ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        230..253
FT                   /evidence="ECO:0000250|UniProtKB:P29695,
FT                   ECO:0000255|PROSITE-ProRule:PRU00861"
SQ   SEQUENCE   341 AA;  38779 MW;  1C11D320AED9FC21 CRC64;
     MNSLVALVLL GQIIGSTLSS QVRGDLECDE KDAKEWTDTG VRYINEHKLH GYKYALNVIK
     NIVVVPWDGD WVAVFLKLNL LETECHVLDP TPVKNCTVRP QHNHAVEMDC DVKIMFNVDT
     FKEDVFAKCH STPDSVENVR RNCPKCPILL PSNNPQVVDS VEYVLNKHNE KLSDHVYEVL
     EISRGQHKYE PEAYYVEFAI VEVNCTAQEL HDDHHHCHPN TAGEDHIGFC RATVFRSHAS
     LEKPKDEQFE SDCVILHVKE GHAHSHLIQQ HVEKDSISPE HNNTALNFVH PHNDTSTSHE
     SHEHLAEVPV AFVKKELPKD ISDRHTTPVK GCPGKVHHFE L