ID   FIBR_AGKCO              Reviewed;         203 AA.
AC   P28891;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   16-DEC-2008, entry version 60.
DE   RecName: Full=Zinc metalloproteinase fibrolase;
DE            EC=3.4.24.72;
DE   AltName: Full=Fibrinolytic proteinase;
DE   AltName: INN=Alfimeprase;
OS   Agkistrodon contortrix contortrix (Southern copperhead).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Crotalinae; Agkistrodon.
OX   NCBI_TaxID=8713;
RN   [1]
RP   PROTEIN SEQUENCE, AND VARIANTS.
RC   TISSUE=Venom;
RX   MEDLINE=93278288; PubMed=1304358;
RA   Randolph A., Chamberlain S.H., Chu H.L.C., Retzios A.D.,
RA   Markland F.S. Jr., Masiarz F.R.;
RT   "Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme
RT   from Agkistrodon contortrix contortrix venom.";
RL   Protein Sci. 1:590-600(1992).
RN   [2]
RP   DISULFIDE BONDS.
RX   MEDLINE=21262576; PubMed=11369866; DOI=10.1110/ps.110101;
RA   Jones G., Ronk M., Mori F., Zhang Z.;
RT   "Disulfide structure of alfimeprase: a recombinant analog of
RT   fibrolase.";
RL   Protein Sci. 10:1264-1267(2001).
CC   -!- FUNCTION: This protein is a zinc protease from snake venom that
CC       acts in hemorrhage. It cleaves fibrinogen.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of 14-Ala-|-Leu-15 in insulin B
CC       chain and 413-Lys-|-Leu-414 in alpha-chain of fibrinogen.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (Probable).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PHARMACEUTICAL: Is currently used in a clinical trial for the
CC       treatment of peripheral arterial occlusion.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase family. P-I
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
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DR   HSSP; P34179; 4AIG.
DR   MEROPS; M12.133; -.
DR   HOVERGEN; P28891; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR006025; Pept_M_Zn_BS.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
KW   Pharmaceutical; Protease; Pyrrolidone carboxylic acid; Secreted;
KW   Toxin; Zinc.
FT   CHAIN         1    203       Zinc metalloproteinase fibrolase.
FT                                /FTId=PRO_0000078197.
FT   DOMAIN        7    203       Peptidase M12B.
FT   ACT_SITE    144    144       By similarity.
FT   METAL       143    143       Zinc; catalytic (Probable).
FT   METAL       147    147       Zinc; catalytic (Probable).
FT   METAL       153    153       Zinc; catalytic (Probable).
FT   MOD_RES       1      1       Pyrrolidone carboxylic acid.
FT   DISULFID    118    198
FT   DISULFID    158    182
FT   DISULFID    160    165
FT   VARIANT       1      1       Missing (in some of the chains).
FT   VARIANT     189    189       T -> E.
FT   VARIANT     192    192       T -> L.
SQ   SEQUENCE   203 AA;  22908 MW;  646EBE6F7F1EA191 CRC64;
     QQRFPQRYVQ LVIVADHRMN TKYNGDSDKI RQWVHQIVNT INEIYRPLNI QFTLVGLEIW
     SNQDLITVTS VSHDTLASFG NWRETDLLRR QRHDNAQLLT AIDFDGDTVG LAYVGGMCQL
     KHSTGVIQDH SAINLLVALT MAHELGHNLG MNHDGNQCHC GANSCVMAAM LSDQPSKLFS
     DCSKKDYQTF LTVNNPQCIL NKP
//