[1]	PROTEIN SEQUENCE, AND VARIANTS. TISSUE=Venom; PubMed=1304358 [NCBI, ExPASy, EBI, Israel, Japan] Randolph A., Chamberlain S.H., Chu H.L.C., Retzios A.D., Markland F.S. Jr., Masiarz F.R.; "Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme from Agkistrodon contortrix contortrix venom."; Protein Sci. 1:590-600(1992).
[2]	DISULFIDE BONDS. DOI=10.1110/ps.110101; PubMed=11369866 [NCBI, ExPASy, EBI, Israel, Japan] Jones G., Ronk M., Mori F., Zhang Z.; "Disulfide structure of alfimeprase: a recombinant analog of fibrolase."; Protein Sci. 10:1264-1267(2001).

Comments

FUNCTION: This protein is a zinc protease from snake venom that acts in hemorrhage. It cleaves fibrinogen.
CATALYTIC ACTIVITY: Hydrolysis of 14-Ala-|-Leu-15 in insulin B chain and 413-Lys-|-Leu-414 in alpha-chain of fibrinogen.
COFACTOR: Binds 1 zinc ion per subunit (Probable).
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
PHARMACEUTICAL: Is currently used in a clinical trial for the treatment of peripheral arterial occlusion.
SIMILARITY: Belongs to the snake venom metalloproteinase family. P-I subfamily.
SIMILARITY: Contains 1 peptidase M12B domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

HSSP

P34179; 4AIG. [HSSP ENTRY / PDB]

ModBase

P28891.

Protein family/group databases

MEROPS

M12.133; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006025; Pept_M_Zn_BS.
IPR001590; Peptidase_M12B.
Graphical view of domain structure.

Pfam

PF01421; Reprolysin; 1.
Pfam graphical view of domain structure.

PROSITE

PS50215; ADAM_MEPRO; 1.
PS00142; ZINC_PROTEASE; 1.
PROSITE graphical view of domain structure (profiles).

Phylogenomic databases

HOVERGEN

P28891; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Pharmaceutical; Protease; Pyrrolidone carboxylic acid; Secreted; Toxin; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 203`	`203`	`Zinc metalloproteinase fibrolase.`	`PRO_0000078197`
`DOMAIN`	`7 203`	`197`	`Peptidase M12B.`
`ACT_SITE`	`144 144`		`By similarity.`
`METAL`	`143 143`		`Zinc; catalytic (Probable).`
`METAL`	`147 147`		`Zinc; catalytic (Probable).`
`METAL`	`153 153`		`Zinc; catalytic (Probable).`
`MOD_RES`	`1 1`		`Pyrrolidone carboxylic acid.`
`DISULFID`	`118 198`
`DISULFID`	`158 182`
`DISULFID`	`160 165`
`VARIANT`	`1 1`	`1`	`Missing (in some of the chains).`
`VARIANT`	`189 189`	`1`	`T -> E.`
`VARIANT`	`192 192`	`1`	`T -> L.`

Sequence information

Length: 203 AA [This is the length of the unprocessed precursor]

Molecular weight: 22908 Da [This is the MW of the unprocessed precursor]

CRC64: 646EBE6F7F1EA191 [This is a checksum on the sequence]

        10         20         30         40         50         60 
QQRFPQRYVQ LVIVADHRMN TKYNGDSDKI RQWVHQIVNT INEIYRPLNI QFTLVGLEIW 

        70         80         90        100        110        120 
SNQDLITVTS VSHDTLASFG NWRETDLLRR QRHDNAQLLT AIDFDGDTVG LAYVGGMCQL 

       130        140        150        160        170        180 
KHSTGVIQDH SAINLLVALT MAHELGHNLG MNHDGNQCHC GANSCVMAAM LSDQPSKLFS 

       190        200 
DCSKKDYQTF LTVNNPQCIL NKP

P28891 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools