[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Venom gland; DOI=10.1016/S0041-0101(02)00081-8; PubMed=12076658 [NCBI, ExPASy, EBI, Israel, Japan] Kishimoto M., Takahashi T.; "Molecular cloning and sequence analysis of cDNA encoding flavoridin, a disintegrin from the venom of Trimeresurus flavoviridis."; Toxicon 40:1033-1040(2002).
[2]	PROTEIN SEQUENCE OF 414-483. TISSUE=Venom; PubMed=2364514 [NCBI, ExPASy, EBI, Israel, Japan] Musial J., Niewiarowski S., Rucinski B., Stewart G.J., Cook J.J., Williams J.A., Edmunds L.H. Jr.; "Inhibition of platelet adhesion to surfaces of extracorporeal circuits by disintegrins. RGD-containing peptides from viper venoms."; Circulation 82:261-273(1990).
[3]	PROTEIN SEQUENCE OF DISINTEGRIN FLAVORIDIN, AND DISULFIDE BONDS. TISSUE=Venom; DOI=10.1016/0014-5793(92)80797-K; PubMed=1516704 [NCBI, ExPASy, EBI, Israel, Japan] Calvete J.J., Wang Y., Mann K., Schaefer W., Niewiarwoski S., Stewart G.J.; "The disulfide bridge pattern of snake venom disintegrins, flavoridin and echistatin."; FEBS Lett. 309:316-320(1992).
[4]	DISULFIDE BONDS IN DISINTEGRIN FLAVORIDIN. DOI=10.1006/jmbi.1993.1438; PubMed=8355276 [NCBI, ExPASy, EBI, Israel, Japan] Klaus W., Broger C., Gerber P., Senn H.; "Determination of the disulphide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data. Application to flavoridin."; J. Mol. Biol. 232:897-906(1993).
[5]	STRUCTURE BY NMR OF 414-483. DOI=10.1006/jmbi.1993.1439; PubMed=8355277 [NCBI, ExPASy, EBI, Israel, Japan] Senn H., Klaus W.; "The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP IIb-IIIa receptor."; J. Mol. Biol. 232:907-925(1993).

Comments

FUNCTION: The metalloproteinase is a probable venom zinc protease that acts in hemorrhage (By similarity).
FUNCTION: The disintegrin inhibits fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex. Acts by binding to the glycoprotein IIb-IIIa receptor on the platelet surface and inhibits aggregation induced by ADP, thrombin, platelet-activating factor and collagen.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
SIMILARITY: Belongs to the snake venom metalloproteinase family. P-II subfamily.
SIMILARITY: Contains 1 disintegrin domain.
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

Sequence databases

EMBL

AB052155; BAC00515.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A58649; A58649.

3D structure databases

PDB

1FVL; NMR; -; A=414-483.

[ExPASy / RCSB / EBI]

1FVL; -.

P18619; 194-394.

Protein family/group databases

MEROPS

M12.155; -.

Family and domain databases

InterPro

IPR001762; Blood-coag_inhib_Disintegrin.
IPR006025; Pept_M_Zn_BS.
IPR001590; Peptidase_M12B.
IPR002870; Peptidase_M12B_N.
Graphical view of domain structure.

Gene3D

G3DSA:4.10.70.10; Blood-coag_inhib_Disintegrin; 1.

Pfam

PF00200; Disintegrin; 1.
PF01562; Pep_M12B_propep; 1.
PF01421; Reprolysin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00289; DISINTEGRIN.

ProDom

PD000664; Disintegrin; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00050; DISIN; 1.
SMART graphical view of domain structure.

PROSITE

PS50215; ADAM_MEPRO; 1.
PS00427; DISINTEGRIN_1; 1.
PS50214; DISINTEGRIN_2; 1.
PS00142; ZINC_PROTEASE; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P18619.

Phylogenomic databases

HOVERGEN

P18619; -.

Other

P18619; -.

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

Keywords

3D-structure; Blood coagulation; Cell adhesion; Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`Potential.`
`PROPEP`	`21 190`	`170`	`By similarity.`	`PRO_0000028996`
`CHAIN`	`191 395`	`205`	`Metalloproteinase.`	`PRO_0000028997`
`PROPEP`	`396 413`	`18`		`PRO_0000028998`
`CHAIN`	`414 483`	`70`	`Disintegrin flavoridin.`	`PRO_0000028999`
`DOMAIN`	`197 395`	`199`	`Peptidase M12B.`
`DOMAIN`	`403 483`	`81`	`Disintegrin.`
`MOTIF`	`462 464`	`3`	`Cell attachment site.`
`ACT_SITE`	`334 334`		`By similarity.`
`METAL`	`333 333`		`Zinc; catalytic (Probable).`
`METAL`	`337 337`		`Zinc; catalytic (Probable).`
`METAL`	`343 343`		`Zinc; catalytic (Probable).`
`CARBOHYD`	`263 263`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`293 293`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`308 390`		`By similarity.`
`DISULFID`	`352 374`		`By similarity.`
`DISULFID`	`354 357`		`By similarity.`
`DISULFID`	`417 432`
`DISULFID`	`419 427`
`DISULFID`	`426 449`
`DISULFID`	`440 446`
`DISULFID`	`445 470`
`DISULFID`	`458 477`
`CONFLICT`	`455 456`		`RT -> TG (in Ref. 2; AA sequence).`
`TURN`	`429 432`	`4`
`STRAND`	`444 446`	`3`
`STRAND`	`448 451`	`4`
`STRAND`	`457 459`	`3`
`STRAND`	`462 465`	`4`

Sequence information

Length: 483 AA [This is the length of the unprocessed precursor]

Molecular weight: 54514 Da [This is the MW of the unprocessed precursor]

CRC64: 3B943C81E6C7E1C3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPKRAVQQK YEDAMQYELK 

        70         80         90        100        110        120 
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE DHCYYHGRIH NDADSTASIS 

       130        140        150        160        170        180 
ACDGLKGYFK LQGETYLIEP LKLSDSEAHA VYKYENIEKE DEAPKMCGVT QNWESDESIK 

       190        200        210        220        230        240 
KASQLYLTPE QQRFPQRYIE LAIVVDHGMY KKYNHDSDKI KVRVHQMVNH INEMYRPLNI 

       250        260        270        280        290        300 
AITLSLLQIW SNKDLITVKS ASNVTLNLFG NWRETVLLKR RSHDCAHLLT DINFTGNIIG 

       310        320        330        340        350        360 
LAYKQGMCNP KLSVGLVQDY SSNVFVVAVI MTHELGHNLG MEHDEEKNGK KCNCKTCIMS 

       370        380        390        400        410        420 
PAISDPPAQL FSDCSKNDYH TFLTNRNPQC ILNAPLRTDT VSTPVSGNEF LEAGEECDCG 

       430        440        450        460        470        480 
SPSNPCCDAA TCKLRPGAQC ADGLCCDQCR FKKKRTICRI ARGDFPDDRC TGLSNDCPRW 


NDL

P18619 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