Q7T046 (RVVX_MACLB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Coagulation factor X-activating enzyme heavy chain EC=3.4.24.58 Alternative name(s): Coagulation factor X-activating enzyme chain alpha VL factor X activator VLFXA heavy chain Cleaved into the following chain: Coagulation factor X-activating enzyme heavy chain alternate form
Organism	Macrovipera lebetina (Levantine viper) (Vipera lebetina)
Taxonomic identifier	8709 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Macrovipera

Protein attributes

Sequence length	612 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic subunit of coagulation factor X-activating enzyme, a zinc-protease enzyme that acts in hemorrhage. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond at position 234, activates coagulation factor IX (F9) by cleaving the Arg-Val bond at position 226 and is also able to activate protein C. Ref.2
Catalytic activity	Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of Arg-|-Xaa bonds. Has no action on insulin B chain.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Heterotrimer; disulfide-linked. The heterotrimer consists of 1 heavy chain and 2 light chains: LC1 and LC2. Ref.1 Ref.2
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	N-glycosylated. Ref.1 Ref.2
Sequence similarities	Belongs to the venom metalloproteinase family. P-III subfamily. Contains 1 disintegrin domain. Contains 1 peptidase M12B domain.
Caution	According to the current nomenclature, this heterotrimer is a member of the P-IV subfamily. This classification is due to the quaternary structure, where two C-type lectin-like proteins are connected to the main chain of the P-III subfamily by disulfide bonds.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease Toxin
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 193	173	Or 194		PRO_0000029029
	Chain	194 – 612	419	Coagulation factor X-activating enzyme heavy chain		PRO_0000029030
	Chain	195 – 612	418	Coagulation factor X-activating enzyme heavy chain alternate form		PRO_0000029031
Regions
	Domain	201 – 395	195	Peptidase M12B
	Domain	403 – 489	87	Disintegrin
	Motif	467 – 469	3	D/ECD-tripeptide
	Compositional bias	490 – 612	123	Cys-rich
Sites
	Active site	336	1	By similarity
	Metal binding	335	1	Zinc; catalytic By similarity
	Metal binding	339	1	Zinc; catalytic By similarity
	Metal binding	345	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	259	1	N-linked (GlcNAc...) Potential
	Glycosylation	353	1	N-linked (GlcNAc...) Potential
	Glycosylation	373	1	N-linked (GlcNAc...) Potential
	Disulfide bond	310 ↔ 390		By similarity
	Disulfide bond	350 ↔ 374		By similarity
	Disulfide bond	352 ↔ 357		By similarity
	Disulfide bond	461 ↔ 481		By similarity
	Disulfide bond	579		Interchain (with C-158 in coagulation factor X-activating enzyme light chain LC2) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q7T046 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: C61B42CC9AC00DC1	FASTA	612	68,775
	10 20 30 40 50 60 MMQVLLVTIS LAVFPYQGSS IILESGNVND YEVVYPQKIT ALPEEAVQQP EQKYEDTMQY 70 80 90 100 110 120 EFEVNGEPVV LHLEKNKDLF SEDYSETRYS PDGRETTTKP PVQDHCYYHG RIQNDAYSSA 130 140 150 160 170 180 SISACNGLKG HFKLQGETYL IEPLKIPDSE AHAVYKYENI EKEDEAPKMC GVTQTNWESD 190 200 210 220 230 240 EPIKKASQLV ATSAKRKFHK TFIELVIVVD HRVVKKYDSA ATNTKIYEIV NTVNEIFIPL 250 260 270 280 290 300 NIRLTLIGVE FWCNRDLINV TSSADDTLDS FGEWRGSDLL NRKRHDNAQL FTDMKFDLST 310 320 330 340 350 360 LGITFLDGMC QAYRSVGIVQ EHGNKNFKTA VIMAHELGHN LGMYHDRKNC ICNDSSCIMS 370 380 390 400 410 420 AVLSSQPSKL FSNCSNHDYR RYLTTYKPKC ILNPPLRKDI ASPPICGNEI WEEGEECDCG 430 440 450 460 470 480 SPKDCQNPCC DAATCKLTPG AECGNGLCCE KCKIKTAGTV CRRARDECDV PEHCTGQSAE 490 500 510 520 530 540 CPADGFHANG QPCQNNNGYC YNGDCPIMTK QCISLFGSRA TVAEDSCFQE NQKGSYYGYC 550 560 570 580 590 600 RKENGRKIPC APQDIKCGRL YCLDNSPGNK NPCKMHYRCR DQHKGMVEPG TKCEDGKVCN 610 NKRQCVDVNT AY

References

[1]	"Factor X activator from Vipera lebetina venom is synthesized from different genes." Siigur E., Aaspollu A., Trummal K., Tonismaegi K., Tammiste I., Kalkkinen N., Siigur J. Biochim. Biophys. Acta 1702:41-51(2004) [PubMed: 15450849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 194-207, GLYCOSYLATION, SUBUNIT. Tissue: Venom and Venom gland.
[2]	"Factor X activator from Vipera lebetina snake venom, molecular characterization and substrate specificity." Siigur E., Tonismagi K., Trummal K., Samel M., Vija H., Subbi J., Siigur J. Biochim. Biophys. Acta 1568:90-98(2001) [PubMed: 11731090] [Abstract] Cited for: FUNCTION, SUBUNIT, GLYCOSYLATION. Tissue: Venom.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY339162 mRNA. Translation: AAQ17467.1.
3D structure databases
ProteinModelPortal	Q7T046.
SMR	Q7T046. Positions 197-612.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG006978.
Family and domain databases
InterPro	IPR006586. ADAM_Cys-rich. IPR001762. Blood-coag_inhib_Disintegrin. IPR018358. Disintegrin_CS. IPR024079. MetalloPept_cat_dom. IPR001590. Peptidase_M12B. IPR002870. Peptidase_M12B_N. [Graphical view]
Gene3D	G3DSA:4.10.70.10. Blood-coag_inhib_Disintegrin. 1 hit. G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
Pfam	PF08516. ADAM_CR. 1 hit. PF00200. Disintegrin. 1 hit. PF01562. Pep_M12B_propep. 1 hit. PF01421. Reprolysin. 1 hit. [Graphical view]
PRINTS	PR00289. DISINTEGRIN.
SMART	SM00608. ACR. 1 hit. SM00050. DISIN. 1 hit. [Graphical view]
SUPFAM	SSF57552. Disintegrin. 1 hit.
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS00427. DISINTEGRIN_1. 1 hit. PS50214. DISINTEGRIN_2. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RVVX_MACLB

Accession

Primary (citable) accession number: Q7T046

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	October 1, 2003
Last modified:	November 16, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program

Annotation program

Chordata Protein Annotation Program