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UniProtKB/Swiss-Prot entry Q7T046


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RVXX_VIPLE
Primary accession number Q7T046
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on October 1, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 32)
Name and origin of the protein
Protein name Coagulation factor X-activating enzyme heavy chain [Precursor]
Synonyms EC 3.4.24.58
Coagulation factor X-activating enzyme chain alpha
VLFXA heavy chain
VL factor X activator
Contains Coagulation factor X-activating enzyme heavy chain alternate form
Gene name None
From
Vipera lebetina (Elephant snake) (Leventine viper) [TaxID: 8709] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 194-207, GLYCOSYLATION, AND SUBUNIT.
TISSUE=Venom, and Venom gland;
DOI=10.1016/j.bbapap.2004.07.007; PubMed=15450849 [NCBI, ExPASy, EBI, Israel, Japan]
Siigur E., Aaspollu A., Trummal K., Tonismaegi K., Tammiste I., Kalkkinen N., Siigur J.;
"Factor X activator from Vipera lebetina venom is synthesized from different genes.";
Biochim. Biophys. Acta 1702:41-51(2004).
[2]
FUNCTION, SUBUNIT, AND GLYCOSYLATION.
TISSUE=Venom;
DOI=10.1016/S0304-4165(01)00206-9; PubMed=11731090 [NCBI, ExPASy, EBI, Israel, Japan]
Siigur E., Tonismagi K., Trummal K., Samel M., Vija H., Subbi J., Siigur J.;
"Factor X activator from Vipera lebetina snake venom, molecular characterization and substrate specificity.";
Biochim. Biophys. Acta 1568:90-98(2001).
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.
  • 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: Heterotrimer; disulfide-linked. The heterotrimer consists of 1 heavy chain and 2 light chains: LC1 and LC2.
  • SUBCELLULAR LOCATION: Secreted.
  • TISSUE SPECIFICITY: Expressed by the venom gland.
  • PTM: N-glycosylated.
  • SIMILARITY: Belongs to the snake venom metalloproteinase family. P-III subfamily.
  • SIMILARITY: Contains 1 disintegrin domain.
  • SIMILARITY: Contains 1 peptidase M12B domain [view classification].
  • 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.
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
AY339162; AAQ17467.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P21859; 1J2L. [HSSP ENTRY / PDB]
ModBase Q7T046.
Protein family/group databases
MEROPS M12.158; -.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0007596; Biological process: blood coagulation (inferred from electronic annotation from UniProtKB-KW).
GO:0009405; Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006586; ADAM_cysteine.
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 PF08516; ADAM_CR; 1.
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 SM00608; ACR; 1.
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 Q7T046.
ProtoNet Q7T046.
Phylogenomic databases
HOVERGEN Q7T046; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Blood coagulation; Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20     Potential. 
PROPEP   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
DOMAIN   201   395  195     Peptidase M12B. 
DOMAIN   403   489  87     Disintegrin. 
MOTIF   467   469  3     D/ECD-tripeptide. 
COMPBIAS   490   612  123     Cys-rich. 
ACT_SITE   336   336        By similarity. 
METAL   335   335        Zinc; catalytic (By similarity). 
METAL   339   339        Zinc; catalytic (By similarity). 
METAL   345   345        Zinc; catalytic (By similarity). 
CARBOHYD   259   259        N-linked (GlcNAc...) (Potential). 
CARBOHYD   353   353        N-linked (GlcNAc...) (Potential). 
CARBOHYD   373   373        N-linked (GlcNAc...) (Potential). 
DISULFID   310   390        By similarity. 
DISULFID   350   374        By similarity. 
DISULFID   352   357        By similarity. 
DISULFID   461   481        By similarity. 
DISULFID   579   579        Interchain (with C-158 in coagulation factor X-activating enzyme light chain LC2) (Potential). 
Sequence information
Length: 612 AA [This is the length of the unprocessed precursor] Molecular weight: 68775 Da [This is the MW of the unprocessed precursor] CRC64: C61B42CC9AC00DC1 [This is a checksum on the sequence]
        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 

Q7T046 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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