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Database: UniProt
Entry: Q7LZ61
LinkDB: Q7LZ61
Original site: Q7LZ61 
ID   VM3CX_DABSI             Reviewed;         619 AA.
AC   Q7LZ61; B4UT23;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   26-NOV-2014, entry version 74.
DE   RecName: Full=Coagulation factor X-activating enzyme heavy chain;
DE            EC=3.4.24.58;
DE   AltName: Full=Coagulation factor X-activating enzyme chain alpha;
DE   AltName: Full=RVV-X heavy chain;
DE   AltName: Full=Russellysin;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   Flags: Precursor;
OS   Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC   Toxicofera; Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX   NCBI_TaxID=343250;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND GLYCOSYLATION PATTERN.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=18616470; DOI=10.1111/j.1742-4658.2008.06540.x;
RA   Chen H.S., Chen J.M., Lin C.W., Khoo K.H., Tsai I.H.;
RT   "New insights into the functions and N-glycan structures of factor X
RT   activator from Russell's viper venom.";
RL   FEBS J. 275:3944-3958(2008).
RN   [2]
RP   PROTEIN SEQUENCE OF 189-429, ENZYME ACTIVITY, AND GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=1629211;
RA   Takeya H., Nishida S., Miyata T., Kawada S., Saisaka Y., Morita T.,
RA   Iwanaga S.;
RT   "Coagulation factor X activating enzyme from Russell's viper venom
RT   (RVV-X). A novel metalloproteinase with disintegrin (platelet
RT   aggregation inhibitor)-like and C-type lectin-like domains.";
RL   J. Biol. Chem. 267:14109-14117(1992).
RN   [3]
RP   PROTEIN SEQUENCE OF 189-207, ENZYME ACTIVITY, SUBUNIT, AND
RP   GLYCOSYLATION AT ASN-216; ASN-257; ASN-351 AND ASN-371.
RC   TISSUE=Venom;
RX   PubMed=8144654;
RA   Gowda D.C., Jackson C.M., Hensley P., Davidson E.A.;
RT   "Factor X-activating glycoprotein of Russell's viper venom.
RT   Polypeptide composition and characterization of the carbohydrate
RT   moieties.";
RL   J. Biol. Chem. 269:10644-10650(1994).
RN   [4]
RP   ROLE OF GLYCOSYLATION.
RX   PubMed=8639544; DOI=10.1021/bi953043e;
RA   Gowda D.C., Jackson C.M., Kurzban G.P., McPhie P., Davidson E.A.;
RT   "Core sugar residues of the N-linked oligosaccharides of Russell's
RT   viper venom factor X-activator maintain functionally active
RT   polypeptide structure.";
RL   Biochemistry 35:5833-5837(1996).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 189-615 IN COMPLEX WITH LC1
RP   AND LC2, METAL-BINDING SITES, GLYCOSYLATION AT ASN-257 AND ASN-371,
RP   SUBUNIT, AND DISULFIDE BONDS.
RX   PubMed=18060879; DOI=10.1016/j.febslet.2007.11.062;
RA   Takeda S., Igarashi T., Mori H.;
RT   "Crystal structure of RVV-X: an example of evolutionary gain of
RT   specificity by ADAM proteinases.";
RL   FEBS Lett. 581:5859-5864(2007).
RN   [6]
RP   REVIEW.
RX   PubMed=11910189;
RA   Tans G., Rosing J.;
RT   "Snake venom activators of factor X: an overview.";
RL   Haemostasis 31:225-233(2001).
CC   -!- FUNCTION: Catalytic subunit of blood coagulation factor X-
CC       activating enzyme. Activates coagulation factor X (F10) by
CC       cleaving the Arg-Ile bond and is also able to activate coagulation
CC       factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-
CC       Ile and Arg-Val bonds. {ECO:0000269|PubMed:18616470}.
CC   -!- CATALYTIC ACTIVITY: Specifically activates several components of
CC       the blood clotting system, including coagulation factor X,
CC       coagulation factor IX and protein C by cleavage of Arg-|-Xaa
CC       bonds. Has no action on insulin B chain.
CC       {ECO:0000269|PubMed:1629211, ECO:0000269|PubMed:8144654}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterotrimer; disulfide-linked. The heterotrimer consists
CC       of 1 heavy chain and 2 light chains (lectins): LC1 and LC2.
CC       {ECO:0000269|PubMed:18060879, ECO:0000269|PubMed:8144654}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: N-glycosylated; probably required for conformation. Removal
CC       of easily accessible sugars does not change its functional
CC       capacity, but removal of the core sugars with N-glycanase causes a
CC       virtually complete loss of enzyme activity, apparently as a result
CC       of major conformational changes in the molecule. Not O-
CC       glycosylated. {ECO:0000269|PubMed:1629211,
CC       ECO:0000269|PubMed:18060879, ECO:0000269|PubMed:18616470,
CC       ECO:0000269|PubMed:8144654}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC       P-III subfamily. P-IIId sub-subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 disintegrin domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00068}.
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00276}.
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DR   EMBL; DQ137799; AAZ39881.1; -; mRNA.
DR   PIR; A42972; A42972.
DR   PDB; 2E3X; X-ray; 2.91 A; A=189-615.
DR   PDBsum; 2E3X; -.
DR   ProteinModelPortal; Q7LZ61; -.
DR   MEROPS; M12.158; -.
DR   HOVERGEN; HBG006978; -.
DR   EvolutionaryTrace; Q7LZ61; -.
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   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Blood-coag_inhib_Disintegrin.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR024079; MetalloPept_cat_dom.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Blood coagulation cascade activating toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Toxin; Zinc.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   PROPEP       21    188       {ECO:0000269|PubMed:1629211,
FT                                ECO:0000269|PubMed:8144654}.
FT                                /FTId=PRO_0000355226.
FT   CHAIN       189    619       Coagulation factor X-activating enzyme
FT                                heavy chain.
FT                                /FTId=PRO_0000078204.
FT   DOMAIN      199    393       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      401    487       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   MOTIF       465    467       D/ECD-tripeptide.
FT   COMPBIAS    488    615       Cys-rich.
FT   ACT_SITE    334    334       {ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       333    333       Zinc; catalytic.
FT   METAL       337    337       Zinc; catalytic.
FT   METAL       343    343       Zinc; catalytic.
FT   METAL       403    403       Calcium 1; via carbonyl oxygen.
FT   METAL       406    406       Calcium 1.
FT   METAL       408    408       Calcium 1; via carbonyl oxygen.
FT   METAL       410    410       Calcium 1.
FT   METAL       413    413       Calcium 1.
FT   METAL       416    416       Calcium 1.
FT   METAL       467    467       Calcium 2.
FT   METAL       468    468       Calcium 2; via carbonyl oxygen.
FT   METAL       470    470       Calcium 2.
FT   METAL       482    482       Calcium 2.
FT   METAL       483    483       Calcium 2; via carbonyl oxygen.
FT   CARBOHYD    216    216       N-linked (GlcNAc...) (complex).
FT                                {ECO:0000269|PubMed:8144654}.
FT   CARBOHYD    257    257       N-linked (GlcNAc...) (complex).
FT                                {ECO:0000269|PubMed:18060879,
FT                                ECO:0000269|PubMed:8144654}.
FT   CARBOHYD    351    351       N-linked (GlcNAc...) (complex).
FT                                {ECO:0000269|PubMed:8144654}.
FT   CARBOHYD    371    371       N-linked (GlcNAc...) (complex).
FT                                {ECO:0000269|PubMed:18060879,
FT                                ECO:0000269|PubMed:8144654}.
FT   DISULFID    215    251       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    308    388       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    348    372       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    350    355       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    404    433       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    415    428       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    417    423       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    427    450       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    441    447       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    446    472       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    459    479       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    466    498       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    491    503       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    510    560       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    525    571       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    538    548       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    555    597       {ECO:0000269|PubMed:18060879}.
FT   DISULFID    577    577       Interchain (with C-158 in coagulation
FT                                factor X-activating enzyme light chain
FT                                LC2). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068, ECO:0000255|PROSITE-
FT                                ProRule:PRU00276,
FT                                ECO:0000269|PubMed:18060879}.
FT   DISULFID    591    603       {ECO:0000269|PubMed:18060879}.
FT   CONFLICT    191    191       S -> A (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND      199    207       {ECO:0000244|PDB:2E3X}.
FT   TURN        209    214       {ECO:0000244|PDB:2E3X}.
FT   HELIX       219    235       {ECO:0000244|PDB:2E3X}.
FT   HELIX       236    238       {ECO:0000244|PDB:2E3X}.
FT   STRAND      240    249       {ECO:0000244|PDB:2E3X}.
FT   HELIX       262    275       {ECO:0000244|PDB:2E3X}.
FT   HELIX       277    280       {ECO:0000244|PDB:2E3X}.
FT   STRAND      284    290       {ECO:0000244|PDB:2E3X}.
FT   HELIX       295    297       {ECO:0000244|PDB:2E3X}.
FT   STRAND      300    302       {ECO:0000244|PDB:2E3X}.
FT   TURN        310    312       {ECO:0000244|PDB:2E3X}.
FT   STRAND      313    318       {ECO:0000244|PDB:2E3X}.
FT   HELIX       324    337       {ECO:0000244|PDB:2E3X}.
FT   TURN        338    340       {ECO:0000244|PDB:2E3X}.
FT   HELIX       371    384       {ECO:0000244|PDB:2E3X}.
FT   HELIX       395    397       {ECO:0000244|PDB:2E3X}.
FT   TURN        430    432       {ECO:0000244|PDB:2E3X}.
FT   STRAND      442    444       {ECO:0000244|PDB:2E3X}.
FT   STRAND      458    460       {ECO:0000244|PDB:2E3X}.
FT   TURN        492    495       {ECO:0000244|PDB:2E3X}.
FT   HELIX       506    514       {ECO:0000244|PDB:2E3X}.
FT   HELIX       523    530       {ECO:0000244|PDB:2E3X}.
FT   STRAND      534    536       {ECO:0000244|PDB:2E3X}.
FT   HELIX       553    555       {ECO:0000244|PDB:2E3X}.
FT   STRAND      570    573       {ECO:0000244|PDB:2E3X}.
FT   STRAND      590    592       {ECO:0000244|PDB:2E3X}.
FT   STRAND      595    597       {ECO:0000244|PDB:2E3X}.
FT   STRAND      603    605       {ECO:0000244|PDB:2E3X}.
FT   HELIX       606    609       {ECO:0000244|PDB:2E3X}.
SQ   SEQUENCE   619 AA;  69648 MW;  71084A3B46338797 CRC64;
     MMQVLLVTIS LAVFPYQGSS IILESGNVND YEVVYPQKVT ALPKGAVQQP EQKYEDTMQY
     EFEVNGEPVV LHLEKNKILF SEDYSETHYY PDGREITTNP PVEDHCYYHG RIQNDAHSSA
     SISACNGLKG HFKLRGEMYF IEPLKLSNSE AHAVYKYENI EKEDEIPKMC GVTQTNWESD
     KPIKKASQLV STSAQFNKIF IELVIIVDHS MAKKCNSTAT NTKIYEIVNS ANEIFNPLNI
     HVTLIGVEFW CDRDLINVTS SADETLNSFG EWRASDLMTR KSHDNALLFT DMRFDLNTLG
     ITFLAGMCQA YRSVEIVQEQ GNRNFKTAVI MAHELSHNLG MYHDGKNCIC NDSSCVMSPV
     LSDQPSKLFS NCSIHDYQRY LTRYKPKCIF NPPLRKDIVS PPVCGNEIWE EGEECDCGSP
     ANCQNPCCDA ATCKLKPGAE CGNGLCCYQC KIKTAGTVCR RARDECDVPE HCTGQSAECP
     RDQLQQNGKP CQNNRGYCYN GDCPIMRNQC ISLFGSRANV AKDSCFQENL KGSYYGYCRK
     ENGRKIPCAP QDVKCGRLFC LNNSPRNKNP CNMHYSCMDQ HKGMVDPGTK CEDGKVCNNK
     RQCVDVNTAY QSTTGFSQI
//
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