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 01-MAY-2013, entry version 65.
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; Scleroglossa; Serpentes; Colubroidea;
OC 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.
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 -!- COFACTOR: Binds 2 calcium ion per subunit.
CC -!- COFACTOR: Binds 1 zinc ion per subunit.
CC -!- SUBUNIT: Heterotrimer; disulfide-linked. The heterotrimer consists
CC of 1 heavy chain and 2 light chains: LC1 and LC2.
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.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC P-III subfamily. P-IIId sub-subfamily.
CC -!- SIMILARITY: Contains 1 disintegrin domain.
CC -!- SIMILARITY: Contains 1 peptidase M12B domain.
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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 MEROPS; M12.158; -.
DR HOVERGEN; HBG006978; -.
DR EvolutionaryTrace; Q7LZ61; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; Disintegrin; 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 Potential.
FT PROPEP 21 188
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.
FT DOMAIN 401 487 Disintegrin.
FT MOTIF 465 467 D/ECD-tripeptide.
FT COMPBIAS 488 615 Cys-rich.
FT ACT_SITE 334 334 By similarity.
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 CARBOHYD 257 257 N-linked (GlcNAc...) (complex).
FT CARBOHYD 351 351 N-linked (GlcNAc...) (complex).
FT CARBOHYD 371 371 N-linked (GlcNAc...) (complex).
FT DISULFID 215 251
FT DISULFID 308 388
FT DISULFID 348 372
FT DISULFID 350 355
FT DISULFID 404 433
FT DISULFID 415 428
FT DISULFID 417 423
FT DISULFID 427 450
FT DISULFID 441 447
FT DISULFID 446 472
FT DISULFID 459 479
FT DISULFID 466 498
FT DISULFID 491 503
FT DISULFID 510 560
FT DISULFID 525 571
FT DISULFID 538 548
FT DISULFID 555 597
FT DISULFID 577 577 Interchain (with C-158 in coagulation
FT factor X-activating enzyme light chain
FT LC2).
FT DISULFID 591 603
FT CONFLICT 191 191 S -> A (in Ref. 3; AA sequence).
FT STRAND 199 207
FT TURN 209 214
FT HELIX 219 235
FT HELIX 236 238
FT STRAND 240 249
FT HELIX 262 275
FT HELIX 277 280
FT STRAND 284 290
FT HELIX 295 297
FT STRAND 300 302
FT TURN 310 312
FT STRAND 313 318
FT HELIX 324 337
FT TURN 338 340
FT HELIX 371 384
FT HELIX 395 397
FT TURN 430 432
FT STRAND 442 444
FT STRAND 458 460
FT TURN 492 495
FT HELIX 506 514
FT HELIX 523 530
FT STRAND 534 536
FT HELIX 553 555
FT STRAND 570 573
FT STRAND 590 592
FT STRAND 595 597
FT STRAND 603 605
FT HELIX 606 609
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
//
