VM3CX_MACLB
ID VM3CX_MACLB Reviewed; 612 AA.
AC Q7T046;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Snake venom metalloproteinase;
DE Short=SVMP;
DE AltName: Full=VL factor X activator;
DE AltName: Full=VLFXA heavy chain;
DE Contains:
DE RecName: Full=Coagulation factor X-activating enzyme heavy chain alternate form;
DE Flags: Precursor;
OS Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX NCBI_TaxID=8709;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 194-207, GLYCOSYLATION, AND
RP SUBUNIT.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15450849; DOI=10.1016/j.bbapap.2004.07.007;
RA Siigur E., Aaspollu A., Trummal K., Tonismaegi K., Tammiste I.,
RA Kalkkinen N., Siigur J.;
RT "Factor X activator from Vipera lebetina venom is synthesized from
RT different genes.";
RL Biochim. Biophys. Acta 1702:41-51(2004).
RN [2]
RP FUNCTION, SUBUNIT, AND GLYCOSYLATION.
RC TISSUE=Venom;
RX PubMed=11731090; DOI=10.1016/s0304-4165(01)00206-9;
RA Siigur E., Tonismagi K., Trummal K., Samel M., Vija H., Subbi J.,
RA Siigur J.;
RT "Factor X activator from Vipera lebetina snake venom, molecular
RT characterization and substrate specificity.";
RL Biochim. Biophys. Acta 1568:90-98(2001).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP GLYCOSYLATION.
RC TISSUE=Venom;
RX PubMed=11910177; DOI=10.1159/000048055;
RA Siigur J., Aaspollu A., Tonismagi K., Trummal K., Samel M., Vija H.,
RA Subbi J., Siigur E.;
RT "Proteases from Vipera lebetina venom affecting coagulation and
RT fibrinolysis.";
RL Haemostasis 31:123-132(2001).
CC -!- FUNCTION: Catalytic subunit of blood coagulation factor X-activating
CC enzyme. Activates coagulation factor X (F10) by cleaving the Arg(234)-
CC Ile(235) bond, activates coagulation factor IX (F9) by cleaving the
CC Arg(226)-Val(227) bond and is also able to activate protein C (PROC).
CC {ECO:0000269|PubMed:11731090, ECO:0000269|PubMed:11910177}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specifically activates several components of the blood
CC clotting system, including coagulation factor X, coagulation factor
CC IX and protein C by cleavage of Arg-|-Xaa bonds. Has no action on
CC insulin B chain.; EC=3.4.24.58;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Calcium is required for the activity of the
CC heterotrimer. {ECO:0000269|PubMed:11910177}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:11910177};
CC -!- SUBUNIT: Heterotrimer; disulfide-linked. The heterotrimer consists of 1
CC heavy chain and 2 light chains (lectins): LC1 and LC2 (AC Q7T045 and AC
CC Q696W1). {ECO:0000269|PubMed:11731090, ECO:0000269|PubMed:15450849}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated. Contains 8.0% of hexoses, 2.5% of hexosamines and
CC 2.5% of sialic acids. {ECO:0000269|PubMed:11731090,
CC ECO:0000269|PubMed:11910177, ECO:0000269|PubMed:15450849}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIId sub-subfamily. {ECO:0000305}.
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DR EMBL; AY339162; AAQ17467.1; -; mRNA.
DR AlphaFoldDB; Q7T046; -.
DR SMR; Q7T046; -.
DR MEROPS; M12.158; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
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 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; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..193
FT /note="Or 194"
FT /evidence="ECO:0000269|PubMed:15450849"
FT /id="PRO_0000029029"
FT CHAIN 194..612
FT /note="Coagulation factor X-activating enzyme heavy chain"
FT /id="PRO_0000029030"
FT CHAIN 195..612
FT /note="Coagulation factor X-activating enzyme heavy chain
FT alternate form"
FT /id="PRO_0000029031"
FT DOMAIN 201..395
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 403..489
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 467..469
FT /note="D/ECD-tripeptide"
FT ACT_SITE 336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..390
FT /evidence="ECO:0000250"
FT DISULFID 350..374
FT /evidence="ECO:0000250"
FT DISULFID 352..357
FT /evidence="ECO:0000250"
FT DISULFID 461..481
FT /evidence="ECO:0000250"
FT DISULFID 579
FT /note="Interchain (with C-158 in coagulation factor X-
FT activating enzyme light chain LC2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 612 AA; 68775 MW; C61B42CC9AC00DC1 CRC64;
MMQVLLVTIS LAVFPYQGSS IILESGNVND YEVVYPQKIT ALPEEAVQQP EQKYEDTMQY
EFEVNGEPVV LHLEKNKDLF SEDYSETRYS PDGRETTTKP PVQDHCYYHG RIQNDAYSSA
SISACNGLKG HFKLQGETYL IEPLKIPDSE AHAVYKYENI EKEDEAPKMC GVTQTNWESD
EPIKKASQLV ATSAKRKFHK TFIELVIVVD HRVVKKYDSA ATNTKIYEIV NTVNEIFIPL
NIRLTLIGVE FWCNRDLINV TSSADDTLDS FGEWRGSDLL NRKRHDNAQL FTDMKFDLST
LGITFLDGMC QAYRSVGIVQ EHGNKNFKTA VIMAHELGHN LGMYHDRKNC ICNDSSCIMS
AVLSSQPSKL FSNCSNHDYR RYLTTYKPKC ILNPPLRKDI ASPPICGNEI WEEGEECDCG
SPKDCQNPCC DAATCKLTPG AECGNGLCCE KCKIKTAGTV CRRARDECDV PEHCTGQSAE
CPADGFHANG QPCQNNNGYC YNGDCPIMTK QCISLFGSRA TVAEDSCFQE NQKGSYYGYC
RKENGRKIPC APQDIKCGRL YCLDNSPGNK NPCKMHYRCR DQHKGMVEPG TKCEDGKVCN
NKRQCVDVNT AY
