VM3E_ECHCA
ID VM3E_ECHCA Reviewed; 616 AA.
AC Q90495;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like ecarin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Echis carinatus (Saw-scaled viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX NCBI_TaxID=40353;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 191-228; 353-357; 372-383;
RP 393-415; 446-453; 459-474; 553-561; 574-597 AND 610-616, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=7849037; DOI=10.1021/bi00005a034;
RA Nishida S., Fujita T., Kohno N., Atoda H., Morita T., Takeya H., Kido I.,
RA Paine M.J.I., Kawabata S., Iwanaga S.;
RT "cDNA cloning and deduced amino acid sequence of prothrombin activator
RT (ecarin) from Kenyan Echis carinatus venom.";
RL Biochemistry 34:1771-1778(1995).
RN [2]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=956136; DOI=10.1093/oxfordjournals.jbchem.a131150;
RA Morita T., Iwanaga S., Suzuki T.;
RT "The mechanism of activation of bovine prothrombin by an activator isolated
RT from Echis carinatus venom and characterization of the new active
RT intermediates.";
RL J. Biochem. 79:1089-1108(1976).
RN [3]
RP REVIEW.
RX PubMed=15922779; DOI=10.1016/j.toxicon.2005.02.019;
RA Kini R.M.;
RT "The intriguing world of prothrombin activators from snake venom.";
RL Toxicon 45:1133-1145(2005).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that catalyzes the
CC conversion of prothrombin (F2) to alpha-thrombin through formation of a
CC thrombin intermediate. Has a low Km for prothrombin and a high kcat.
CC Cleaves the 320-Arg-Ile-321 bond in prothrombin and produces
CC meizothrombin which is ultimately converted to alpha-thrombin by
CC autolysis. {ECO:0000269|PubMed:956136}.
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: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7849037}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- MISCELLANEOUS: Does not inhibit platelet aggregation and does not
CC promote hemorrhage. {ECO:0000303|PubMed:15922779}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; D32212; BAA06910.1; -; mRNA.
DR PIR; A55796; A55796.
DR AlphaFoldDB; Q90495; -.
DR SMR; Q90495; -.
DR MEROPS; M12.151; -.
DR BRENDA; 3.4.21.60; 2035.
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:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
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; Prothrombin activator; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..190
FT /evidence="ECO:0000269|PubMed:7849037"
FT /id="PRO_0000029027"
FT CHAIN 191..616
FT /note="Zinc metalloproteinase-disintegrin-like ecarin"
FT /id="PRO_0000029028"
FT DOMAIN 201..397
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 405..491
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 469..471
FT /note="D/ECD-tripeptide"
FT ACT_SITE 338
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 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 312..392
FT /evidence="ECO:0000250"
FT DISULFID 352..376
FT /evidence="ECO:0000250"
FT DISULFID 354..359
FT /evidence="ECO:0000250"
FT DISULFID 408..437
FT /evidence="ECO:0000250"
FT DISULFID 419..432
FT /evidence="ECO:0000250"
FT DISULFID 421..427
FT /evidence="ECO:0000250"
FT DISULFID 431..454
FT /evidence="ECO:0000250"
FT DISULFID 445..451
FT /evidence="ECO:0000250"
FT DISULFID 450..476
FT /evidence="ECO:0000250"
FT DISULFID 463..483
FT /evidence="ECO:0000250"
FT DISULFID 470..502
FT /evidence="ECO:0000250"
FT DISULFID 495..507
FT /evidence="ECO:0000250"
FT DISULFID 514..567
FT /evidence="ECO:0000250"
FT DISULFID 529..578
FT /evidence="ECO:0000250"
FT DISULFID 542..555
FT /evidence="ECO:0000250"
FT DISULFID 562..604
FT /evidence="ECO:0000250"
FT DISULFID 598..609
FT /evidence="ECO:0000250"
SQ SEQUENCE 616 AA; 69463 MW; 09CC3CD1AD252346 CRC64;
MIQILLVIIC LAVFPYQGCS IILGSGNVND YEVVYPQKVT ALPKGAVQQP EQKYEDAMQY
EFEVKGEPVV LHLEKNKELF SEDYSETHYS SDDREITTNP SVEDHCYYHG RIQNDAESTA
SISACNGLKG HFKLRGETYF IEPLKIPDSE AHAVYKYENI ENEDEAPKMC GVTQDNWESD
EPIKKTLGLI VPPHERKFEK KFIELVVVVD HSMVTKYNND STAIRTWIYE MLNTVNEIYL
PFNIRVALVG LEFWCNGDLI NVTSTADDTL HSFGEWRASD LLNRKRHDHA QLLTNVTLDH
STLGITFVYG MCKSDRSVEL ILDYSNITFN MAYIIAHEMG HSLGMLHDTK FCTCGAKPCI
MFGKESIPPP KEFSSCSYDQ YNKYLLKYNP KCILDPPLRK DIASPAVCGN EIWEEGEECD
CGSPADCRNP CCDAATCKLK PGAECGNGEC CDKCKIRKAG TECRPARDDC DVAEHCTGQS
AECPRNEFQR NGQPCLNNSG YCYNGDCPIM LNQCIALFSP SATVAQDSCF QRNLQGSYYG
YCTKEIGYYG KRFPCAPQDV KCGRLYCLDN SFKKNMRCKN DYSYADENKG IVEPGTKCED
GKVCINRKCV DVNTAY
