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Protein

Zinc metalloproteinase-disintegrin-like ecarin

Gene
N/A
Organism
Echis carinatus (Saw-scaled viper)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Snake venom zinc metalloproteinase that catalyzes the conversion of prothrombin (F2) to alpha-thrombin through formation of a thrombin intermediate. Has a low Km for prothrombin and a high kcat. Cleaves the 320-Arg-Ile-321 bond in prothrombin and produces meizothrombin which is ultimately converted to alpha-thrombin by autolysis.1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi204 – 2041Calcium 1By similarity
Metal bindingi288 – 2881Calcium 1By similarity
Metal bindingi337 – 3371Zinc; catalyticCurated
Active sitei338 – 3381PROSITE-ProRule annotation
Metal bindingi341 – 3411Zinc; catalyticCurated
Metal bindingi347 – 3471Zinc; catalyticCurated
Metal bindingi392 – 3921Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi395 – 3951Calcium 1By similarity
Metal bindingi410 – 4101Calcium 2By similarity
Metal bindingi414 – 4141Calcium 2By similarity
Metal bindingi417 – 4171Calcium 2By similarity
Metal bindingi420 – 4201Calcium 2By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade activating toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Protease, Prothrombin activator, Toxin

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.151.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc metalloproteinase-disintegrin-like ecarin (EC:3.4.24.-)
Alternative name(s):
Snake venom metalloproteinase
Short name:
SVMP
OrganismiEchis carinatus (Saw-scaled viper)
Taxonomic identifieri40353 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeEchis

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 1901701 PublicationPRO_0000029027Add
BLAST
Chaini191 – 616426Zinc metalloproteinase-disintegrin-like ecarinPRO_0000029028Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence analysis
Glycosylationi261 – 2611N-linked (GlcNAc...)Sequence analysis
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence analysis
Disulfide bondi312 ↔ 392By similarity
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence analysis
Disulfide bondi352 ↔ 376By similarity
Disulfide bondi354 ↔ 359By similarity
Disulfide bondi408 ↔ 437By similarity
Disulfide bondi419 ↔ 432By similarity
Disulfide bondi421 ↔ 427By similarity
Disulfide bondi431 ↔ 454By similarity
Disulfide bondi445 ↔ 451By similarity
Disulfide bondi450 ↔ 476By similarity
Disulfide bondi463 ↔ 483By similarity
Disulfide bondi470 ↔ 502By similarity
Disulfide bondi495 ↔ 507By similarity
Glycosylationi497 – 4971N-linked (GlcNAc...)Sequence analysis
Disulfide bondi514 ↔ 567By similarity
Disulfide bondi529 ↔ 578By similarity
Disulfide bondi542 ↔ 555By similarity
Disulfide bondi562 ↔ 604By similarity
Disulfide bondi598 ↔ 609By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Tissue specificityi

Expressed by the venom gland.Curated

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliQ90495.
SMRiQ90495. Positions 197-616.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini201 – 397197Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini405 – 49187DisintegrinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi469 – 4713D/ECD-tripeptide

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi492 – 616125Cys-richAdd
BLAST

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006978.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q90495-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQILLVIIC LAVFPYQGCS IILGSGNVND YEVVYPQKVT ALPKGAVQQP
60 70 80 90 100
EQKYEDAMQY EFEVKGEPVV LHLEKNKELF SEDYSETHYS SDDREITTNP
110 120 130 140 150
SVEDHCYYHG RIQNDAESTA SISACNGLKG HFKLRGETYF IEPLKIPDSE
160 170 180 190 200
AHAVYKYENI ENEDEAPKMC GVTQDNWESD EPIKKTLGLI VPPHERKFEK
210 220 230 240 250
KFIELVVVVD HSMVTKYNND STAIRTWIYE MLNTVNEIYL PFNIRVALVG
260 270 280 290 300
LEFWCNGDLI NVTSTADDTL HSFGEWRASD LLNRKRHDHA QLLTNVTLDH
310 320 330 340 350
STLGITFVYG MCKSDRSVEL ILDYSNITFN MAYIIAHEMG HSLGMLHDTK
360 370 380 390 400
FCTCGAKPCI MFGKESIPPP KEFSSCSYDQ YNKYLLKYNP KCILDPPLRK
410 420 430 440 450
DIASPAVCGN EIWEEGEECD CGSPADCRNP CCDAATCKLK PGAECGNGEC
460 470 480 490 500
CDKCKIRKAG TECRPARDDC DVAEHCTGQS AECPRNEFQR NGQPCLNNSG
510 520 530 540 550
YCYNGDCPIM LNQCIALFSP SATVAQDSCF QRNLQGSYYG YCTKEIGYYG
560 570 580 590 600
KRFPCAPQDV KCGRLYCLDN SFKKNMRCKN DYSYADENKG IVEPGTKCED
610
GKVCINRKCV DVNTAY
Length:616
Mass (Da):69,463
Last modified:November 1, 1996 - v1
Checksum:i09CC3CD1AD252346
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D32212 mRNA. Translation: BAA06910.1.
PIRiA55796.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D32212 mRNA. Translation: BAA06910.1.
PIRiA55796.

3D structure databases

ProteinModelPortaliQ90495.
SMRiQ90495. Positions 197-616.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.151.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006978.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "cDNA cloning and deduced amino acid sequence of prothrombin activator (ecarin) from Kenyan Echis carinatus venom."
    Nishida S., Fujita T., Kohno N., Atoda H., Morita T., Takeya H., Kido I., Paine M.J.I., Kawabata S., Iwanaga S.
    Biochemistry 34:1771-1778(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 191-228; 353-357; 372-383; 393-415; 446-453; 459-474; 553-561; 574-597 AND 610-616, SUBCELLULAR LOCATION.
    Tissue: Venom and Venom gland.
  2. "The mechanism of activation of bovine prothrombin by an activator isolated from Echis carinatus venom and characterization of the new active intermediates."
    Morita T., Iwanaga S., Suzuki T.
    J. Biochem. 79:1089-1108(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Tissue: Venom.
  3. "The intriguing world of prothrombin activators from snake venom."
    Kini R.M.
    Toxicon 45:1133-1145(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiVM3E_ECHCA
AccessioniPrimary (citable) accession number: Q90495
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: November 1, 1996
Last modified: October 14, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Does not inhibit platelet aggregation and does not promote hemorrhage.1 Publication

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.