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Entry version 108 (02 Jun 2021)
Sequence version 1 (01 Nov 1996)
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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:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi204Calcium 1By similarity1
Metal bindingi288Calcium 1By similarity1
Metal bindingi337Zinc; catalyticCurated1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei338PROSITE-ProRule annotation1
Metal bindingi341Zinc; catalyticCurated1
Metal bindingi347Zinc; catalyticCurated1
Metal bindingi392Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi395Calcium 1By similarity1
Metal bindingi410Calcium 2By similarity1
Metal bindingi414Calcium 2By similarity1
Metal bindingi417Calcium 2By similarity1
Metal bindingi420Calcium 2By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionBlood coagulation cascade activating toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Protease, Prothrombin activator, Toxin
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.21.60, 2035

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M12.151

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Zinc metalloproteinase-disintegrin-like ecarin (EC:3.4.24.-)
Alternative name(s):
Snake venom metalloproteinase
Short name:
SVMP
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEchis carinatus (Saw-scaled viper)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri40353 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeEchis

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20Sequence analysisAdd BLAST20
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002902721 – 1901 PublicationAdd BLAST170
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000029028191 – 616Zinc metalloproteinase-disintegrin-like ecarinAdd BLAST426

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi219N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi261N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi295N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi312 ↔ 392By similarity
Glycosylationi326N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi497N-linked (GlcNAc...) asparagineSequence analysis1
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

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed by the venom gland.Curated

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q90495

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini201 – 397Peptidase M12BPROSITE-ProRule annotationAdd BLAST197
Domaini405 – 491DisintegrinPROSITE-ProRule annotationAdd BLAST87

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi469 – 471D/ECD-tripeptide3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04269, ZnMc_adamalysin_II_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.390.10, 1 hit
4.10.70.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006586, ADAM_Cys-rich
IPR018358, Disintegrin_CS
IPR001762, Disintegrin_dom
IPR036436, Disintegrin_dom_sf
IPR024079, MetalloPept_cat_dom_sf
IPR001590, Peptidase_M12B
IPR002870, Peptidase_M12B_N
IPR034027, Reprolysin_adamalysin

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08516, ADAM_CR, 1 hit
PF00200, Disintegrin, 1 hit
PF01562, Pep_M12B_propep, 1 hit
PF01421, Reprolysin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00289, DISINTEGRIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00608, ACR, 1 hit
SM00050, DISIN, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57552, SSF57552, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50215, ADAM_MEPRO, 1 hit
PS00427, DISINTEGRIN_1, 1 hit
PS50214, DISINTEGRIN_2, 1 hit
PS00142, ZINC_PROTEASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i09CC3CD1AD252346
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D32212 mRNA Translation: BAA06910.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A55796

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

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

3D structure databases

SMRiQ90495
ModBaseiSearch...

Protein family/group databases

MEROPSiM12.151

Enzyme and pathway databases

BRENDAi3.4.21.60, 2035

Family and domain databases

CDDicd04269, ZnMc_adamalysin_II_like, 1 hit
Gene3Di3.40.390.10, 1 hit
4.10.70.10, 1 hit
InterProiView protein in InterPro
IPR006586, ADAM_Cys-rich
IPR018358, Disintegrin_CS
IPR001762, Disintegrin_dom
IPR036436, Disintegrin_dom_sf
IPR024079, MetalloPept_cat_dom_sf
IPR001590, Peptidase_M12B
IPR002870, Peptidase_M12B_N
IPR034027, Reprolysin_adamalysin
PfamiView protein in Pfam
PF08516, ADAM_CR, 1 hit
PF00200, Disintegrin, 1 hit
PF01562, Pep_M12B_propep, 1 hit
PF01421, Reprolysin, 1 hit
PRINTSiPR00289, DISINTEGRIN
SMARTiView protein in SMART
SM00608, ACR, 1 hit
SM00050, DISIN, 1 hit
SUPFAMiSSF57552, SSF57552, 1 hit
PROSITEiView protein in PROSITE
PS50215, ADAM_MEPRO, 1 hit
PS00427, DISINTEGRIN_1, 1 hit
PS50214, DISINTEGRIN_2, 1 hit
PS00142, ZINC_PROTEASE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiVM3E_ECHCA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q90495
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: November 1, 1996
Last modified: June 2, 2021
This is version 108 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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