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Entry version 35 (26 Feb 2020)
Sequence version 1 (21 Sep 2011)
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Protein

Zinc metalloproteinase-disintegrin-like MTP8

Gene
N/A
Organism
Drysdalia coronoides (White-lipped snake) (Hoplocephalus coronoides)
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 may impair hemostasis in the prey.

<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 bindingi208Calcium 1By similarity1
Metal bindingi292Calcium 1By similarity1
Metal bindingi341Zinc; catalyticBy similarity1
Metal bindingi345Zinc; catalyticBy similarity1
Metal bindingi351Zinc; catalyticBy similarity1
Metal bindingi396Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi399Calcium 1By similarity1
Metal bindingi414Calcium 2By similarity1
Metal bindingi416Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi418Calcium 2By similarity1
Metal bindingi421Calcium 2By similarity1
Metal bindingi424Calcium 2By similarity1
Metal bindingi475Calcium 3By similarity1
Metal bindingi476Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi478Calcium 3By similarity1
Metal bindingi490Calcium 3By 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 functionHemostasis impairing toxin, Hydrolase, Metalloprotease, Protease, Toxin
LigandCalcium, Metal-binding, Zinc

<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 MTP8 (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>OrganismiDrysdalia coronoides (White-lipped snake) (Hoplocephalus coronoides)
<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 identifieri66186 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeNotechinaeDrysdalia

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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_000042550421 – 191Sequence analysisAdd BLAST171
<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_0000425505192 – 613Zinc metalloproteinase-disintegrin-like MTP8Add BLAST422

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>Glycosylationi282N-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 bondi316 ↔ 396By similarity
Disulfide bondi356 ↔ 380By similarity
Disulfide bondi358 ↔ 363By similarity
Disulfide bondi412 ↔ 441By similarity
Disulfide bondi423 ↔ 436By similarity
Disulfide bondi425 ↔ 431By similarity
Disulfide bondi435 ↔ 458By similarity
Glycosylationi437N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi449 ↔ 455By similarity
Disulfide bondi454 ↔ 480By similarity
Disulfide bondi467 ↔ 487By similarity
Disulfide bondi474 ↔ 506By similarity
Disulfide bondi499 ↔ 511By similarity
Disulfide bondi518 ↔ 568By similarity
Disulfide bondi533 ↔ 575By similarity
Disulfide bondi543 ↔ 577By similarity
Disulfide bondi546 ↔ 556By similarity
Glycosylationi550N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi563 ↔ 601By similarity
Glycosylationi572N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi595 ↔ 606By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
F8RKW0

<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.

<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.

By similarity

<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
F8RKW0

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>Domaini205 – 401Peptidase M12BPROSITE-ProRule annotationAdd BLAST197
Domaini409 – 495DisintegrinPROSITE-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>Motifi473 – 475D/ECD-tripeptide3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi496 – 613Cys-richAdd BLAST118

<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.

F8RKW0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIEVLLVTIC FTVFPYQGSP IILESGNVND YEVVYPQKVP ALPKGGVQNP
60 70 80 90 100
QPETKYEDTM QYEFHVNGEP VVLHLERNKG LFSEDYTETH YAPDGREITT
110 120 130 140 150
SPPVQDHCYY HGYIQNEADS SAAISACDGL KGHFKHRGET YFIEPLKLSN
160 170 180 190 200
SESHAIYKDE HVEKEDEIPK ICGVTQTTSE SDETIEKISQ LTNTPEQDRY
210 220 230 240 250
LQVKKYIELY VVVDNRMYRN YNSNRDAINE RVYEMVNTLN VMYRPLNFFI
260 270 280 290 300
ALIGLEIWSN QDEINIEPEV AVTLRSFGEW RNTTLLPRKR NDNAQLLTGI
310 320 330 340 350
DFNGATVGLA YVGTLCRPTQ SVAVIQDHSK RTSMVASTMA HELGHNLGIN
360 370 380 390 400
HDSASCNCNA GPCIMSATIS NQPLSEFSSC SVQEHQRYLL RVRPQCILNK
410 420 430 440 450
PLRKDIVTPP VCGNYFVERG EECDCGSPQD CQSACCNATT CKLQHEAQCD
460 470 480 490 500
SGECCEQCKF KKAGAECRAA KDDCDLPESC TGQSAKCPTD SFQRNGHPCQ
510 520 530 540 550
NNQGYCYNGK CLIMTNQCIA LKGPGVNVSP DECFTLKQND PECGFCRIEN
560 570 580 590 600
GTKIPCAEKD KMCGKLLCQE GNATCICFPT TDDPDYGMVE PGTKCGDGKV
610
CINRQCVDVQ TAY
Length:613
Mass (Da):68,427
Last modified:September 21, 2011 - 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:i77FAF32F56BC15C2
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
HM627203 mRNA Translation: AEH95530.1

<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
HM627203 mRNA Translation: AEH95530.1

3D structure databases

SMRiF8RKW0
ModBaseiSearch...

Proteomic databases

PRIDEiF8RKW0

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiVM38_DRYCN
<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: F8RKW0
<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: February 19, 2014
Last sequence update: September 21, 2011
Last modified: February 26, 2020
This is version 35 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 programChordata Protein Annotation Program
Annotation programAnimal Toxin 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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