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Entry version 36 (23 May 2018)
Sequence version 1 (15 Jun 2010)
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Protein

Zinc metalloproteinase-disintegrin-like atrase-A

Gene
N/A
Organism
Naja atra (Chinese cobra)
Status
Reviewed-Annotation score:

Annotation score:3 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 transcript 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 inhibits platelet aggregation by cleaving platelet glycoprotein Ib alpha (GP1BA) at Glu-298/Asp-299, and abolishes binding of von Willebrand factor (VWF) to GPIBA.By similarity

<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 ‘Function’ 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 bindingi290Calcium 1By similarity1
Metal bindingi338Zinc; catalyticBy similarity1
Metal bindingi342Zinc; catalyticBy similarity1
Metal bindingi348Zinc; catalyticBy similarity1
Metal bindingi393Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi396Calcium 1By similarity1
Metal bindingi411Calcium 2By similarity1
Metal bindingi413Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi415Calcium 2By similarity1
Metal bindingi418Calcium 2By similarity1
Metal bindingi421Calcium 2By similarity1
Metal bindingi472Calcium 3By similarity1
Metal bindingi473Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi475Calcium 3By similarity1
Metal bindingi487Calcium 3By similarity1
Metal bindingi488Calcium 3; via carbonyl oxygenBy 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 functionCell adhesion impairing toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Platelet aggregation inhibiting toxin, Protease, Toxin
LigandCalcium, Metal-binding, Zinc

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M12.159

<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_and_taxonomy_section">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 atrase-A (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_and_taxonomy_section">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>OrganismiNaja atra (Chinese cobra)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri8656 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

<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_processing_section">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_000041802921 – 196By similarityAdd BLAST176
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000418030197 – 607Zinc metalloproteinase-disintegrin-like atrase-AAdd BLAST411

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi220N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi270N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi301N-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 bondi314 ↔ 393By similarity
Disulfide bondi353 ↔ 377By similarity
Disulfide bondi355 ↔ 360By similarity
Disulfide bondi409 ↔ 438By similarity
Disulfide bondi420 ↔ 433By similarity
Disulfide bondi422 ↔ 428By similarity
Disulfide bondi432 ↔ 455By similarity
Glycosylationi434N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi446 ↔ 452By similarity
Disulfide bondi451 ↔ 477By similarity
Disulfide bondi464 ↔ 484By similarity
Disulfide bondi471 ↔ 503By similarity
Disulfide bondi496 ↔ 508By similarity
Disulfide bondi515 ↔ 565By similarity
Glycosylationi522N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi530 ↔ 573By similarity
Disulfide bondi543 ↔ 553By similarity
Disulfide bondi560 ↔ 599By similarity
Disulfide bondi593 ↔ 604By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
D5LMJ3

<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_section">'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_section">'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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
D5LMJ3

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

More...
SMRi
D5LMJ3

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_and_domains_section">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 – 398Peptidase M12BPROSITE-ProRule annotationAdd BLAST194
Domaini406 – 492DisintegrinPROSITE-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>Motifi470 – 472D/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 biasi493 – 607Cys-richAdd BLAST115

<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
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
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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

D5LMJ3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIQALLVIIC LAVFPHQGSS IILESGNVND YEVVYPQKVP ALLKGGVQNP
60 70 80 90 100
QPETKYEDTM RYEFQVNGEP VVLHLERNKG LFSEDYTETH YAPDGREITT
110 120 130 140 150
SPPVQDHCYY HGYIQNEADS SAVISACNGL KGHFKHQGET YFIEPLELSE
160 170 180 190 200
SEAHAIYKDE NVEKEDETPK ICAVTQTTWE SDESIEKTSQ LTNTPEQDRY
210 220 230 240 250
LQVKKYIEFY LVVDNKMYKN HTSNQELRTR VYEMVNYLNT KYRRLNFHIA
260 270 280 290 300
LIGLEIWSNQ DKVDMDPGAN VTLKSFAEWR AKLPPHKRND NAQLLTGIDF
310 320 330 340 350
NGTTVGLAYT GTLCTWGSVA VVQDYSRRTI LMASTMAHEL GHNMGIHHDK
360 370 380 390 400
ANCRCSHSPC IMSDTISDEP FYEFSSCSVR EHQEYLLRER PQCILNKPSR
410 420 430 440 450
KAIVSRPVCG NNFVEVGEQC DCGSLQDCQS TCCNATTCKL QPHAQCDSEE
460 470 480 490 500
CCEKCKFKGA ETECRAAKDD CDLPEFCTGQ SAECPTDSLQ RNGHPCQNNQ
510 520 530 540 550
GYCYNGKCPT MENQCITLLG PNYTVGPAGC FKNNRKGDDV SHCRKENGAK
560 570 580 590 600
IPCAAKDEKC GTLYCTEIKK TGCIVPVSPR DPDSRMVEPG TKCEDKKVCS

KSQCVKV
Length:607
Mass (Da):68,254
Last modified:June 15, 2010 - 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:i38E9A800C2FD7D65
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
GU944972 mRNA Translation: ADF43026.1

<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
GU944972 mRNA Translation: ADF43026.1

3D structure databases

ProteinModelPortaliD5LMJ3
SMRiD5LMJ3
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.159

Proteomic databases

PRIDEiD5LMJ3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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
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
PS50214 DISINTEGRIN_2, 1 hit
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiVM3A_NAJAT
<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: D5LMJ3
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: June 15, 2010
Last modified: May 23, 2018
This is version 36 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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