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Entry version 107 (05 Dec 2018)
Sequence version 2 (01 Nov 1999)
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Protein

Zinc metalloproteinase-disintegrin-like bothropasin

Gene
N/A
Organism
Bothrops jararaca (Jararaca) (Bothrops jajaraca)
Status
Reviewed-Annotation score:

Annotation score:5 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

Zinc metalloproteinase-disintegrin-like bothropasin: has caseinolytic activity. Causes hemorrhage on rabbit skin and causes myonecrosis in mouse tibialis anterior muscle.
Disintegrin-like bothropasin: inhibits platelet aggregation.

Miscellaneous

The metalloproteinase domain which is released from the cleavage of the disintegrin bothropasin may be unstable.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 in insulin B chain.1 Publication EC:3.4.24.49

<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+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by EDTA and EGTA.1 Publication

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 bindingi201Calcium 11 PublicationImported1
Metal bindingi285Calcium 11 PublicationImported1
Metal bindingi334Zinc; catalytic1 PublicationImported1
<p>This subsection of the ‘Function’ 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 sitei335PROSITE-ProRule annotation1
Metal bindingi338Zinc; catalytic1 PublicationImported1
Metal bindingi344Zinc; catalytic1 PublicationImported1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei378Necessary, but not sufficient, for proteolytic processingBy similarity1
Metal bindingi389Calcium 1; via carbonyl oxygen1 PublicationImported1
Metal bindingi392Calcium 11 PublicationImported1
Metal bindingi404Calcium 2; via carbonyl oxygen1 PublicationImported1
Metal bindingi407Calcium 21 PublicationImported1
Metal bindingi409Calcium 2; via carbonyl oxygen1 PublicationImported1
Metal bindingi411Calcium 21 PublicationImported1
Metal bindingi414Calcium 21 PublicationImported1
Metal bindingi417Calcium 21 PublicationImported1
Metal bindingi468Calcium 31 PublicationImported1
Metal bindingi469Calcium 3; via carbonyl oxygen1 PublicationImported1
Metal bindingi471Calcium 31 PublicationImported1
Metal bindingi483Calcium 31 PublicationImported1
Metal bindingi484Calcium 3; via carbonyl oxygen1 PublicationImported1

<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, Hemorrhagic toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Platelet aggregation inhibiting toxin, Protease, Toxin
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.49 911

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M12.140

<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 bothropasin1 Publication (EC:3.4.24.49)
Alternative name(s):
Snake venom metalloproteinase
Short name:
SVMP
Cleaved into the following chain:
<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>OrganismiBothrops jararaca (Jararaca) (Bothrops jajaraca)
<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 identifieri8724 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

<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; 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_000032641821 – 191By similarityAdd BLAST171
<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_0000326419192 – 610Zinc metalloproteinase-disintegrin-like bothropasin1 PublicationAdd BLAST419
ChainiPRO_0000326420399 – 610Disintegrin-like bothropasinBy similarityAdd BLAST212

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei192Pyrrolidone carboxylic acid1 Publication1
<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 bondi309 ↔ 389In zinc metalloproteinase-disintegrin-like bothropasin1 PublicationImported
Disulfide bondi349 ↔ 373In zinc metalloproteinase-disintegrin-like bothropasin1 PublicationImported
Disulfide bondi351 ↔ 356In zinc metalloproteinase-disintegrin-like bothropasin1 PublicationImported
<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>Glycosylationi372N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi405 ↔ 434In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 PublicationImported
Disulfide bondi405 ↔ 424In disintegrin-like bothropasin; alternateBy similarity
Disulfide bondi416 ↔ 434In disintegrin-like bothropasin; alternateBy similarity
Disulfide bondi416 ↔ 429In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 PublicationImported
Disulfide bondi418 ↔ 424In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 PublicationImported
Disulfide bondi428 ↔ 451In zinc metalloproteinase-disintegrin-like bothropasin1 PublicationImported
Disulfide bondi442 ↔ 448In zinc metalloproteinase-disintegrin-like bothropasin1 PublicationImported
Disulfide bondi447 ↔ 473In zinc metalloproteinase-disintegrin-like bothropasin1 PublicationImported
Disulfide bondi460 ↔ 480In both disintegrin-like bothropasin and zinc metalloproteinase-disintegrin-like bothropasinPROSITE-ProRule annotation1 PublicationImported
Disulfide bondi467 ↔ 499In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 PublicationImported
Disulfide bondi467 ↔ 492In disintegrin-like bothropasin; alternateBy similarity
Disulfide bondi492 ↔ 504In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 PublicationImported
Disulfide bondi499 ↔ 504In disintegrin-like bothropasinBy similarity
Disulfide bondi511 ↔ 561In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 PublicationImported
Disulfide bondi511 ↔ 526In disintegrin-like bothropasin; alternateBy similarity
Disulfide bondi526 ↔ 572In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 PublicationImported
Disulfide bondi539 ↔ 549In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 PublicationImported
Disulfide bondi549 ↔ 556In disintegrin-like bothropasin; alternateBy similarity
Disulfide bondi556 ↔ 598In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 PublicationImported
Disulfide bondi561 ↔ 572In disintegrin-like bothropasinBy similarity
Disulfide bondi592 ↔ 603In zinc metalloproteinase-disintegrin-like bothropasin; alternate1 PublicationImported
Disulfide bondi598 ↔ 603In disintegrin-like bothropasinBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid, Zymogen

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O93523

<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.2 Publications

<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

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DSLX-ray2.70A/B192-610[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
O93523

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

More...
SMRi
O93523

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O93523

<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>Domaini198 – 394Peptidase M12BPROSITE-ProRule annotationAdd BLAST197
Domaini402 – 488DisintegrinPROSITE-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>Motifi466 – 468D/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 biasi489 – 610Cys-richAdd BLAST122

<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

Phylogenomic databases

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG006978

KEGG Orthology (KO)

More...
KOi
K20745

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_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.

O93523-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIEVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK
60 70 80 90 100
YEDAMQYEFK VNGEPVVLHL EKNKGLFSKD YSETHYSPDG REITTYPAVE
110 120 130 140 150
DHCYYHGRIE NDADSTASIS ACNGLKGHFK LQRETYFIEP LKLSNSEAHA
160 170 180 190 200
VFKYENVEKE DEAPKMCGVT QNWKSYEPIK KASQLVVTAE QQKYNPFRYV
210 220 230 240 250
ELFIVVDQGM VTKNNGDLDK IKARMYELAN IVNEILRYLY MHAALVGLEI
260 270 280 290 300
WSNGDKITVK PDVDYTLNSF AEWRKTDLLT RKKHDNAQLL TAIDFNGPTI
310 320 330 340 350
GYAYIGSMCH PKRSVAIVED YSPINLVVAV IMAHEMGHNL GIHHDTDFCS
360 370 380 390 400
CGDYPCIMGP TISNEPSKFF SNCSYIQCWD FIMKENPQCI LNEPLGTDIV
410 420 430 440 450
SPPVCGNELL EVGEECDCGT PENCQNECCD AATCKLKSGS QCGHGDCCEQ
460 470 480 490 500
CKFSKSGTEC RASMSECDPA EHCTGQSSEC PADVFHKNGQ PCLDNYGYCY
510 520 530 540 550
NGNCPIMYHQ CYALFGADVY EAEDSCFKDN QKGNYYGYCR KENGKKIPCA
560 570 580 590 600
PEDVKCGRLY CKDNSPGQNN PCKMFYSNDD EHKGMVLPGT KCADGKVCSN
610
GHCVDVATAY
Length:610
Mass (Da):68,213
Last modified:November 1, 1999 - v2
<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:i014C8AE6B86F25DD
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
AF056025 mRNA Translation: AAC61986.2

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AAC61986

<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
AF056025 mRNA Translation: AAC61986.2

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DSLX-ray2.70A/B192-610[»]
ProteinModelPortaliO93523
SMRiO93523
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.140

PTM databases

iPTMnetiO93523

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC61986

Phylogenomic databases

HOVERGENiHBG006978
KOiK20745

Enzyme and pathway databases

BRENDAi3.4.24.49 911

Miscellaneous databases

EvolutionaryTraceiO93523

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...

<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 nameiVM3BP_BOTJA
<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: O93523
<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: March 18, 2008
Last sequence update: November 1, 1999
Last modified: December 5, 2018
This is version 107 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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