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Entry version 192 (13 Feb 2019)
Sequence version 2 (14 Nov 2003)
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Protein

Disintegrin and metalloproteinase domain-containing protein 15

Gene

Adam15

Organism
Mus musculus (Mouse)
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

Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration (By similarity). Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. Interactions with egg membrane could be mediated via binding between the disintegrin-like domain to one or more integrin receptors on the egg.By similarity4 Publications

Miscellaneous

Mice targeted for deletion of the first 27 amino acids of the ADAM15 N-terminal sequence are viable and fertile, showing no major developmental defects and displaying normal mortality or morbidity. These mutant mice, however, exhibit significantly reduced ischemia-induced retinal neovascularization, choroidal neovascularization at rupture sites in Bruch's membrane, and VEGF-induced subretinal neovascularization, and develop significantly smaller tumors following implantation of B16F0 melanoma cells. Aging mutant mice exhibit accelerated development of osteoarthritic lesions in knee joints.

<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+CuratedNote: Binds 1 zinc ion per subunit.Curated

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 bindingi179Zinc; in inhibited formBy similarity1
Metal bindingi349Zinc; catalyticSequence analysis1
<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 sitei350PROSITE-ProRule annotation1
Metal bindingi353Zinc; catalyticSequence analysis1
Metal bindingi359Zinc; catalyticSequence analysis1

<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

GO - Biological processi

<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 functionHydrolase, Metalloprotease, Protease
Biological processAngiogenesis, Cell adhesion, Collagen degradation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1474228 Degradation of the extracellular matrix
R-MMU-8941237 Invadopodia formation

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M12.215

<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:
Disintegrin and metalloproteinase domain-containing protein 15 (EC:3.4.24.-)
Short name:
ADAM 15
Alternative name(s):
AD56
Metalloprotease RGD disintegrin protein
Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15
Short name:
MDC-15
Metargidin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Adam15
Synonyms:Mdc15
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1333882 Adam15

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini208 – 696ExtracellularSequence analysisAdd BLAST489
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei697 – 717HelicalSequence analysisAdd BLAST21
Topological domaini718 – 864CytoplasmicSequence analysisAdd BLAST147

Keywords - Cellular componenti

Cell junction, Cell projection, Cilium, Cytoplasmic vesicle, Flagellum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi482R → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication1
Mutagenesisi489D → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication1
Mutagenesisi490L → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication1
Mutagenesisi491P → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication1
Mutagenesisi492E → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication1
Mutagenesisi493F → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication1

<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 – 17Sequence analysisAdd BLAST17
<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_000002908418 – 207CuratedAdd BLAST190
<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_0000029085208 – 864Disintegrin and metalloproteinase domain-containing protein 15Add BLAST657

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>Glycosylationi238N-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 bondi324 ↔ 410By similarity
Disulfide bondi366 ↔ 394By similarity
Disulfide bondi368 ↔ 377By similarity
Glycosylationi390N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi393N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi481 ↔ 501By similarity
Glycosylationi607N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi612N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi658 ↔ 668By similarity
Disulfide bondi662 ↔ 674By similarity
Disulfide bondi676 ↔ 685By similarity
<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 residuei716Phosphotyrosine; by HCK and LCKBy similarity1
Modified residuei736Phosphotyrosine; by HCK and LCKBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The precursor is cleaved by a furin endopeptidase. An additional membrane proximal site of cleavage affects a small percentage of the proteins and results in disulfide-linked fragments. The prodomain is apparently cleaved in several positions that are N-terminal of the furin cleavage site.1 Publication
May be partially sialylated.
Phosphorylation increases association with PTKs.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei289 – 290Cleavage; by furinSequence analysis2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O88839

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
O88839

PeptideAtlas

More...
PeptideAtlasi
O88839

PRoteomics IDEntifications database

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PRIDEi
O88839

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O88839

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O88839

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O88839

<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 moderately in pericytes of retina. Expressed in testis and in spermatozoa from the caput, corpus, and cauda epididymis, as well as in non-capacitated and acrosome-reacted sperm (at protein level). Highly expressed in heart, brain, lung, and kidney. Expressed at lower levels in spleen, liver, testis and muscle.2 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

At 13.5 dpc, strongly expressed in the developing vasculature of the endocardium. At P17, expressed throughout the retina (at protein level). At 9.5 dpc and thereafter, prominently expressed in the vasculature, including in ventral and dorsal aorta and the caudal artery. In developing heart, detected in endocardium and blood vessels of the ventricle, bulbus arteriosus, and atrium. Also highly expressed in hypertrophic cells of the developing bone. In adult, expressed prominently in brain, including in hippocampus, cerebellum, pons, thalamus, cortex, and olfactory bulb.2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By hypoxic stimulus in retina (at protein level). Up-regulated by VEGF in retina.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000028041 Expressed in 240 organ(s), highest expression level in bone marrow macrophage

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O88839 MM

<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

Interacts specifically with Src family protein-tyrosine kinases (PTKs) (By similarity). Interacts with ITAGV-ITGB3 (vitronectin receptor). Interacts with SH3GL2 and SNX9; this interaction occurs preferentially with ADAM15 precursor, rather than the processed form, suggesting it occurs in a secretory pathway compartment prior to the medial Golgi. Interacts with ITAG9-ITGB1. Interacts with SH3PXD2A (By similarity). Interacts with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN, MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
O88839, 3 interactors

Molecular INTeraction database

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MINTi
O88839

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000029676

<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

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ProteinModelPortali
O88839

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

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SMRi
O88839

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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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>Domaini214 – 415Peptidase M12BPROSITE-ProRule annotationAdd BLAST202
Domaini422 – 509DisintegrinPROSITE-ProRule annotationAdd BLAST88
Domaini658 – 686EGF-likePROSITE-ProRule annotationAdd BLAST29

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>Motifi177 – 184Cysteine switchBy similarity8
Motifi816 – 822SH3-bindingSequence analysis7
Motifi851 – 857SH3-bindingSequence analysis7

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 biasi510 – 657Cys-richAdd BLAST148
Compositional biasi699 – 712Poly-LeuAdd BLAST14

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The cytoplasmic domain is required for SH3GL2- and SNX9-binding.
Disintegrin domain binds to integrin alphaV-beta3.By similarity
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Keywords - Domaini

EGF-like domain, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3607 Eukaryota
ENOG410XX2M LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159822

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG006978

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O88839

KEGG Orthology (KO)

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KOi
K06836

Identification of Orthologs from Complete Genome Data

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OMAi
ADHQEFL

Database of Orthologous Groups

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OrthoDBi
162519at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O88839

TreeFam database of animal gene trees

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TreeFami
TF314733

Family and domain databases

Conserved Domains Database

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CDDi
cd04269 ZnMc_adamalysin_II_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.390.10, 1 hit
4.10.70.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR033605 ADAM15
IPR006586 ADAM_Cys-rich
IPR001762 Disintegrin_dom
IPR036436 Disintegrin_dom_sf
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR024079 MetalloPept_cat_dom_sf
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
IPR034027 Reprolysin_adamalysin

The PANTHER Classification System

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PANTHERi
PTHR11905:SF130 PTHR11905:SF130, 1 hit

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF57552 SSF57552, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50214 DISINTEGRIN_2, 1 hit
PS01186 EGF_2, 1 hit
PS50026 EGF_3, 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>Sequences (4)i

<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.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: O88839-1) [UniParc]FASTAAdd to basket
Also known as: ADAM15v2

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MRLALLWALG LLGAGSPRPS PPLPNIGGTE EEQQASPERT LSGSMESRVV
60 70 80 90 100
QDSPPMSLAD VLQTGLPEAL RISLELDSES HVLELLQNRD LIPGRPTLVW
110 120 130 140 150
YQPDGTRMVS EGYSLENCCY RGRVQGHPSS WVSLCACSGI RGLIVLSPER
160 170 180 190 200
GYTLELGPGD LQRPVISRIQ DHLLLGHTCA PSWHASVPTR AGPDLLLEQH
210 220 230 240 250
HAHRLKRDVV TETKIVELVI VADNSEVRKY PDFQQLLNRT LEAALLLDTF
260 270 280 290 300
FQPLNVRVAL VGLEAWTQHN LIEMSSNPAV LLDNFLRWRR TDLLPRLPHD
310 320 330 340 350
SAQLVTVTSF SGPMVGMAIQ NSICSPDFSG GVNMDHSTSI LGVASSIAHE
360 370 380 390 400
LGHSLGLDHD SPGHSCPCPG PAPAKSCIME ASTDFLPGLN FSNCSRQALE
410 420 430 440 450
KALLEGMGSC LFERQPSLAP MSSLCGNMFV DPGEQCDCGF PDECTDPCCD
460 470 480 490 500
HFTCQLRPGA QCASDGPCCQ NCKLHPAGWL CRPPTDDCDL PEFCPGDSSQ
510 520 530 540 550
CPSDIRLGDG EPCASGEAVC MHGRCASYAR QCQSLWGPGA QPAAPLCLQT
560 570 580 590 600
ANTRGNAFGS CGRSPGGSYM PCAPRDVMCG QLQCQWGRSQ PLLGSVQDRL
610 620 630 640 650
SEVLEANGTQ LNCSWVDLDL GNDVAQPLLA LPGTACGPGL VCIGHRCQPV
660 670 680 690 700
DLLGAQECRR KCHGHGVCDS SGHCRCEEGW APPDCMTQLK ATSSLTTGLL
710 720 730 740 750
LSLLLLLVLV LLGASYWHRA RLHQRLCQLK GSSCQYRAPQ SCPPERPGPP
760 770 780 790 800
QRAQQMTGTK QASVVSFPVP PSRPLPPNPV PKKLQAALAD RSNPPTRPLP
810 820 830 840 850
ADPVVRRPKS QGPTKPPPPR KPLPANPQGQ HPPGDLPGPG DGSLPLVVPS
860
RPAPPPPAAS SLYL
Length:864
Mass (Da):92,664
Last modified:November 14, 2003 - 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:iB1CBEB923463BB15
GO
Isoform 2 (identifier: O88839-2) [UniParc]FASTAAdd to basket
Also known as: ADAM15v1

The sequence of this isoform differs from the canonical sequence as follows:
     761-785: Missing.

Show »
Length:839
Mass (Da):90,002
Checksum:i0C61FAA9B79B8123
GO
Isoform 3 (identifier: O88839-3) [UniParc]FASTAAdd to basket
Also known as: ADAM15

The sequence of this isoform differs from the canonical sequence as follows:
     761-809: Missing.

Show »
Length:815
Mass (Da):87,425
Checksum:iC064BD3B7347D19B
GO
Isoform 4 (identifier: O88839-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     415-830: Missing.

Note: No experimental confirmation available.
Show »
Length:448
Mass (Da):48,417
Checksum:i37FEB93BD3704400
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti21 – 22PP → RR in BAA88903 (PubMed:13679040).Curated2
Sequence conflicti51Q → H in BAE29090 (PubMed:16141072).Curated1
Sequence conflicti73S → P in BAE41564 (PubMed:16141072).Curated1
Sequence conflicti443E → Q in BAA88903 (PubMed:13679040).Curated1
Sequence conflicti459G → E in BAA88903 (PubMed:13679040).Curated1
Sequence conflicti564 – 565SP → T in BAA88903 (PubMed:13679040).Curated2
Sequence conflicti654G → E in BAA88903 (PubMed:13679040).Curated1
Sequence conflicti660R → S in BAA88903 (PubMed:13679040).Curated1
Sequence conflicti703L → R in BAA88903 (PubMed:13679040).Curated1
Sequence conflicti712L → R in BAA88903 (PubMed:13679040).Curated1
Sequence conflicti729L → R in BAA88903 (PubMed:13679040).Curated1
Sequence conflicti830Q → R in BAE41564 (PubMed:16141072).Curated1
Sequence conflicti846L → S in BAA88903 (PubMed:13679040).Curated1
Sequence conflicti852 – 854PAP → AAS in BAA88903 (PubMed:13679040).Curated3
Sequence conflicti859A → P in BAA88903 (PubMed:13679040).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_008879415 – 830Missing in isoform 4. 1 PublicationAdd BLAST416
Alternative sequenceiVSP_008881761 – 809Missing in isoform 3. 2 PublicationsAdd BLAST49
Alternative sequenceiVSP_008880761 – 785Missing in isoform 2. CuratedAdd BLAST25

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
AF006196 mRNA Translation: AAC61896.1
AB022089 Genomic DNA Translation: BAA88903.1
AK048901 mRNA Translation: BAC33485.1
AK149796 mRNA Translation: BAE29090.1
AK151804 mRNA Translation: BAE30703.1
AK152725 mRNA Translation: BAE31447.1
AK170101 mRNA Translation: BAE41564.1
BC009132 mRNA Translation: AAH09132.1
EF506571 mRNA Translation: ABP73662.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS17502.1 [O88839-1]
CCDS17503.1 [O88839-3]

NCBI Reference Sequences

More...
RefSeqi
NP_001032811.2, NM_001037722.3 [O88839-1]
NP_033744.1, NM_009614.3 [O88839-3]
XP_006500981.1, XM_006500918.1 [O88839-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.274049
Mm.470104

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000029676; ENSMUSP00000029676; ENSMUSG00000028041 [O88839-1]
ENSMUST00000074582; ENSMUSP00000074167; ENSMUSG00000028041 [O88839-3]
ENSMUST00000107446; ENSMUSP00000103070; ENSMUSG00000028041 [O88839-4]
ENSMUST00000107448; ENSMUSP00000103072; ENSMUSG00000028041 [O88839-2]
ENSMUST00000184651; ENSMUSP00000139147; ENSMUSG00000028041 [O88839-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
11490

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:11490

UCSC genome browser

More...
UCSCi
uc008pyv.1 mouse [O88839-1]
uc008pyw.1 mouse [O88839-3]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF006196 mRNA Translation: AAC61896.1
AB022089 Genomic DNA Translation: BAA88903.1
AK048901 mRNA Translation: BAC33485.1
AK149796 mRNA Translation: BAE29090.1
AK151804 mRNA Translation: BAE30703.1
AK152725 mRNA Translation: BAE31447.1
AK170101 mRNA Translation: BAE41564.1
BC009132 mRNA Translation: AAH09132.1
EF506571 mRNA Translation: ABP73662.1
CCDSiCCDS17502.1 [O88839-1]
CCDS17503.1 [O88839-3]
RefSeqiNP_001032811.2, NM_001037722.3 [O88839-1]
NP_033744.1, NM_009614.3 [O88839-3]
XP_006500981.1, XM_006500918.1 [O88839-2]
UniGeneiMm.274049
Mm.470104

3D structure databases

ProteinModelPortaliO88839
SMRiO88839
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO88839, 3 interactors
MINTiO88839
STRINGi10090.ENSMUSP00000029676

Protein family/group databases

MEROPSiM12.215

PTM databases

iPTMnetiO88839
PhosphoSitePlusiO88839
SwissPalmiO88839

Proteomic databases

MaxQBiO88839
PaxDbiO88839
PeptideAtlasiO88839
PRIDEiO88839

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029676; ENSMUSP00000029676; ENSMUSG00000028041 [O88839-1]
ENSMUST00000074582; ENSMUSP00000074167; ENSMUSG00000028041 [O88839-3]
ENSMUST00000107446; ENSMUSP00000103070; ENSMUSG00000028041 [O88839-4]
ENSMUST00000107448; ENSMUSP00000103072; ENSMUSG00000028041 [O88839-2]
ENSMUST00000184651; ENSMUSP00000139147; ENSMUSG00000028041 [O88839-1]
GeneIDi11490
KEGGimmu:11490
UCSCiuc008pyv.1 mouse [O88839-1]
uc008pyw.1 mouse [O88839-3]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8751
MGIiMGI:1333882 Adam15

Phylogenomic databases

eggNOGiKOG3607 Eukaryota
ENOG410XX2M LUCA
GeneTreeiENSGT00940000159822
HOVERGENiHBG006978
InParanoidiO88839
KOiK06836
OMAiADHQEFL
OrthoDBi162519at2759
PhylomeDBiO88839
TreeFamiTF314733

Enzyme and pathway databases

ReactomeiR-MMU-1474228 Degradation of the extracellular matrix
R-MMU-8941237 Invadopodia formation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O88839

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028041 Expressed in 240 organ(s), highest expression level in bone marrow macrophage
GenevisibleiO88839 MM

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
IPR033605 ADAM15
IPR006586 ADAM_Cys-rich
IPR001762 Disintegrin_dom
IPR036436 Disintegrin_dom_sf
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR024079 MetalloPept_cat_dom_sf
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
IPR034027 Reprolysin_adamalysin
PANTHERiPTHR11905:SF130 PTHR11905:SF130, 1 hit
PfamiView protein in Pfam
PF08516 ADAM_CR, 1 hit
PF00200 Disintegrin, 1 hit
PF01562 Pep_M12B_propep, 1 hit
PF01421 Reprolysin, 1 hit
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
PS01186 EGF_2, 1 hit
PS50026 EGF_3, 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 nameiADA15_MOUSE
<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: O88839
Secondary accession number(s): A4ZYV2
, Q3TDN7, Q3U7C2, Q3UE21, Q8C7Z0, Q91VS9, Q9QYL2
<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 1, 2001
Last sequence update: November 14, 2003
Last modified: February 13, 2019
This is version 192 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

<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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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