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Entry version 187 (13 Feb 2019)
Sequence version 3 (27 Jul 2011)
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Protein

Disintegrin and metalloproteinase domain-containing protein 17

Gene

Adam17

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

Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Plays a role in the proteolytic processing of ACE2 (By similarity). Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein (PubMed:10799547, PubMed:11108241). Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called notch extracellular truncation (NEXT) (PubMed:10882063). Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain (PubMed:12907434).By similarity4 Publications

<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

  • Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNF-alpha). Similarly cleaves other membrane-anchored, cell-surface proteins to 'shed' the extracellular domains.By similarity EC:3.4.24.86

<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

<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 metalloproteinase inhibitor 3 (TIMP-3), but not by TIMP-1, TIMP-2 and TIMP-4.1 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 bindingi184Zinc; in inhibited formBy similarity1
Metal bindingi405Zinc; catalyticBy similarity1
<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 sitei406PROSITE-ProRule annotation1
Metal bindingi409Zinc; catalyticBy similarity1
Metal bindingi415Zinc; catalyticBy 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

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 processNotch signaling pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-193692 Regulated proteolysis of p75NTR
R-MMU-75893 TNF signaling

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M12.217

<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 17 (EC:3.4.24.86By similarity)
Short name:
ADAM 17
Alternative name(s):
TNF-alpha convertase
TNF-alpha-converting enzyme
CD_antigen: CD156b
<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:Adam17
Synonyms:Tace
<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 12

Organism-specific databases

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

More...
MGIi
MGI:1096335 Adam17

<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

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 domaini215 – 671ExtracellularSequence analysisAdd BLAST457
<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>Transmembranei672 – 692HelicalSequence analysisAdd BLAST21
Topological domaini693 – 827CytoplasmicSequence analysisAdd BLAST135

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4379

<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 – 17By similarityAdd 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_000002909018 – 214By similarityAdd BLAST197
<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_0000029091215 – 827Disintegrin and metalloproteinase domain-containing protein 17Add BLAST613

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>Glycosylationi157N-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 bondi225 ↔ 333By similarity
Glycosylationi264N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi365 ↔ 469By similarity
Disulfide bondi423 ↔ 453By similarity
Glycosylationi452N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi498N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi534 ↔ 555By similarity
Glycosylationi539N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi551N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi573 ↔ 582By similarity
Disulfide bondi578 ↔ 591By similarity
Disulfide bondi593 ↔ 600By similarity
Glycosylationi606N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei735PhosphothreonineCombined sources1
Modified residuei764PhosphothreonineBy similarity1
Modified residuei770PhosphoserineBy similarity1
Modified residuei794PhosphoserineCombined sources1
Modified residuei822PhosphoserineBy 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.By similarity
Phosphorylated. Stimulation by growth factor or phorbol 12-myristate 13-acetate induces phosphorylation of Ser-822 but decreases phosphorylation of Ser-794. Phosphorylation at THR-735 by MAPK14 is required for ADAM17-mediated ectodomain shedding (By similarity).By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9Z0F8

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9Z0F8

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

More...
PaxDbi
Q9Z0F8

PeptideAtlas

More...
PeptideAtlasi
Q9Z0F8

PRoteomics IDEntifications database

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PRIDEi
Q9Z0F8

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9Z0F8

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

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PhosphoSitePlusi
Q9Z0F8

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q9Z0F8

<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

Ubiquitously expressed. Expressed at highest levels in heart, liver, skeletal muscle, kidney and testes. Expressed at lower levels in brain, spleen and lung.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000052593 Expressed in 248 organ(s), highest expression level in saccule of membranous labyrinth

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9Z0F8 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9Z0F8 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 with MAD2L1, MAPK14 and MUC1.By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Rhbdf2Q80WQ66EBI-7848498,EBI-647271

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
197964, 1 interactor

Database of interacting proteins

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DIPi
DIP-41747N

Protein interaction database and analysis system

More...
IntActi
Q9Z0F8, 3 interactors

Molecular INTeraction database

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MINTi
Q9Z0F8

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000067953

<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
Q9Z0F8

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

More...
SMRi
Q9Z0F8

Database of comparative protein structure models

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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>Domaini223 – 474Peptidase M12BPROSITE-ProRule annotationAdd BLAST252
Domaini475 – 563DisintegrinPROSITE-ProRule annotationAdd BLAST89

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni603 – 671Crambin-likeAdd BLAST69

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>Motifi182 – 189Cysteine switchBy similarity8
Motifi731 – 738SH3-bindingSequence analysis8

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 biasi96 – 99Poly-Val4
Compositional biasi564 – 602Cys-richAdd BLAST39

<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

Must be membrane anchored to cleave the different substrates. The cytoplasmic domain is not required for the this activity. Only the catalytic domain is essential to shed TNF and p75 TNFR.
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

SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3658 Eukaryota
ENOG410XQWB LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155443

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000033797

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG050457

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9Z0F8

KEGG Orthology (KO)

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KOi
K06059

Identification of Orthologs from Complete Genome Data

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OMAi
VCSDKNS

Database of Orthologous Groups

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OrthoDBi
162519at2759

TreeFam database of animal gene trees

More...
TreeFami
TF314733

Family and domain databases

Conserved Domains Database

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CDDi
cd14246 ADAM17_MPD, 1 hit
cd04270 ZnMc_TACE_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
IPR034025 ADAM10_ADAM17
IPR032029 ADAM17_MPD
IPR001762 Disintegrin_dom
IPR036436 Disintegrin_dom_sf
IPR024079 MetalloPept_cat_dom_sf
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16698 ADAM17_MPD, 1 hit
PF00200 Disintegrin, 1 hit
PF01562 Pep_M12B_propep, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
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>Sequences (2+)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 2 <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

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform Long (identifier: Q9Z0F8-1) [UniParc]FASTAAdd to basket

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
MRRRLLILTT LVPFVLAPRP PEEAGSGSHP RLEKLDSLLS DYDILSLANI
60 70 80 90 100
QQHSIRKRDL QSATHLETLL TFSALKRHFK LYLTSSTERF SQNLRVVVVD
110 120 130 140 150
GKEESEYSVK WQNFFSGHVV GEPDSRVLAH IGDDDVTVRI NTDGAEYNVE
160 170 180 190 200
PLWRFVNDTK DKRMLVYKSE DIKDFSRLQS PKVCGYLNAD SEELLPKGLI
210 220 230 240 250
DREPSEEFVR RVKRRAEPNP LKNTCKLLVV ADHRFYKYMG RGEESTTTNY
260 270 280 290 300
LIELIDRVDD IYRNTSWDNA GFKGYGVQIE QIRILKSPQE VKPGERHFNM
310 320 330 340 350
AKSFPNEEKD AWDVKMLLEQ FSFDIAEEAS KVCLAHLFTY QDFDMGTLGL
360 370 380 390 400
AYVGSPRANS HGGVCPKAYY NPTVKKNIYL NSGLTSTKNY GKTILTKEAD
410 420 430 440 450
LVTTHELGHN FGAEHDPDGL AECAPNEDQG GKYVMYPIAV SGDHENNKMF
460 470 480 490 500
SNCSKQSIYK TIESKAQECF QERSNKVCGN SRVDEGEECD PGIMYLNNDT
510 520 530 540 550
CCNSDCTLKP GVQCSDRNSP CCKNCQFETA QKKCQEAINA TCKGVSYCTG
560 570 580 590 600
NSSECPPPGD AEDDTVCLDL GKCKAGKCIP FCKREQELES CACVDTDNSC
610 620 630 640 650
KVCCRNLSGP CVPYVDAEQK NLFLRKGKPC TVGFCDMNGK CEKRVQDVIE
660 670 680 690 700
RFWDFIDQLS INTFGKFLAD NIVGSVLVFS LIFWIPFSIL VHCVDKKLDK
710 720 730 740 750
QYESLSLFHH SNIEMLSSMD SASVRIIKPF PAPQTPGRLQ ALQPAAMMPP
760 770 780 790 800
VPAAPKLDHQ RMDTIQEDPS TDSHADDDGF EKDPFPNSST AAKSFEDLTD
810 820
HPVTRSEKAA SFKLQRQSRV DSKETEC
Length:827
Mass (Da):93,056
Last modified:July 27, 2011 - v3
<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:i6B434F80878197F5
GO
Isoform Short (identifier: Q9Z0F8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     639-655: GKCEKRVQDVIERFWDF → CDFFSPYRANVRNEYRT
     656-827: Missing.

Show »
Length:655
Mass (Da):73,884
Checksum:i9F4B11FD8D99DDF8
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PXU2E9PXU2_MOUSE
Disintegrin and metalloproteinase d...
Adam17
846Annotation score:

Annotation score:2 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>
J3QMF2J3QMF2_MOUSE
A disintegrin and metallopeptidase ...
Adam17 mCG_8913
94Annotation score:

Annotation score:1 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>
J3QNB3J3QNB3_MOUSE
Disintegrin and metalloproteinase d...
Adam17
222Annotation score:

Annotation score:1 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>
A0A338P6I8A0A338P6I8_MOUSE
Disintegrin and metalloproteinase d...
Adam17
123Annotation score:

Annotation score:1 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>
A0A338P6F3A0A338P6F3_MOUSE
Disintegrin and metalloproteinase d...
Adam17
38Annotation score:

Annotation score:1 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 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 conflicti3 – 4RR → QS in CAA07480 (PubMed:9755855).Curated2
Sequence conflicti7I → F in CAA07480 (PubMed:9755855).Curated1
Sequence conflicti28S → A in CAA07480 (PubMed:9755855).Curated1
Sequence conflicti28S → A in BAA78578 (PubMed:10375622).Curated1
Sequence conflicti113N → D in AAC62934 (PubMed:10433800).Curated1
Sequence conflicti113N → D in CAA07480 (PubMed:9755855).Curated1
Sequence conflicti113N → D in BAA78578 (PubMed:10375622).Curated1
Sequence conflicti113N → D in AAD09627 (Ref. 4) Curated1
Sequence conflicti113N → D in AAD09628 (Ref. 4) Curated1
Sequence conflicti149V → I in CAA07480 (PubMed:9755855).Curated1
Sequence conflicti149V → I in BAA78578 (PubMed:10375622).Curated1
Sequence conflicti594V → I in AAC62934 (PubMed:10433800).Curated1
Sequence conflicti594V → I in AAD09627 (Ref. 4) Curated1
Sequence conflicti594V → I in AAD09628 (Ref. 4) Curated1
Sequence conflicti752P → S in CAA07480 (PubMed:9755855).Curated1
Sequence conflicti752P → S in BAA78578 (PubMed:10375622).Curated1
Sequence conflicti775A → V in CAA07480 (PubMed:9755855).Curated1
Sequence conflicti775A → V in BAA78578 (PubMed:10375622).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_005479639 – 655GKCEK…RFWDF → CDFFSPYRANVRNEYRT in isoform Short. 1 PublicationAdd BLAST17
Alternative sequenceiVSP_005480656 – 827Missing in isoform Short. 1 PublicationAdd BLAST172

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF056359
, AF056345, AF056346, AF056347, AF056348, AF056349, AF056350, AF056351, AF056352, AF056353, AF056354, AF056355, AF056356, AF056357, AF056358 Genomic DNA Translation: AAC62934.1
AJ007365 mRNA Translation: CAA07480.1
AB021709 mRNA Translation: BAA78578.1
U69613 mRNA Translation: AAD09627.1
U69614 mRNA Translation: AAD09628.1
AK139471 mRNA Translation: BAE24023.1
BC094655 mRNA Translation: AAH94655.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS25836.1 [Q9Z0F8-1]

NCBI Reference Sequences

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RefSeqi
NP_001264195.1, NM_001277266.1
NP_001278800.1, NM_001291871.1
NP_033745.4, NM_009615.6 [Q9Z0F8-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.27681

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000064536; ENSMUSP00000067953; ENSMUSG00000052593 [Q9Z0F8-1]
ENSMUST00000145118; ENSMUSP00000136407; ENSMUSG00000052593 [Q9Z0F8-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
11491

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:11491

UCSC genome browser

More...
UCSCi
uc007ndu.2 mouse [Q9Z0F8-1]

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
AF056359
, AF056345, AF056346, AF056347, AF056348, AF056349, AF056350, AF056351, AF056352, AF056353, AF056354, AF056355, AF056356, AF056357, AF056358 Genomic DNA Translation: AAC62934.1
AJ007365 mRNA Translation: CAA07480.1
AB021709 mRNA Translation: BAA78578.1
U69613 mRNA Translation: AAD09627.1
U69614 mRNA Translation: AAD09628.1
AK139471 mRNA Translation: BAE24023.1
BC094655 mRNA Translation: AAH94655.1
CCDSiCCDS25836.1 [Q9Z0F8-1]
RefSeqiNP_001264195.1, NM_001277266.1
NP_001278800.1, NM_001291871.1
NP_033745.4, NM_009615.6 [Q9Z0F8-1]
UniGeneiMm.27681

3D structure databases

ProteinModelPortaliQ9Z0F8
SMRiQ9Z0F8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197964, 1 interactor
DIPiDIP-41747N
IntActiQ9Z0F8, 3 interactors
MINTiQ9Z0F8
STRINGi10090.ENSMUSP00000067953

Chemistry databases

ChEMBLiCHEMBL4379

Protein family/group databases

MEROPSiM12.217

PTM databases

iPTMnetiQ9Z0F8
PhosphoSitePlusiQ9Z0F8
SwissPalmiQ9Z0F8

Proteomic databases

EPDiQ9Z0F8
jPOSTiQ9Z0F8
PaxDbiQ9Z0F8
PeptideAtlasiQ9Z0F8
PRIDEiQ9Z0F8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064536; ENSMUSP00000067953; ENSMUSG00000052593 [Q9Z0F8-1]
ENSMUST00000145118; ENSMUSP00000136407; ENSMUSG00000052593 [Q9Z0F8-2]
GeneIDi11491
KEGGimmu:11491
UCSCiuc007ndu.2 mouse [Q9Z0F8-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6868
MGIiMGI:1096335 Adam17

Phylogenomic databases

eggNOGiKOG3658 Eukaryota
ENOG410XQWB LUCA
GeneTreeiENSGT00940000155443
HOGENOMiHOG000033797
HOVERGENiHBG050457
InParanoidiQ9Z0F8
KOiK06059
OMAiVCSDKNS
OrthoDBi162519at2759
TreeFamiTF314733

Enzyme and pathway databases

ReactomeiR-MMU-193692 Regulated proteolysis of p75NTR
R-MMU-75893 TNF signaling

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9Z0F8

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000052593 Expressed in 248 organ(s), highest expression level in saccule of membranous labyrinth
ExpressionAtlasiQ9Z0F8 baseline and differential
GenevisibleiQ9Z0F8 MM

Family and domain databases

CDDicd14246 ADAM17_MPD, 1 hit
cd04270 ZnMc_TACE_like, 1 hit
Gene3Di3.40.390.10, 1 hit
4.10.70.10, 1 hit
InterProiView protein in InterPro
IPR034025 ADAM10_ADAM17
IPR032029 ADAM17_MPD
IPR001762 Disintegrin_dom
IPR036436 Disintegrin_dom_sf
IPR024079 MetalloPept_cat_dom_sf
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
PfamiView protein in Pfam
PF16698 ADAM17_MPD, 1 hit
PF00200 Disintegrin, 1 hit
PF01562 Pep_M12B_propep, 1 hit
SMARTiView protein in SMART
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 nameiADA17_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: Q9Z0F8
Secondary accession number(s): O88726
, Q505A7, Q9R1U4, Q9Z0K3
<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 20, 2001
Last sequence update: July 27, 2011
Last modified: February 13, 2019
This is version 187 of the entry and version 3 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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