O35674 · ADA19_MOUSE
- ProteinDisintegrin and metalloproteinase domain-containing protein 19
- GeneAdam19
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids920 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Participates in the proteolytic processing of beta-type neuregulin isoforms which are involved in neurogenesis and synaptogenesis, suggesting a regulatory role in glial cell. Also cleaves alpha-2 macroglobulin. May be involved in osteoblast differentiation and/or osteoblast activity in bone (By similarity).
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 133 | Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 346 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 347 | |||||
Sequence: E | ||||||
Binding site | 350 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 356 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | Golgi apparatus | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | SH3 domain binding | |
Biological Process | heart development | |
Biological Process | membrane protein ectodomain proteolysis | |
Biological Process | placenta development | |
Biological Process | positive regulation of cell-cell adhesion mediated by cadherin | |
Biological Process | positive regulation of gene expression |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDisintegrin and metalloproteinase domain-containing protein 19
- EC number
- Short namesADAM 19
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO35674
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 27-703 | Extracellular | ||||
Sequence: EPGWTTRGSQEGSPPLQHELIIPQWRTSESPGRGKHPLRAELRVMAEGRELILDLEKNEHLFAPAYTETCYTASGNPQTSTLKSEDHCFYHGTVRDVDESSVTLSTCRGIRGLIIVRSNLSYIIEPVPNSDSQHRIYRSEHLTLPPGNCGFEHSGPTSKDWALQFTHQTKKQPRRMKREDLHSMKYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRKLLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHCCSASAADGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCLSNMPDTRTLYGGRRCGNGYLEDGEECDCGEEEECKNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTNYYQMDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKGLNGQYRKCSPRDAKCGKIQCQSTQARPLESNAVSIDTTITLNGRRIHCRGTHVYRGPEEEEGEGDMLDPGLVMTGTKCGHNHICFEGQCRNTSFFETEGCGKKCNGHGVCNNNKNCHCFPGWSPPFCNTPGDGGSVDSGPLPPKS | ||||||
Transmembrane | 704-724 | Helical | ||||
Sequence: VGPVIAGVFSALFVLAVLVLL | ||||||
Topological domain | 725-920 | Cytoplasmic | ||||
Sequence: CHCYRQSHKLGKPSALPFKLRHQFSCPFRVSQSGGTGHANPTFKLQTPQGKRKVTNTPESLRKPSHPPPRPPPDYLRVESPPAPLPAHLNRAAGSSPEAGARIERKESARRPPPSRPMPPAPNCLLSQDFSRPRPPQKALPANPVPGQRTGPRSGGTSLLQPPTSGPQPPRPPAVPVPKLPEYRSQRVGAIISSKI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, propeptide, glycosylation, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MPGRAGVARFCLLALALQLHWPLAAC | ||||||
Propeptide | PRO_0000029104 | 27-204 | ||||
Sequence: EPGWTTRGSQEGSPPLQHELIIPQWRTSESPGRGKHPLRAELRVMAEGRELILDLEKNEHLFAPAYTETCYTASGNPQTSTLKSEDHCFYHGTVRDVDESSVTLSTCRGIRGLIIVRSNLSYIIEPVPNSDSQHRIYRSEHLTLPPGNCGFEHSGPTSKDWALQFTHQTKKQPRRMKR | ||||||
Glycosylation | 145 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000029105 | 205-920 | Disintegrin and metalloproteinase domain-containing protein 19 | |||
Sequence: EDLHSMKYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRKLLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHCCSASAADGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCLSNMPDTRTLYGGRRCGNGYLEDGEECDCGEEEECKNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTNYYQMDGTPCEGGQAYCYNGMCLTYQEQCQQLWGPGARPALDLCFERVNAAGDTYGNCGKGLNGQYRKCSPRDAKCGKIQCQSTQARPLESNAVSIDTTITLNGRRIHCRGTHVYRGPEEEEGEGDMLDPGLVMTGTKCGHNHICFEGQCRNTSFFETEGCGKKCNGHGVCNNNKNCHCFPGWSPPFCNTPGDGGSVDSGPLPPKSVGPVIAGVFSALFVLAVLVLLCHCYRQSHKLGKPSALPFKLRHQFSCPFRVSQSGGTGHANPTFKLQTPQGKRKVTNTPESLRKPSHPPPRPPPDYLRVESPPAPLPAHLNRAAGSSPEAGARIERKESARRPPPSRPMPPAPNCLLSQDFSRPRPPQKALPANPVPGQRTGPRSGGTSLLQPPTSGPQPPRPPAVPVPKLPEYRSQRVGAIISSKI | ||||||
Disulfide bond | 321↔404 | |||||
Sequence: CSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHCCSASAADGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMC | ||||||
Disulfide bond | 361↔388 | |||||
Sequence: CCSASAADGGCIMAAATGHPFPKVFSWC | ||||||
Disulfide bond | 362↔371 | |||||
Sequence: CSASAADGGC | ||||||
Glycosylation | 445 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 448 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 475↔495 | |||||
Sequence: CREQVRQCDLPEFCTGKSPHC | ||||||
Glycosylation | 649 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 658↔668 | |||||
Sequence: CGKKCNGHGVC | ||||||
Disulfide bond | 662↔674 | |||||
Sequence: CNGHGVCNNNKNC | ||||||
Disulfide bond | 676↔685 | |||||
Sequence: CFPGWSPPFC |
Post-translational modification
The precursor is cleaved by a furin endopeptidase.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed, with the highest expression in bone, heart and lung, followed by brain and spleen and relatively low expression in liver, skeletal muscle, kidney and testis. In bone, primarily expressed in cell of the osteoblast lineage and not detected in mature osteoclasts.
Induction
By calcitriol and during osteoblast differentiation.
Developmental stage
Expressed in the heart and in the tail bud at 8.0 dpc, and then in the cranial and dorsal root ganglia. Also expressed weakly and transiently in the intestine, lung and in bone marrow.
Gene expression databases
Structure
Family & Domains
Features
Showing features for motif, domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 131-138 | Cysteine switch | ||||
Sequence: STCRGIRG | ||||||
Domain | 211-409 | Peptidase M12B | ||||
Sequence: KYVELYLVADYAEFQKNRHDQDATKRKLMEIANYVDKFYRSLNIRIALVGLEVWTHGDKCEVSENPYSTLWSFLSWRRKLLAQKSHDNAQLITGRSFQGTTIGLAPLMAMCSVYQSGGVSMDHSENAIGVASTVAHEIGHNFGMSHDSAHCCSASAADGGCIMAAATGHPFPKVFSWCNRKELDRYLQTGGGMCLSNMP | ||||||
Domain | 417-503 | Disintegrin | ||||
Sequence: GRRCGNGYLEDGEECDCGEEEECKNPCCNASNCTLKEGAECAHGSCCHQCKLVAPGTQCREQVRQCDLPEFCTGKSPHCPTNYYQMD | ||||||
Domain | 654-686 | EGF-like | ||||
Sequence: ETEGCGKKCNGHGVCNNNKNCHCFPGWSPPFCN | ||||||
Compositional bias | 755-779 | Polar residues | ||||
Sequence: SQSGGTGHANPTFKLQTPQGKRKVT | ||||||
Region | 755-920 | Disordered | ||||
Sequence: SQSGGTGHANPTFKLQTPQGKRKVTNTPESLRKPSHPPPRPPPDYLRVESPPAPLPAHLNRAAGSSPEAGARIERKESARRPPPSRPMPPAPNCLLSQDFSRPRPPQKALPANPVPGQRTGPRSGGTSLLQPPTSGPQPPRPPAVPVPKLPEYRSQRVGAIISSKI | ||||||
Compositional bias | 786-804 | Pro residues | ||||
Sequence: RKPSHPPPRPPPDYLRVES | ||||||
Motif | 835-846 | SH3-binding | ||||
Sequence: RPPPSRPMPPAP | ||||||
Compositional bias | 887-903 | Pro residues | ||||
Sequence: PTSGPQPPRPPAVPVPK |
Domain
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length920
- Mass (Da)100,860
- Last updated1998-11-01 v2
- Checksum7094FDD4EE547382
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 755-779 | Polar residues | ||||
Sequence: SQSGGTGHANPTFKLQTPQGKRKVT | ||||||
Compositional bias | 786-804 | Pro residues | ||||
Sequence: RKPSHPPPRPPPDYLRVES | ||||||
Compositional bias | 887-903 | Pro residues | ||||
Sequence: PTSGPQPPRPPAVPVPK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF019887 EMBL· GenBank· DDBJ | AAC40037.1 EMBL· GenBank· DDBJ | mRNA | ||
D50410 EMBL· GenBank· DDBJ | BAA18923.2 EMBL· GenBank· DDBJ | mRNA |