F6Q262 · F6Q262_MACMU
- ProteinADAM metallopeptidase with thrombospondin type 1 motif 18
- GeneADAMTS18
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1221 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 296 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 296 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 384 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 436 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 437 | |||||
Sequence: E | ||||||
Binding site | 440 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 446 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 493 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 496 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 496 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
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 | extracellular matrix | |
Cellular Component | extracellular region | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Biological Process | extracellular matrix organization | |
Biological Process | eye development | |
Biological Process | negative regulation of platelet aggregation | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Macaca
Accessions
- Primary accessionF6Q262
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MECALLLACALPAAGS | ||||||
Chain | PRO_5003344473 | 17-1221 | ||||
Sequence: GPPRGPAGLGRVAKALQLCCLCCASVAAALASDSSSGASGLNDDYVFVTPVEVDSAGSYISHDILHNGRKKRSAQNARSSLHYRFSAFGQELHLELKPSAILSSHFIVQVVGKDGASETLKPEVQQCFYQGFIRNDSSSSVAVSTCAGLSGLIRTRKNEFLISPLPQLLAQEHNYSSPAGHHPHVLYKRTAEEKVQRYRGYPSSGQNYPGYSPSHIPHASQSQETEYHHRRLQKQHFCGRRKKYAPKPPTEDTYLRFDEYGSSGRPRRSAGKSQKGLNVETLVVADKKMVEKHGKGNVTTYILTVMNMVSGLFKDGTIGSDINVVVVSLILLEQEPGGLLINHHADQSLNSFCQWQSALIGKNGKRHDHAILLTGFDICSWKNEPCDTLGFAPISGMCSKYRSCTINEDTGLGLAFTIAHESGHNFGMIHDGEGNPCRKAEGNIMSPTLTGNNGVFSWSSCSRQYLKKFLSTPQAGCLVDEPKQAGQYKYPDKLPGQIYDADTQCKWQFGAKAKLCSLGFVKDICKSLWCHRVGHRCETKFMPAAEGTVCGLSMWCRQGQCVKFGELGPRPIHGQWSAWSKWSECSRTCGGGVKYQERHCNNPKPQYGGKFCPGSSRIYQLCNINPCNENSLDFRAQQCAEYNSKPFRGWFYQWKPYTKVEEEDRCKLYCKAENFEFFFAMSGKVKDGTPCSPNKNDVCIDGVCELVGCDHELGSKAVSDACGVCKGDNSTCKFYKGLYLNQHKANEYYPVVIIPAGARSIEIQELQVSSSYLAVRSLSQKYYLTGGWSIDWPGEFPFAGTTFEYQRSFNLPERLYAPGPTNETLVFEILMQGKNPGIAWKYALPKVMNGTPPATKRPAYAWSIVQSECPVSCGGGYINVKAICLRDQNIQVNSSFCSVRTKPVTEPKICNAFSCPAYWMPGEWSTCSKSCAGGQQSRKIQCVQKKPFQKEEAVLHSLCPVSTPTQVQACNSHACPPEWSLGPWSQCSKTCGRGVRRRELLCKGSAAETLPESQCTSLPRPELQEGCVLGRCPKNNRLQWVASSWSECSATCGLGVRKREIKCSEKGFQGKLITFPERRCRNIKRPNLDLEETCNQRACPAHPVYNVVAGWYSSPWQQCTVTCGGGVQTRSVHCVQQGRPSSSCLLHQKPPVLRACNTNFCPAPEKREDPSCVDFFNWCHLVPQHGVCNHKFYGKQCCKSCTRKI | ||||||
Disulfide bond | 369↔420 | |||||
Sequence: CQWQSALIGKNGKRHDHAILLTGFDICSWKNEPCDTLGFAPISGMCSKYRSC | ||||||
Disulfide bond | 395↔402 | |||||
Sequence: CSWKNEPC | ||||||
Disulfide bond | 414↔493 | |||||
Sequence: CSKYRSCTINEDTGLGLAFTIAHESGHNFGMIHDGEGNPCRKAEGNIMSPTLTGNNGVFSWSSCSRQYLKKFLSTPQAGC | ||||||
Disulfide bond | 453↔477 | |||||
Sequence: CRKAEGNIMSPTLTGNNGVFSWSSC | ||||||
Disulfide bond | 521↔546 | |||||
Sequence: CKWQFGAKAKLCSLGFVKDICKSLWC | ||||||
Disulfide bond | 532↔553 | |||||
Sequence: CSLGFVKDICKSLWCHRVGHRC | ||||||
Disulfide bond | 541↔572 | |||||
Sequence: CKSLWCHRVGHRCETKFMPAAEGTVCGLSMWC | ||||||
Disulfide bond | 566↔577 | |||||
Sequence: CGLSMWCRQGQC | ||||||
Disulfide bond | 601↔638 | |||||
Sequence: CSRTCGGGVKYQERHCNNPKPQYGGKFCPGSSRIYQLC | ||||||
Disulfide bond | 605↔643 | |||||
Sequence: CGGGVKYQERHCNNPKPQYGGKFCPGSSRIYQLCNINPC | ||||||
Disulfide bond | 616↔628 | |||||
Sequence: CNNPKPQYGGKFC |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 216-237 | Polar residues | ||||
Sequence: GYPSSGQNYPGYSPSHIPHASQ | ||||||
Region | 216-291 | Disordered | ||||
Sequence: GYPSSGQNYPGYSPSHIPHASQSQETEYHHRRLQKQHFCGRRKKYAPKPPTEDTYLRFDEYGSSGRPRRSAGKSQK | ||||||
Domain | 293-498 | Peptidase M12B | ||||
Sequence: LNVETLVVADKKMVEKHGKGNVTTYILTVMNMVSGLFKDGTIGSDINVVVVSLILLEQEPGGLLINHHADQSLNSFCQWQSALIGKNGKRHDHAILLTGFDICSWKNEPCDTLGFAPISGMCSKYRSCTINEDTGLGLAFTIAHESGHNFGMIHDGEGNPCRKAEGNIMSPTLTGNNGVFSWSSCSRQYLKKFLSTPQAGCLVDEP | ||||||
Domain | 1184-1221 | PLAC | ||||
Sequence: EDPSCVDFFNWCHLVPQHGVCNHKFYGKQCCKSCTRKI |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,221
- Mass (Da)135,080
- Last updated2016-11-30 v2
- ChecksumF8FC3790D808CC55
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5F7ZNN3 | A0A5F7ZNN3_MACMU | ADAMTS18 | 1198 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 216-237 | Polar residues | ||||
Sequence: GYPSSGQNYPGYSPSHIPHASQ |
Keywords
- Technical term