O43506 · ADA20_HUMAN
- ProteinDisintegrin and metalloproteinase domain-containing protein 20
- GeneADAM20
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids726 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
May be involved in sperm maturation and/or fertilization.
Miscellaneous
May be the functional equivalent of ADAM 1/fertilin alpha which is a pseudogene in human.
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 173 | Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 342 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 343 | |||||
Sequence: E | ||||||
Binding site | 346 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 352 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | external side of plasma membrane | |
Cellular Component | plasma membrane | |
Cellular Component | sperm head plasma membrane | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | metallopeptidase activity | |
Biological Process | male gonad development | |
Biological Process | proteolysis | |
Biological Process | single fertilization |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDisintegrin and metalloproteinase domain-containing protein 20
- EC number
- Short namesADAM 20
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO43506
- Secondary accessions
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 | 207-693 | Extracellular | ||||
Sequence: RFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYNLNNRLQHDVAHLFIKDTQGMKLGVAYVKGICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDTQWCVCELQWCIMHAYRKVTTKFSNCSYAQYWDSTISSGLCIQPPPYPGNIFRLKYCGNLVVEEGEECDCGTIRQCAKDPCCLLNCTLHPGAACAFGICCKDCKFLPSGTLCRQQVGECDLPEWCNGTSHQCPDDVYVQDGISCNVNAFCYEKTCNNHDIQCKEIFGQDARSASQSCYQEINTQGNRFGHCGIVGTTYVKCWTPDIMCGRVQCENVGVIPNLIEHSTVQQFHLNDTTCWGTDYHLGMAIPDIGEVKDGTVCGPEKICIRKKCASMVHLSQACQPKTCNMRGICNNKQHCHCNHEWAPPYCKDKGYGGSADSGPPPKNNMEGLNVMGKLRY | ||||||
Transmembrane | 694-714 | Helical | ||||
Sequence: LSLLCLLPLVAFLLFCLHVLF | ||||||
Topological domain | 715-726 | Cytoplasmic | ||||
Sequence: KKRTKSKEDEEG |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_047311 | 19 | in dbSNP:rs1059166 | |||
Sequence: F → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 864 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, propeptide, glycosylation, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-31 | |||||
Sequence: MAVGEPLVHIRVTLLLLWFGMFLSISGHSQA | ||||||
Propeptide | PRO_0000029106 | 32-206 | ||||
Sequence: RPSQYFTSPEVVIPLKVISRGRGAKAPGWLSYSLRFGGQRYIVHMRVNKLLFAAHLPVFTYTEQHALLQDQPFIQDDCYYHGYVEGVPESLVALSTCSGGFLGMLQINDLVYEIKPISVSATFEHLVYKIDSDDTQFPPMRCGLTEEKIAHQMELQLSYNFTLKQSSFVGWWTHQ | ||||||
Glycosylation | 191 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000029107 | 207-726 | Disintegrin and metalloproteinase domain-containing protein 20 | |||
Sequence: RFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYNLNNRLQHDVAHLFIKDTQGMKLGVAYVKGICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDTQWCVCELQWCIMHAYRKVTTKFSNCSYAQYWDSTISSGLCIQPPPYPGNIFRLKYCGNLVVEEGEECDCGTIRQCAKDPCCLLNCTLHPGAACAFGICCKDCKFLPSGTLCRQQVGECDLPEWCNGTSHQCPDDVYVQDGISCNVNAFCYEKTCNNHDIQCKEIFGQDARSASQSCYQEINTQGNRFGHCGIVGTTYVKCWTPDIMCGRVQCENVGVIPNLIEHSTVQQFHLNDTTCWGTDYHLGMAIPDIGEVKDGTVCGPEKICIRKKCASMVHLSQACQPKTCNMRGICNNKQHCHCNHEWAPPYCKDKGYGGSADSGPPPKNNMEGLNVMGKLRYLSLLCLLPLVAFLLFCLHVLFKKRTKSKEDEEG | ||||||
Glycosylation | 226 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 317↔394 | |||||
Sequence: CQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDTQWCVCELQWCIMHAYRKVTTKFSNCSYAQYWDSTISSGLC | ||||||
Disulfide bond | 357↔379 | |||||
Sequence: CVCELQWCIMHAYRKVTTKFSNC | ||||||
Disulfide bond | 359↔364 | |||||
Sequence: CELQWC | ||||||
Glycosylation | 378 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 438 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 465↔485 | |||||
Sequence: CRQQVGECDLPEWCNGTSHQC | ||||||
Glycosylation | 479 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 587 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 635↔646 | |||||
Sequence: CQPKTCNMRGIC | ||||||
Disulfide bond | 640↔652 | |||||
Sequence: CNMRGICNNKQHC | ||||||
Disulfide bond | 654↔663 | |||||
Sequence: CNHEWAPPYC |
Post-translational modification
Has no obvious cleavage site for furin endopeptidase, suggesting that the proteolytic processing is regulated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Testis specific.
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 171-178 | Cysteine switch | ||||
Sequence: MRCGLTEE | ||||||
Domain | 207-400 | Peptidase M12B | ||||
Sequence: RFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYNLNNRLQHDVAHLFIKDTQGMKLGVAYVKGICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDTQWCVCELQWCIMHAYRKVTTKFSNCSYAQYWDSTISSGLCIQPPPY | ||||||
Domain | 407-493 | Disintegrin | ||||
Sequence: LKYCGNLVVEEGEECDCGTIRQCAKDPCCLLNCTLHPGAACAFGICCKDCKFLPSGTLCRQQVGECDLPEWCNGTSHQCPDDVYVQD | ||||||
Domain | 635-663 | EGF-like | ||||
Sequence: CQPKTCNMRGICNNKQHCHCNHEWAPPYC |
Domain
A tripeptide motif (VGE) within disintegrin-like domain could be involved in the binding to egg integrin receptor and thus could mediate sperm/egg binding.
The cysteine-rich domain encodes putative cell-fusion peptides, which could be involved in sperm-egg fusion.
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.
- Length726
- Mass (Da)81,603
- Last updated2008-11-25 v2
- Checksum7DB864FA1796A9B0
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A494C0E3 | A0A494C0E3_HUMAN | ADAM20 | 776 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 109 | in Ref. 1; AAC52041 | ||||
Sequence: C → W | ||||||
Sequence conflict | 637 | in Ref. 1; AAC52041 | ||||
Sequence: P → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF029899 EMBL· GenBank· DDBJ | AAC52041.1 EMBL· GenBank· DDBJ | mRNA | ||
AF158643 EMBL· GenBank· DDBJ | AAD55254.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL357153 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471061 EMBL· GenBank· DDBJ | EAW81037.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
BC025378 EMBL· GenBank· DDBJ | AAH25378.2 EMBL· GenBank· DDBJ | mRNA | Different initiation |