P16620 · PTP69_DROME
- ProteinTyrosine-protein phosphatase 69D
- GenePtp69D
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1462 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Possible cell adhesion receptor.
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 1097 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Active site | 1391 | Phosphocysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cell surface | |
Cellular Component | plasma membrane | |
Molecular Function | protein tyrosine phosphatase activity | |
Molecular Function | transmembrane receptor protein tyrosine phosphatase activity | |
Biological Process | axon guidance | |
Biological Process | cell adhesion | |
Biological Process | defasciculation of motor neuron axon | |
Biological Process | dendrite morphogenesis | |
Biological Process | fasciculation of sensory neuron axon | |
Biological Process | motor neuron axon guidance | |
Biological Process | synaptic target inhibition |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine-protein phosphatase 69D
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP16620
- 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 | 29-805 | Extracellular | ||||
Sequence: SVKQEWAEIGKNVSLECASENEAVAWKLGNQTINKNHTRYKIRTEPLKSNDDGSENNDSQDFIKYKNVLALLDVNIKDSGNYTCTAQTGQNHSTEFQVRPYLPSKVLQSTPDRIKRKIKQDVMLYCLIEMYPQNETTNRNLKWLKDGSQFEFLDTFSSISKLNDTHLNFTLEFTEVYKKENGTYKCTVFDDTGLEITSKEITLFVMEVPQVSIDFAKAVGANKIYLNWTVNDGNDPIQKFFITLQEAGTPTFTYHKDFINGSHTSYILDHFKPNTTYFLRIVGKNSIGNGQPTQYPQGITTLSYDPIFIPKVETTGSTASTITIGWNPPPPDLIDYIQYYELIVSESGEVPKVIEEAIYQQNSRNLPYMFDKLKTATDYEFRVRACSDLTKTCGPWSENVNGTTMDGVATKPTNLSIQCHHDNVTRGNSIAINWDVPKTPNGKVVSYLIHLLGNPMSTVDREMWGPKIRRIDEPHHKTLYESVSPNTNYTVTVSAITRHKKNGEPATGSCLMPVSTPDAIGRTMWSKVNLDSKYVLKLYLPKISERNGPICCYRLYLVRINNDNKELPDPEKLNIATYQEVHSDNVTRSSAYIAEMISSKYFRPEIFLGDEKRFSENNDIIRDNDEICRKCLEGTPFLRKPEIIHIPPQGSLSNSDSELPILSEKDNLIKGANLTEHALKILESKLRDKRNAVTSDENPILSAVNPNVPLHDSSRDVFDGEIDINSNYTGFLEIIVRDRNNALMAYSKYFDIITPATEAEPIQSLNNMDYYLSIGVK | ||||||
Transmembrane | 806-823 | Helical | ||||
Sequence: AGAVLLGVILVFIVLWVF | ||||||
Topological domain | 824-1462 | Cytoplasmic | ||||
Sequence: HHKKTKNELQGEDTLTLRDSLSRALFGRRNHNHSHFITSGNHKGFDAGPIHRLDLENAYKNRHKDTDYGFLREYEMLPNRFSDRTTKNSDLKENACKNRYPDIKAYDQTRVKLAVINGLQTTDYINANFVIGYKERKKFICAQGPMESTIDDFWRMIWEQHLEIIVMLTNLEEYNKAKCAKYWPEKVFDTKQFGDILVKFAQERKTGDYIERTLNVSKNKANVGEEEDRRQITQYHYLTWKDFMAPEHPHGIIKFIRQINSVYSLQRGPILVHCSAGVGRTGTLVALDSLIQQLEEEDSVSIYNTVCDLRHQRNFLVQSLKQYIFLYRALLDTGTFGNTDICIDTMASAIESLKRKPNEGKCKLEVEFEKLLATADEISKSCSVGENEENNMKNRSQEIIPYDRNRVILTPLPMRENSTYINASFIEGYDNSETFIIAQDPLENTIGDFWRMISEQSVTTLVMISEIGDGPRKCPRYWADDEVQYDHILVKYVHSESCPYYTRREFYVTNCKIDDTLKVTQFQYNGWPTVDGEVPEVCRGIIELVDQAYNHYKNNKNSGCRSPLTVHCSLGTDRSSIFVAMCILVQHLRLEKCVDICATTRKLRSQRTGLINSYAQYEFLHRAIINYSDLHHIAESTLD |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-28 | |||||
Sequence: MALLYRRMSMLLNIILAYIFLCAICVQG | ||||||
Chain | PRO_0000025428 | 29-1462 | Tyrosine-protein phosphatase 69D | |||
Sequence: SVKQEWAEIGKNVSLECASENEAVAWKLGNQTINKNHTRYKIRTEPLKSNDDGSENNDSQDFIKYKNVLALLDVNIKDSGNYTCTAQTGQNHSTEFQVRPYLPSKVLQSTPDRIKRKIKQDVMLYCLIEMYPQNETTNRNLKWLKDGSQFEFLDTFSSISKLNDTHLNFTLEFTEVYKKENGTYKCTVFDDTGLEITSKEITLFVMEVPQVSIDFAKAVGANKIYLNWTVNDGNDPIQKFFITLQEAGTPTFTYHKDFINGSHTSYILDHFKPNTTYFLRIVGKNSIGNGQPTQYPQGITTLSYDPIFIPKVETTGSTASTITIGWNPPPPDLIDYIQYYELIVSESGEVPKVIEEAIYQQNSRNLPYMFDKLKTATDYEFRVRACSDLTKTCGPWSENVNGTTMDGVATKPTNLSIQCHHDNVTRGNSIAINWDVPKTPNGKVVSYLIHLLGNPMSTVDREMWGPKIRRIDEPHHKTLYESVSPNTNYTVTVSAITRHKKNGEPATGSCLMPVSTPDAIGRTMWSKVNLDSKYVLKLYLPKISERNGPICCYRLYLVRINNDNKELPDPEKLNIATYQEVHSDNVTRSSAYIAEMISSKYFRPEIFLGDEKRFSENNDIIRDNDEICRKCLEGTPFLRKPEIIHIPPQGSLSNSDSELPILSEKDNLIKGANLTEHALKILESKLRDKRNAVTSDENPILSAVNPNVPLHDSSRDVFDGEIDINSNYTGFLEIIVRDRNNALMAYSKYFDIITPATEAEPIQSLNNMDYYLSIGVKAGAVLLGVILVFIVLWVFHHKKTKNELQGEDTLTLRDSLSRALFGRRNHNHSHFITSGNHKGFDAGPIHRLDLENAYKNRHKDTDYGFLREYEMLPNRFSDRTTKNSDLKENACKNRYPDIKAYDQTRVKLAVINGLQTTDYINANFVIGYKERKKFICAQGPMESTIDDFWRMIWEQHLEIIVMLTNLEEYNKAKCAKYWPEKVFDTKQFGDILVKFAQERKTGDYIERTLNVSKNKANVGEEEDRRQITQYHYLTWKDFMAPEHPHGIIKFIRQINSVYSLQRGPILVHCSAGVGRTGTLVALDSLIQQLEEEDSVSIYNTVCDLRHQRNFLVQSLKQYIFLYRALLDTGTFGNTDICIDTMASAIESLKRKPNEGKCKLEVEFEKLLATADEISKSCSVGENEENNMKNRSQEIIPYDRNRVILTPLPMRENSTYINASFIEGYDNSETFIIAQDPLENTIGDFWRMISEQSVTTLVMISEIGDGPRKCPRYWADDEVQYDHILVKYVHSESCPYYTRREFYVTNCKIDDTLKVTQFQYNGWPTVDGEVPEVCRGIIELVDQAYNHYKNNKNSGCRSPLTVHCSLGTDRSSIFVAMCILVQHLRLEKCVDICATTRKLRSQRTGLINSYAQYEFLHRAIINYSDLHHIAESTLD | ||||||
Glycosylation | 40 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 45↔112 | |||||
Sequence: CASENEAVAWKLGNQTINKNHTRYKIRTEPLKSNDDGSENNDSQDFIKYKNVLALLDVNIKDSGNYTC | ||||||
Glycosylation | 58 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 64 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 85 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 109 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 119 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 154↔214 | |||||
Sequence: CLIEMYPQNETTNRNLKWLKDGSQFEFLDTFSSISKLNDTHLNFTLEFTEVYKKENGTYKC | ||||||
Glycosylation | 162 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 191 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 196 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 209 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 255 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 288 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 302 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 429 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 442 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 451 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 516 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 613 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 701 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 755 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 29-125 | Ig-like C2-type 1 | ||||
Sequence: SVKQEWAEIGKNVSLECASENEAVAWKLGNQTINKNHTRYKIRTEPLKSNDDGSENNDSQDFIKYKNVLALLDVNIKDSGNYTCTAQTGQNHSTEFQ | ||||||
Domain | 131-230 | Ig-like C2-type 2 | ||||
Sequence: PSKVLQSTPDRIKRKIKQDVMLYCLIEMYPQNETTNRNLKWLKDGSQFEFLDTFSSISKLNDTHLNFTLEFTEVYKKENGTYKCTVFDDTGLEITSKEIT | ||||||
Domain | 237-332 | Fibronectin type-III 1 | ||||
Sequence: PQVSIDFAKAVGANKIYLNWTVNDGNDPIQKFFITLQEAGTPTFTYHKDFINGSHTSYILDHFKPNTTYFLRIVGKNSIGNGQPTQYPQGITTLSY | ||||||
Domain | 334-435 | Fibronectin type-III 2 | ||||
Sequence: PIFIPKVETTGSTASTITIGWNPPPPDLIDYIQYYELIVSESGEVPKVIEEAIYQQNSRNLPYMFDKLKTATDYEFRVRACSDLTKTCGPWSENVNGTTMDG | ||||||
Domain | 439-547 | Fibronectin type-III 3 | ||||
Sequence: KPTNLSIQCHHDNVTRGNSIAINWDVPKTPNGKVVSYLIHLLGNPMSTVDREMWGPKIRRIDEPHHKTLYESVSPNTNYTVTVSAITRHKKNGEPATGSCLMPVSTPDA | ||||||
Domain | 893-1156 | Tyrosine-protein phosphatase 1 | ||||
Sequence: FLREYEMLPNRFSDRTTKNSDLKENACKNRYPDIKAYDQTRVKLAVINGLQTTDYINANFVIGYKERKKFICAQGPMESTIDDFWRMIWEQHLEIIVMLTNLEEYNKAKCAKYWPEKVFDTKQFGDILVKFAQERKTGDYIERTLNVSKNKANVGEEEDRRQITQYHYLTWKDFMAPEHPHGIIKFIRQINSVYSLQRGPILVHCSAGVGRTGTLVALDSLIQQLEEEDSVSIYNTVCDLRHQRNFLVQSLKQYIFLYRALLDT | ||||||
Domain | 1187-1450 | Tyrosine-protein phosphatase 2 | ||||
Sequence: LEVEFEKLLATADEISKSCSVGENEENNMKNRSQEIIPYDRNRVILTPLPMRENSTYINASFIEGYDNSETFIIAQDPLENTIGDFWRMISEQSVTTLVMISEIGDGPRKCPRYWADDEVQYDHILVKYVHSESCPYYTRREFYVTNCKIDDTLKVTQFQYNGWPTVDGEVPEVCRGIIELVDQAYNHYKNNKNSGCRSPLTVHCSLGTDRSSIFVAMCILVQHLRLEKCVDICATTRKLRSQRTGLINSYAQYEFLHRAIINY |
Sequence similarities
Belongs to the protein-tyrosine phosphatase family. Receptor class subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P16620-1
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.
- NameA
- Length1,462
- Mass (Da)167,460
- Last updated2005-08-30 v2
- Checksum61214ADC778D319A
P16620-2
- NameB
- Differences from canonical
- 845-845: Missing
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 91 | in Ref. 1; AAA28842 | ||||
Sequence: I → M | ||||||
Sequence conflict | 98 | in Ref. 1; AAA28842 | ||||
Sequence: A → T | ||||||
Sequence conflict | 105 | in Ref. 1; AAA28842 | ||||
Sequence: K → N | ||||||
Sequence conflict | 127 | in Ref. 1; AAA28842 | ||||
Sequence: R → K | ||||||
Sequence conflict | 638 | in Ref. 1; AAA28842 | ||||
Sequence: D → A | ||||||
Sequence conflict | 651 | in Ref. 1; AAA28842 | ||||
Sequence: D → G | ||||||
Alternative sequence | VSP_015257 | 845 | in isoform B | |||
Sequence: Missing | ||||||
Sequence conflict | 990 | in Ref. 1; AAA28842 | ||||
Sequence: M → I | ||||||
Sequence conflict | 1189 | in Ref. 1; AAA28842 | ||||
Sequence: V → M | ||||||
Sequence conflict | 1265 | in Ref. 1; AAA28842 | ||||
Sequence: L → F |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M27699 EMBL· GenBank· DDBJ | AAA28842.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014296 EMBL· GenBank· DDBJ | AAF49892.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAO41254.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT001531 EMBL· GenBank· DDBJ | AAN71286.1 EMBL· GenBank· DDBJ | mRNA |