A0A484DFV9 · A0A484DFV9_PERFV
- Proteinreceptor protein-tyrosine kinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1374 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | basal plasma membrane | |
Cellular Component | receptor complex | |
Molecular Function | ATP binding | |
Molecular Function | hepatocyte growth factor receptor activity | |
Biological Process | axon guidance | |
Biological Process | cell migration | |
Biological Process | liver development | |
Biological Process | pancreas development |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namereceptor protein-tyrosine kinase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Perciformes > Percoidei > Percidae > Percinae > Perca
Accessions
- Primary accessionA0A484DFV9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 939-962 | Helical | ||||
Sequence: YMVGVVLGILAALVAGAVLAFVVM |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MVHWTSKWGTCVCVQTLLAFALA | ||||||
Chain | PRO_5019824721 | 24-1374 | receptor protein-tyrosine kinase | |||
Sequence: NCPSLAPSPVNFSVVYTMPFFQARGPIQNIVNNSLYQEVYVASQNVIEAVNRSLEKVWELRTGPVGSPECQICDLCDIDKDPDFPEDTNNQILLLDTLFMYLYSCGSSQYGVCYFHQLNSNGESPSLSKCLFRKAANSAVYCPDCVASPLGTKVTMVEEGQTVYFFVASTVNDSVTQRYGRKSISVRRPLATEDGFYSDVRGLTVLPGLRRTYHIEYVYSFFSQEFVYFLSVQRESPDQDSSPFQTRLGRLPRNEWEMKRYREVILECRFEPKRRRRNVASEPYKDVVYNVVQAAHFGKAGRELAEELGAEEEDDILYGVFAVTDDNGVTEHDSALCAFPMDNVNKAIVDGVDDCCESGPEQLSRGLCHFQPCESCPHESMENNATCRDHPTMVSKPYYRVDLFNRQMIDVLLTALLVTTIENKTVAHIGTSTGRLLQLVLTRSSPIIFANYSLVENQRVSSIAAVYSSEYLLFVVGDKMIQVPQRGPGCQHFLTCAMCLTAPKFMGCGWCSGVCSWESECNRRWRNESCPPGITGFFPRTAPPDGQTELTVCGWEFQSPLRPAITSRTHQVRLGQTACTVLPVKSNNTHFVCKIRSGATELSKPVNITVEVHEGKVEGRYSIDGKAEMPGFTFVIPNITEIQPNYGPRVGGTLITVTGPHLDAGKTRKVTLNDMPCPIKRVTEPKGNVSSIICLSQPISEVRDVPLSVFIDKSPVLTTKVFYYKENPMITAVLPDCSFDRGSKIVIGGENLDSVYRTIIRFKPNESHLKPVTRECIGKSLPTRMECISPVFPRDETEEGELSFDMDGALGLWNKEFSYHPYGEPIPFETDGHVLNLYPGFDEVSLHHQKLNLVSSCMTIIMTVAGVDCDAKVLDNEITCRIPKNMTITSEGLPVKISINGQVHNVGTVVRVSNHYMVGVVLGILAALVAGAVLAFVVMKHLRKTKKASMVETRLAHSANLSGTNNVELSPVGDYRRVVSLSPSTPLVGSMVFPSLSFAAGSIDPTLTPLMPSEKISISSFRPELLEEVKDVLIPAEMLIVQHHRIIGKGHFGTVYHGYFTDHNNREIHCAVKSLNRITDVEEVEQFLKEGIIMKGFHHSNVLSLLGILLPQEGLPLVVLPYMKHGDLRHFIRCEKRNPTVKDLIGFGLQVARGMEYLAQKKFVHRDLAGRNCMLDESYTVKVADFGMARDVFDKEYYSVQDHRKAKLPVKWMAIESLQTQKFTSKSDVWSFGVLMWEMLTRGASPYPEVDPYDITHYLLKGRRLPQPQYCPDPLYSIMLQCWDPDPELRPSFATLVSAVFTILSGLEGEHYISLNVTYVNLDQPRPYPALTESADEYNSTDVEDSGSVSS | ||||||
Disulfide bond | 96↔99 | |||||
Sequence: CDLC | ||||||
Disulfide bond | 128↔136 | |||||
Sequence: CGSSQYGVC | ||||||
Disulfide bond | 165↔168 | |||||
Sequence: CPDC | ||||||
Disulfide bond | 291↔360 | |||||
Sequence: CRFEPKRRRRNVASEPYKDVVYNVVQAAHFGKAGRELAEELGAEEEDDILYGVFAVTDDNGVTEHDSALC | ||||||
Disulfide bond | 378↔399 | |||||
Sequence: CCESGPEQLSRGLCHFQPCESC | ||||||
Disulfide bond | 513↔531 | |||||
Sequence: CQHFLTCAMCLTAPKFMGC | ||||||
Disulfide bond | 519↔553 | |||||
Sequence: CAMCLTAPKFMGCGWCSGVCSWESECNRRWRNESC | ||||||
Disulfide bond | 522↔538 | |||||
Sequence: CLTAPKFMGCGWCSGVC | ||||||
Disulfide bond | 534↔544 | |||||
Sequence: CSGVCSWESEC | ||||||
Modified residue | 1220 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | ||||||
Modified residue | 1221 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | ||||||
Modified residue | 1335 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y | ||||||
Modified residue | 1342 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y |
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-508 | Sema | ||||
Sequence: CPSLAPSPVNFSVVYTMPFFQARGPIQNIVNNSLYQEVYVASQNVIEAVNRSLEKVWELRTGPVGSPECQICDLCDIDKDPDFPEDTNNQILLLDTLFMYLYSCGSSQYGVCYFHQLNSNGESPSLSKCLFRKAANSAVYCPDCVASPLGTKVTMVEEGQTVYFFVASTVNDSVTQRYGRKSISVRRPLATEDGFYSDVRGLTVLPGLRRTYHIEYVYSFFSQEFVYFLSVQRESPDQDSSPFQTRLGRLPRNEWEMKRYREVILECRFEPKRRRRNVASEPYKDVVYNVVQAAHFGKAGRELAEELGAEEEDDILYGVFAVTDDNGVTEHDSALCAFPMDNVNKAIVDGVDDCCESGPEQLSRGLCHFQPCESCPHESMENNATCRDHPTMVSKPYYRVDLFNRQMIDVLLTALLVTTIENKTVAHIGTSTGRLLQLVLTRSSPIIFANYSLVENQRVSSIAAVYSSEYLLFVVGDKMIQVPQ | ||||||
Domain | 1064-1325 | Protein kinase | ||||
Sequence: VQHHRIIGKGHFGTVYHGYFTDHNNREIHCAVKSLNRITDVEEVEQFLKEGIIMKGFHHSNVLSLLGILLPQEGLPLVVLPYMKHGDLRHFIRCEKRNPTVKDLIGFGLQVARGMEYLAQKKFVHRDLAGRNCMLDESYTVKVADFGMARDVFDKEYYSVQDHRKAKLPVKWMAIESLQTQKFTSKSDVWSFGVLMWEMLTRGASPYPEVDPYDITHYLLKGRRLPQPQYCPDPLYSIMLQCWDPDPELRPSFATLVSAVFT | ||||||
Region | 1353-1374 | Disordered | ||||
Sequence: ALTESADEYNSTDVEDSGSVSS | ||||||
Compositional bias | 1357-1374 | Polar residues | ||||
Sequence: SADEYNSTDVEDSGSVSS |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,374
- Mass (Da)153,585
- Last updated2019-06-05 v1
- Checksum69739A2E13851482
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1357-1374 | Polar residues | ||||
Sequence: SADEYNSTDVEDSGSVSS |
Keywords
- Technical term