ID A7S4Y9_NEMVE Unreviewed; 277 AA.
AC A7S4Y9;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN ORFNames=NEMVEDRAFT_v1g229403 {ECO:0000313|EMBL:EDO41236.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO41236.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO41236.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion
CC molecule that regulates neural recognition during the development of
CC the nervous system. Component of the repulsive Plexin signaling
CC response to regulate motor axon guidance at the embryonic stage. Also
CC component of a receptor complex that is required in the adult visual
CC system to innervate the lamina layer; specific targeting of R1-R6
CC axons. {ECO:0000256|ARBA:ARBA00034468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171,
CC ECO:0000256|RuleBase:RU000312};
CC -!- SUBUNIT: Interacts with plexA; component of a receptor complex that
CC mediates the repulsive signaling in response to Semaphorin ligands.
CC {ECO:0000256|ARBA:ARBA00034516}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC {ECO:0000256|RuleBase:RU000312}.
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DR EMBL; DS469580; EDO41236.1; -; Genomic_DNA.
DR RefSeq; XP_001633299.1; XM_001633249.1.
DR AlphaFoldDB; A7S4Y9; -.
DR STRING; 45351.A7S4Y9; -.
DR EnsemblMetazoa; EDO41236; EDO41236; NEMVEDRAFT_v1g229403.
DR GeneID; 5513038; -.
DR KEGG; nve:5513038; -.
DR eggNOG; KOG1026; Eukaryota.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; A7S4Y9; -.
DR OMA; DENCLTE; -.
DR OrthoDB; 1614410at2759; -.
DR PhylomeDB; A7S4Y9; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF573; INACTIVE TYROSINE-PROTEIN KINASE 7; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|RuleBase:RU000312};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|RuleBase:RU000312};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593};
KW Transmembrane {ECO:0000256|RuleBase:RU000312}.
FT DOMAIN 8..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 277 AA; 31763 MW; 326BD7AF17EF2BD9 CRC64;
MEFPRHDLEA LRTLGNGSYG RAFLARASGI KDGERETMVV VKSLIAKDDI VREDFTRELE
SLVNMEHSNV VSLLGVCRDS EPFYMIFECF EKGDLKQFLL SCNDNGRSTL TSSHKLTMCS
NIVSGMSYLA ANKFVHKDLA ARNCMVTKDL QVKIGFLNLS YDLYNAEYYR FNNILIPLRW
MPSEAIFHDD FTEKSDVWSF GVLAWEIYSL GQIPYTDRSD EEVLKCVKDD LRLPKPDNCP
DNMANVMKKC WEPNPNDRPN FDMIFAEMSE VAVDSHV
//
