ID A0A8C5GN58_GOUWI Unreviewed; 941 AA.
AC A0A8C5GN58;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=LOC114461555 {ECO:0000313|Ensembl:ENSGWIP00000032846.1};
OS Gouania willdenowi (Blunt-snouted clingfish) (Lepadogaster willdenowi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Blenniimorphae; Blenniiformes; Gobiesocoidei; Gobiesocidae;
OC Gobiesocinae; Gouania.
OX NCBI_TaxID=441366 {ECO:0000313|Ensembl:ENSGWIP00000032846.1, ECO:0000313|Proteomes:UP000694680};
RN [1] {ECO:0000313|Ensembl:ENSGWIP00000032846.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGWIP00000032846.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGWIP00000032846.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
CC transmembrane ephrin-B family ligands residing on adjacent cells,
CC leading to contact-dependent bidirectional signaling into neighboring
CC cells. The signaling pathway downstream of the receptor is referred to
CC as forward signaling while the signaling pathway downstream of the
CC ephrin ligand is referred to as reverse signaling. Together with its
CC cognate ligand/functional ligand EFNB2 is involved in the regulation of
CC cell adhesion and cell migration, and plays a central role in heart
CC morphogenesis, angiogenesis and blood vessel remodeling and
CC permeability. EPHB4-mediated forward signaling controls cellular
CC repulsion and segregation from EFNB2-expressing cells. Involved in
CC somitogenesis. {ECO:0000256|ARBA:ARBA00055965}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00051243};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}.
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DR AlphaFoldDB; A0A8C5GN58; -.
DR Ensembl; ENSGWIT00000035741.1; ENSGWIP00000032846.1; ENSGWIG00000016505.1.
DR Proteomes; UP000694680; Chromosome 4.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IEA:TreeGrafter.
DR GO; GO:0007411; P:axon guidance; IEA:TreeGrafter.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05065; PTKc_EphR_B; 1.
DR FunFam; 2.60.40.10:FF:000041; ephrin type-A receptor 3; 1.
DR FunFam; 1.10.150.50:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 2.10.50.10:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 2.60.40.1770:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 3.30.200.20:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 1.10.510.10:FF:000015; Ephrin type-B receptor 2; 1.
DR FunFam; 2.60.120.260:FF:000004; Ephrin type-B receptor 2; 1.
DR Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR050449; Ephrin_rcpt_TKs.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF17; EPHRIN TYPE-B RECEPTOR 1; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF25599; Ephrin_CRD; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000666-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000694680};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 1..171
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 292..403
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 404..494
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 572..836
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 867..931
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 697
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 578..586
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 39..153
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 74..84
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 941 AA; 104425 MW; 3544537A43568B59 CRC64;
MDTRTATAEL GWISFPANGW EEVSGYDENL NTIRTYQVCN VFEPSQNNWL LTTYVDRRAA
QRIYVEIRFT VRDCASIPSV LGSCKETFNL YYLETDRSMS DGIKGVDTIA ADESFSQVDF
GGRLMKVNTE VRSFGPLSKG RGFYLAFQDL GACMSLLAVR VFYKKCPSVV QNFAFFPETL
TGAESTSLVI ARGSCIQNAE EVDVPIKLYC NGDGEWMVPI GSCSCKSGYE PDNGNVCRAC
PQGTFKSSQG AGVCQQCPLN SRSTIEAATL CGCRNGYYRG DMDKPEDMCT SVPSAPRNLV
SVVNQTSVLL EWHTPRDTGH REDLSYNILC RRCHSNERRA CQPCDDSVLF LPGKRALKDN
TVEISKLRAH TSYTFDIQAV NGVSNKSPYP AQQLSINITT NQAAPSVVPI MHQVSSTSRS
FSLSWPPPEQ PNGIILDYEI LISFLLSLGC SNTTPNVILE GLRPGTGYAV QVRARTVAGF
GSYSKEMLFQ TLTDDEYKSE LGQQLSLIAG SLVGGVCIVS IVAIAIICSR YLTRTHSLTH
SPGVKIYIDP YTYEDPNEAV HEFAKEIESS CVKIEEVIGS GEFGEVYKGR LKPLGKKEIL
VAIKTLKVGY SERQRRDFLA EASIMGQFDQ PNIIRLEGVV TKSRPTMIIT EFMENGALDS
FLRQNDGQFP VIQLVGMLRG IASGMRYLAE MSYVHRDLAA RNILVNSNLV CKVSDFGLSR
YLEDEDTSDP TYTSSLGGKI PVRWTAPEAI AYRKFTSASD VWSYGIVTWE VMSYGERPYW
DMSNQDVINA IEQDFRLPAP MDCPVVLHQL MLDCWQKDRN ARPKFHDIVS MLDKMIRNPA
SLKAGTNNIG LGPPHHPLLD RGAPDLSRVS SVEDWLTALK MSQYRDSFLL SGFNSLPLVT
QITAEDLQRI GVLLAGHQKK ILTSVQSMRP NADDQSPTES V
//
