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Database: UniProt
Entry: A0A3B4EC11_PYGNA
LinkDB: A0A3B4EC11_PYGNA
Original site: A0A3B4EC11_PYGNA 
ID   A0A3B4EC11_PYGNA        Unreviewed;       936 AA.
AC   A0A3B4EC11;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=EPHA4 {ECO:0000313|Ensembl:ENSPNAP00000033238.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000033238.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000033238.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Early endosome {ECO:0000256|ARBA:ARBA00004412}. Endosome
CC       {ECO:0000256|ARBA:ARBA00004177}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A3B4EC11; -.
DR   STRING; 42514.ENSPNAP00000033238; -.
DR   Ensembl; ENSPNAT00000023936.1; ENSPNAP00000033238.1; ENSPNAG00000021825.1.
DR   GeneTree; ENSGT00940000156948; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0005769; C:early endosome; 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:0005003; F:ephrin receptor activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05066; PTKc_EphR_A; 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; 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; 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; 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:SF18; EPHRIN TYPE-A RECEPTOR 4; 1.
DR   Pfam; PF14575; EphA2_TM; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM01411; Ephrin_rec_like; 1.
DR   SMART; SM00060; FN3; 2.
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   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000666-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   TRANSMEM        521..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..183
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          302..412
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          413..508
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          591..852
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          888..927
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   ACT_SITE        716
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT   BINDING         597..605
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   BINDING         623
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        47..165
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        82..92
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   936 AA;  105461 MW;  116F6C2E1991CC97 CRC64;
     WFFMVTLLDS RSVQGELAWV ASPTEGGWEE VSIMDEKNVP IRTYQVCNVM EASQNNWLRT
     HWIQRGPAQR VYIEIKFTLR DCNSLPGVTG TCKETFNLYF QETDSDSERT VRESRFAKID
     TVAADESFTQ VDIGDRIMKL NTEVRDVGVL TRKGFYLAFQ DVGACIALVS VRVFYKRCPL
     AVRNLAQFPD TVTGADTSSL VEVRGSCVDH SEEREVPKMY CGADGEWLVP IGNCLCNSGY
     EERNGQCQVC KLGYYRSLST DGGCSKCPLH SYSVREGATS CDCDKGYYRS ETDPPAMPCT
     RPPSAPQHLI SSVNETSVLL EWSPPLSSGG RQDLTYNVVC KQCVWEASRC VTCADTVRFS
     PQRLSLRTTR VSVHQLQAHT NYTFQIWAIN GVSKHNPNPD QAASISLTTN QAAPSTVMSV
     QSKDMTRDTL TLFWQEPEKP NGVILEYEVK YYEKEQNERS YRIVKTTSRT VSIKDLTPLT
     SYVFHVRART AAGYGDFSAP LEVMTNSVPS PVVGEGVSPT VLLLSAGGTI ILLLIFACTF
     IISKRRAKYS KAKQDEEKHQ PGVRVYVDPF TYEDPNQAIR EFAKEIDASC IKIEKVIGIG
     EFGEVCSGRL KFPGKREICV AIKTLKAGFT EQQKRDFLSE ASVMGQFDHP NIIHLEGVVT
     KCKPIMIITE YMENGSLDTF LRKNDGRFTV IQLVGVLRGI ASGMKYLSDM SYVHRDLAAR
     NILVNSNLVC KVSDFGMSRV LEDEPEGAYT TRGGKIPIRW TAPEAIAYRK FTSASDVWSY
     GIVMWEVMSY GERPYWDMSN QDVIKAIEEG YRLPPPMECP VALHQLMLEC WLRERSERPK
     FSQIVNMLDK LIRNPASLKR TGGETNRSHT HTYAYVHTSE TPPSLGLVEE WLKTISLEKY
     RENFITAGHS NLESIIHMNQ DSAHYHLLFS LEDSHL
//
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