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Database: UniProt
Entry: A0A665VZ17_ECHNA
LinkDB: A0A665VZ17_ECHNA
Original site: A0A665VZ17_ECHNA 
ID   A0A665VZ17_ECHNA        Unreviewed;       952 AA.
AC   A0A665VZ17;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, 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=epha7 {ECO:0000313|Ensembl:ENSENLP00000037069.1};
OS   Echeneis naucrates (Live sharksucker).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Echeneidae; Echeneis.
OX   NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000037069.1, ECO:0000313|Proteomes:UP000472264};
RN   [1] {ECO:0000313|Ensembl:ENSENLP00000037069.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A665VZ17; -.
DR   Ensembl; ENSENLT00000038060.1; ENSENLP00000037069.1; ENSENLG00000013877.1.
DR   Proteomes; UP000472264; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05066; PTKc_EphR_A; 1.
DR   CDD; cd09548; SAM_EPH-A7; 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; 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:SF9; EPHRIN TYPE-A RECEPTOR 7; 1.
DR   Pfam; PF14575; EphA2_TM; 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; 2.
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; 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; 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; PS50105; SAM_DOMAIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000666-
KW   2}; Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000666-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472264};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..952
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025377968"
FT   DOMAIN          31..209
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          330..436
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          439..531
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          589..850
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          877..941
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   ACT_SITE        714
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT   BINDING         595..603
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   BINDING         621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        73..191
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        108..118
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   952 AA;  107082 MW;  D2FE419CEAF2334E CRC64;
     MLSRSNPCVW IIFCLYLCCC VDSGEAQNAK EVILLDSKAQ QTELEWISYP PNGWEEISGL
     DENYTPIRTY QVCQVMEPNQ NNWLRTNWIE KSDAQRIFVE LKFTLRDCNS LPGVVGTCKE
     TFNLYYQETD SEVGRSLREN QYVKIDTIAA DESFTQGDLG ERKMKLNTEV RIIGPLSRRG
     FYLAFQDVGA CIALVSVKVY YKKCWSIIEN LATFPDTVTG SEFSSLVEVE GVCVSDAEEE
     ADNSPKMHCS AEGEWLVPIG KCICKAGFHQ KGDACEPCGR GFYKSSSQDL QCSRCPAHSF
     NDREGSWRCD CEDGYYRGPS DPPSVACTRP PSAPQNLVYN INQTTISLEW SPPVDTGGRN
     DVRYRVICRR CSWEPEECVP CGLNVGYSPA QSELVETYVT ITDLLAHANY TFEVEAVNGV
     SDLSRTQRLF AAVSIATGQV SEVIKEKVQQ RSVQLSWQEP QQPNGVITEY EIKYYEKDQK
     NRIYSTVRSK STSATVNNLK PSTAYVFQIR AFTEAGYGTY GPTLEITTKE EATGKKMHCG
     YSKADQEGDE ELYFQFKFPG TKTYIDPETY EDPNRAVHQF AKELDASCIK IERVIGAGEF
     GEVCSGRLKL PGKRDVSVAI KTLKVGYTEK QRRDFLCEAS IMGQFDHPNV VHLEGVVTRG
     KPVMIVIEYM ENGSLDAFLR KHDGQFTVIQ LVGMLRGIAA GMRYLSDMGY VHRDLAARNI
     LVNSNLVCKV SDFGLSRVID DDPEAVYTTT GGKIPVRWTA PEAIQYRKFT SASDAWSYGI
     VMWEVMSYGE RPYWDMSNQD VIKAIEEGYR LPAPMDCPPG LHQLMLDCWQ KDRAERPKFD
     QIVGILDKMI RNPNTLKTPV GTCTSALVDD PNTPDFTAFR SVGEWLDAIK MERYRDNFTA
     AGYSSLESVA RMSIEDVMSL GITLVGHQKK IMSSIQTMRA QMLHLHGTGV QV
//
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