ID A0A3B5KHQ5_TAKRU Unreviewed; 985 AA.
AC A0A3B5KHQ5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
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=ephb4 {ECO:0000313|Ensembl:ENSTRUP00000054907.2};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000054907.2, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000054907.2, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000054907.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A3B5KHQ5; -.
DR STRING; 31033.ENSTRUP00000054907; -.
DR Ensembl; ENSTRUT00000054814.2; ENSTRUP00000054907.2; ENSTRUG00000016825.3.
DR GeneTree; ENSGT00940000166305; -.
DR InParanoid; A0A3B5KHQ5; -.
DR OMA; CGRDLTF; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000005226; Chromosome 15.
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:0035475; P:angioblast cell migration involved in selective angioblast sprouting; IEA:Ensembl.
DR GO; GO:0060026; P:convergent extension; IEA:Ensembl.
DR GO; GO:0001945; P:lymph vessel development; IEA:Ensembl.
DR GO; GO:0048845; P:venous blood vessel morphogenesis; IEA:Ensembl.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05065; PTKc_EphR_B; 1.
DR CDD; cd09554; SAM_EPH-B4; 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; IPR037636; EPH-B4_SAM.
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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF11; EPHRIN TYPE-B RECEPTOR 2; 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; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 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; 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, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..985
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025411770"
FT TRANSMEM 542..567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..206
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 328..438
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 439..536
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 619..882
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 916..976
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 744
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 625..633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 651
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 106..115
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 985 AA; 110238 MW; 468AF338F504FB75 CRC64;
MELTHWSVFF LPCIFLHWTL RTSAEEEVLM NTKTETSDLK WTIYSTSKPE WDEVSGLDEE
NNSVRIYQIL SCQTGSSTSH WLRSGFIQRQ GASQVYVELR FTMMECSSST HHRSCKETFN
LFYYQTDSDD ATYSYPPWME NPYTKVDTVA ADFLLREGGE RKFNMKTFKL GPLSKRGFYL
AFQAQGACMA LLSVRVFFKK CPALVSALSS FPETVPRTLV QEAQGVCVEQ AAQQGPRPRP
PKLFCGEDGH WVGQPTTSCA CLPGFEPAEG HTRCRACPMG QFKWGTEGQC TNCPGFSYAT
TRGASVCACR SGYLRAKSDA LDTPCTKPPS APRSIVTQMN DSTLSLEWNE PLESGGRTDL
SYSVRCTVCR AAGTPCLSCG DSVSYRPAQH GLVERRVEVW GLLPQATYIF TIQALNGVSQ
LSGKEAASKS VNITTTHDVP SLVSLIQRID STESSLTLHW SVPDHPRYTI LRYQIRYCEK
QERRSEDQCH HTESNRNQAV LTDLRRATPY EVQVRVHTAA GYGSFSPATV FHTLPDGQDS
QFLLPGILIA AGILLLVTFI FVAAYCIRKH SRAKDSELGD KNNQYLVGQG IKVYIDPFTY
EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVCRGRLKI PGKKENYVAI KTLKGGYTDK
QRRDFLSEAS IMGQFQHPNI IHLEGVITAS CPVMILTEFM ENGALDSFLR LNDSQFTPIQ
LVGMLRGIAS GMKYLSEMSY VHRDLAARNI LINSNLVCKV SDFGLSRFLQ ENSSDPTYTS
SLGGKIPIRW TAPEAIAFRK FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD
YRLPPPPDCP THLHQLMLDC WQKDRSARPR FADLVSALDK LIRNPPSLKI VAQDGVGPSY
PLLDQRAPLA LSGCASVGEW LRAIKMERYE DSFLQAGLST VDQLAQISTQ DLLHMGVTLA
GHQRKILSSI QTMTFRNKST TTVTF
//
