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Database: UniProt
Entry: A0A674PI18_TAKRU
LinkDB: A0A674PI18_TAKRU
Original site: A0A674PI18_TAKRU 
ID   A0A674PI18_TAKRU        Unreviewed;       960 AA.
AC   A0A674PI18;
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=LOC101068187 {ECO:0000313|Ensembl:ENSTRUP00000085273.1};
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:ENSTRUP00000085273.1, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000085273.1, 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:ENSTRUP00000085273.1}
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; A0A674PI18; -.
DR   Ensembl; ENSTRUT00000065539.1; ENSTRUP00000085273.1; ENSTRUG00000018413.3.
DR   GeneTree; ENSGT00940000155297; -.
DR   Proteomes; UP000005226; Chromosome 20.
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:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05065; PTKc_EphR_B; 1.
DR   CDD; cd00185; TNFRSF; 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; 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; 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; PF07647; SAM_2; 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}; Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
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};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226};
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   DOMAIN          1..182
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          301..412
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          413..506
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          591..854
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          886..950
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        39..164
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        74..84
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   960 AA;  106872 MW;  61039979C538F60F CRC64;
     MDTRTATAEL GWISFPANGW EEVSGYDENL NTIRTYQVCN VFEPSQNNWL LTTYIDRRAA
     QRIYVEIRFT VRDCASIPSV LGSCKETFNL YYLETDRTVS ESIKGVEYWA NAPFLKVDTI
     AADESFSQVD FGGRLMKVNT EVRSFGPLSK GRGFHLAFQD LGACMSILAV RVFYKKCPSV
     VQNFAYFPET LTGAESTSLV IARGSCISNA EEVDVPIKLY CNGDGEWMVP IGSCSCKAGY
     EPDNSNVCRA CPQGTFKSFQ GAGLCQQCPP NSRSTIEAAT LCSCRNGYYR GDMDRPEDVC
     VPSAPRNVVS VINQTSVLLE WHSPRDTGHR DDLSYNVLCR RCHSAERRAC QPCDDSVKFV
     PGKRGLKETQ VEISKLRAHT SYTFIIQATN GVSNKSPYPA QQLSINITTN QAAPSVVPIM
     HQVSSTSRSF SLSWPPPEQP NGIILDYEIR FYDKTLLNSS VVQSQTPGVV LEGLRPGTGY
     VVQVRARTVA GYGAYSKDML FQTLTDDEYK SELGQQLSLI AGYLVGGVCI VSLIVALRPD
     MFSGPTPTVT FPTRSEGHSS PGVKIYIDPF TYEDPNEAVR EFAKEIDPSC VKIEEVIGSG
     EFGEVYKGRL KPIGKKEIPV AIKTLKVGYS ERQRRDFLSE ASIMGQFDQP NIIRLEGVVT
     KSRPTMIITE FMENGALDSF LRQNDGQFSV IQLVGMLRGI ASGMRYLAEM SYVHRDLAAR
     NILVNSNLVC KVSDFGLSRY LEEDASDSTY TSSLGGKIPV RWTAPEGIAY RKFTSASDVW
     SYGIVTWEVM SYGERPYWDM SNQDVINAIE QDFRLPAPMD CSVVLHQLML DCWQKDRNAR
     PKFPDIVSML DKMMRNPTSL KTETRVIQTY SPSHHPLLDR GAPDLSSISS VEDWLAALKM
     TQYRDSFLGS GFTSLPLVTQ ITAEDLQRIG VSLAGHQKKI LTSVQLMRHN VDDQSPTESV
//
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