ID A0A3B3WU77_9TELE Unreviewed; 1052 AA.
AC A0A3B3WU77;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Receptor protein-tyrosine kinase {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000006332.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000006332.1}
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; A0A3B3WU77; -.
DR STRING; 48701.ENSPMEP00000006332; -.
DR Ensembl; ENSPMET00000006033.1; ENSPMEP00000006332.1; ENSPMEG00000007795.1.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
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; 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; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF16; EPHRIN TYPE-A RECEPTOR 10; 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; 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 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; PS50011; PROTEIN_KINASE_DOM; 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};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Receptor {ECO:0000256|ARBA:ARBA00023170}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1052
FT /note="Receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017288822"
FT TRANSMEM 573..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..205
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 326..435
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 438..531
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 651..907
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 942..1006
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 517..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 68..187
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 104..114
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 1052 AA; 116385 MW; E0A8A6920D0B7186 CRC64;
MDVCRTLAAL LWVLLLRRVQ VSQAEEVVLL NSKETQAELG WTSFPPNGWE EISGVDEKYK
PIRTYQVCNV MEPTQQNNWL QTGWVARRGG QRIFVELQFT LRDCNSIPGV AGTCKETFNL
LYVESDRDLG AVTREDRYSK IDTIAADESF TQGDLGERKM KLNTEVREIG HLNRKGFHLA
FQDVGACVAL VAVRVYYKRC LATVQNLAVF PDTVAEAAFA TLVEVRGGCV NNSEVDSDSP
PRMHCSAEGE WLVPIGKCSC SAGYEEGHSS CEACPPGSYK MSSRQQECFP CPANSVADEE
GSVVCVCEED HFRTPLDSPS TPCTRPPSPP RSLRFSLRQS SLVLDWDPPS DSGGRVDLTY
SVGCRRCGPA RCEPCGPGVG FVPQQVGLTE RTVTVVNLLP NTNYTFSVEA LNGVSDLLPS
KSFYTQVHVS TSLPPPSLIS ELRAEKVEEK SVMLVWREPP NPNRSRTEYE VKYYEKDQKD
QSYSTVKTAA TRIIVNNLKP GTTYVFLIRP FLTPAPSSSL SSSPLSSTSS TSASSSSSSS
SAPPPIDYGA FSAPLELQTL GELALASSEQ NPVVIIVIVS VAALIMLLSM GAGLLIWRRQ
CGYSKASQEG DEELYFQFKI PTRRTYIDPE TCEDLLQAVH AFAKELDQQS IKIERIVHTG
DFGEVCRGCL KLPSKRELPV AIRTLRAGCS DKQRRSFLSE AGILGQFDHA NIIRLEGVIT
TGNTMMIVEE SMTNGALDSF LRKHEGQLSV MQLMDMLTGV ASGMKYLTDM GFVHKRLAAH
KVLVNSNLTC KVSGFRPLQE EKIDSIYTTL HGGKSVVLWT APEAIQYRRF SSASDVWSFG
IVMWEVMSYG ERPYWDMGTQ DVIKAIEDGF RLPAPVNCPP HLHQLMLDCW QKERADRPGF
SQVHSALSKS VRSPDGIGSS TLARRTLSSS ISLAERPLPS FPSFSSVGEW LDAVDMGRYK
DNFTAAGYCY LESVARMTVQ DVLSLGVISL DHQKLILAAI QTLRAQVCRR RGVGSVRPRG
QTSRSWTPLP FLHPFFLFPR GGERRDPRSD VT
//
