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Database: UniProt
Entry: A0A6A5FIH2_PERFL
LinkDB: A0A6A5FIH2_PERFL
Original site: A0A6A5FIH2_PERFL 
ID   A0A6A5FIH2_PERFL        Unreviewed;       988 AA.
AC   A0A6A5FIH2;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   ORFNames=PFLUV_G00052510 {ECO:0000313|EMBL:KAF1389913.1};
OS   Perca fluviatilis (European perch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX   NCBI_TaxID=8168 {ECO:0000313|EMBL:KAF1389913.1, ECO:0000313|Proteomes:UP000465112};
RN   [1] {ECO:0000313|EMBL:KAF1389913.1, ECO:0000313|Proteomes:UP000465112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood {ECO:0000313|EMBL:KAF1389913.1};
RA   Roques C., Zahm M., Cabau C., Klopp C., Bouchez O., Donnadieu C., Kuhl H.,
RA   Gislard M., Guendouz S., Journot L., Haffray P., Bestin A., Morvezen R.,
RA   Feron R., Wen M., Jouanno E., Herpin A., Schartl M., Postlethwait J.,
RA   Schaerlinger B., Chardard D., Lecocq T., Poncet C., Jaffrelo L.,
RA   Lampietro C., Guiguen Y.;
RT   "A chromosome-scale genome assembly of the European perch, Perca
RT   fluviatilis.";
RL   Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAF1389913.1}.
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DR   EMBL; VHII01000005; KAF1389913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6A5FIH2; -.
DR   Proteomes; UP000465112; Chromosome 5.
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   CDD; cd10472; EphR_LBD_B; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05065; PTKc_EphR_B; 1.
DR   CDD; cd09552; SAM_EPH-B2; 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:SF11; EPHRIN TYPE-B RECEPTOR 2; 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; 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; 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; 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}; Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   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:UP000465112};
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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..988
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025676035"
FT   TRANSMEM        544..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..203
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          325..435
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          436..533
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          623..886
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          915..979
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   ACT_SITE        748
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT   BINDING         629..637
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   BINDING         655
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        63..185
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        98..108
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   988 AA;  110777 MW;  E4AE3D9CA2DB227C CRC64;
     MDIFMDMIRI LWILPTVWAV EEVLMDSTTA TAELGWTIYP SQGWEEVSGY DENMNTIRTY
     QVCNVFDSSQ NNWVRTKYIR RRGAQRIHVQ MKFSVRDCSS IPNVPGSCKE TFNLYYYESD
     SDTATKSSPA WMENPWVKVD TIAADESFSQ VDLGGRIMNI NSEIRSFGPV SRNGFYLAFQ
     DYGACMSLIA VRVFYRKCLS VIHNGAIFSE TLSGAESTSL VAARGVCVPN GEEVDVPIKL
     YCNGDGEWMV PIGRCMCKAG YEAVENGTVC RACVSGFFKA AQGDQQCLQC PINSRTTSEG
     ATNCVCRNGY YRADSDPPQM PCTTVPSAPQ NVISMVNETS LRLEWSPPQE AGGREDVVYN
     IICKSCGSGR GGCTRCGDNV QFVPRQLGLT DTRVHISDLL AHTQYTFEIQ AVNGVSDQSP
     YSPQYTSVNI TTNQAAPSAV SIIHQVSRSP DSITLSWSQP DQPNGLILDY ELQYYEKNQA
     EWNSSLTRSQ TNTAVIRGLK PGTIYVFQVR ARTVAGFGRF SGKMYFQTMT EEEYKSSIQE
     KLPLIIGSTA AGLVFIIAIT VLIIVCRSRR SPERSESEYT DKLQHYTSGH MSPGMKIYID
     PFTYEDPNEA VREFAKEIDI SCVKIEQVIG AGEFGEVCSG NLRQPGKREI LVAIKALKAG
     YTERQRRDFL SEASIMGQFD HPNIIHLEGV VTKSSPVMII TEFMENGSLD SFLRQNDGQF
     TVIQLVGMLR GIAAGMKYLC DMNYVHRDLA ARNILVNSNL VCKVSDFGLS RFLEDDTSDP
     TYTSALGGKI PIRWTAPEAI QYRKFTWSSD CWSYGIVMWE VMSYGERPYW DMSNQDVINA
     IEQDYRLPPP MDCPTALHQL MLDCWQKDRS NRPKFSQIVS TLDKMIRNPS SLKAMTPLSS
     SVHLPLLDRT TPDFSSFSTV EEWLDAIKMG QYKENFANED FSSFDVVSKM TMEDIVRVGV
     TLAGHQKKIL NSIQSMRAQM NQITSVEV
//
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