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Database: UniProt
Entry: A0A3P8RPH4_AMPPE
LinkDB: A0A3P8RPH4_AMPPE
Original site: A0A3P8RPH4_AMPPE 
ID   A0A3P8RPH4_AMPPE        Unreviewed;      1369 AA.
AC   A0A3P8RPH4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000001400.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000001400.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000001400.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001171,
CC         ECO:0000256|RuleBase:RU000312};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily.
CC       {ECO:0000256|RuleBase:RU000312}.
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DR   STRING; 161767.ENSAPEP00000001400; -.
DR   Ensembl; ENSAPET00000001433.1; ENSAPEP00000001400.1; ENSAPEG00000000991.1.
DR   GeneTree; ENSGT00940000155404; -.
DR   Proteomes; UP000265080; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043560; F:insulin receptor substrate binding; IEA:InterPro.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043009; P:chordate embryonic development; IEA:Ensembl.
DR   GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR   GO; GO:0006096; P:glycolytic process; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd00064; FU; 1.
DR   CDD; cd05061; PTKc_InsR; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR040969; Insulin_TMD.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-dom_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; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF535; INSULIN RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF17870; Insulin_TMD; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000620; Insulin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00261; FU; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000620-2, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000620-2, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000312};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1369
FT                   /note="Tyrosine-protein kinase receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018240114"
FT   TRANSMEM        945..970
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          622..722
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          844..941
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1009..1285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          556..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1315..1369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1315..1329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1146
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT   BINDING         1019
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1043
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1090..1096
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1150..1151
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ   SEQUENCE   1369 AA;  154455 MW;  FEC893901FA721A2 CRC64;
     MRLKLRAQMV FFIICTCIIC QCGLINGEIC QSKDIRNNVT NLQSLENCTI IEGHLKILLM
     FKTKTDDFRG LSYPKLRVVT DYVLLFRVYG LETLSELFPN LTVIRGNNLF FNYALVLYEM
     LQLKEVGLHS LMNITRGAVR IEKNPDLCYL ATLDWSKILD SVEDNFIVAN KNERECGDVC
     PGTAQGQTVC SQSTINGHFR GRCWTQNHCQ RMCLDNCKHG ACSLQGQCCH DQCLGGCSEP
     GNASSCVACR NLQHGNTCVE KCPPGYYVFR GWRCVSFNFC QELHNQCKQT KKLNQDRESG
     CYEYVIHNGA CIQECPSGYT TITSTTLTCS PCAGLCPKLC VGNKTIDSVT SAQALRGCTV
     LHGNMIIKIR GGNNIAAELE ASLGQIEEIT GYLTVRRAYA LVSLSFLRKL RIIRGEHLEG
     DSYAFYALDN QNLRELWDWS KHNLTIQRGR MFFHYNSKLC MSEISKMEQV TGTKERNQKN
     DIAVRNNGDQ ASCETKLLKF NLIKTTSNMI MLKWEQFWPL DFRDLLGFMV LYKEAPYKNV
     TEFDGQDACG SNSWAIADVD PPSRPTEGKK GEDPGHLIRP LKPWTQYAIM VKTQLSASDE
     HQVHGAKSEI IYVRTNASKP SVPLDPISSS NSSSQIILKW KPPTSPNGNI THYRVICRKQ
     PEDSDLYKFD YCLQGMKLPS RTPTHLDSED EQKWNHTDEP TSGGKCCACP KTDSQLKKEQ
     EEIEYRKTFE NYLHNEVFES RPSRRRRSVG VANATLPPLF LTTIPSLQFG STTATPEDED
     EDQEGSKVEL KVFSKESTVI SNLHHFTSYK IEIMACNHPT DLKRCSMATY VSARTMPEEK
     ADDIPGPVTH EIVMAEPPYV LIKWNTPKSP NGLIILYEVF YRKVGDTEDH TACVSRPAYI
     KSGGTKLSLV QPGNYSVRVR ATSLAGNGSF TETTYFFMPN PDQGLIWIVI GPVICFILLL
     FVAGGVFVIF KKRQTAGPLG DLITSPNPEY FSANDMYVPD EWEVPREKIT LLRELGQGSF
     GMVYEGIAKD IVKGDPDTRV AVKTVNESAS LRERIEFLNE ASVMKAFSCH HVVRLLGVVS
     KGQPTLVVME LMTHGDLKSY LRSLRPDSEN NPSGCPPPTL KDMLQMAAEI ADGMAYLNAK
     KFVHRDLAAR NCMVAEDFTV KIGDFGMTRD IYETDYYRKG GKGLLPVRWM APESLKDGVF
     TAHSDCWSFG VVLWEISTLA EQPYQGLSNE QVLKFVMDGG YLDRPENCPE RMHNLMQMCW
     QYNPKMRPMF HEIIEMLRED LHPSFQEVSF FYSEENKVPE TEEFDLDLDN MESIPLDPSS
     YSQRAESLGR DSGPSVALRG NYEEHVPYTH MNGGKKNGRI LSLPRSSPS
//
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