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Database: UniProt
Entry: A0A3Q1FRR9_9TELE
LinkDB: A0A3Q1FRR9_9TELE
Original site: A0A3Q1FRR9_9TELE 
ID   A0A3Q1FRR9_9TELE        Unreviewed;      1018 AA.
AC   A0A3Q1FRR9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000019938.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000019938.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   AlphaFoldDB; A0A3Q1FRR9; -.
DR   STRING; 80966.ENSAPOP00000019938; -.
DR   Ensembl; ENSAPOT00000029949.1; ENSAPOP00000019938.1; ENSAPOG00000023492.1.
DR   GeneTree; ENSGT00940000156682; -.
DR   InParanoid; A0A3Q1FRR9; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd05032; PTKc_InsR_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_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; 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; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF106; INSULIN-LIKE GROWTH FACTOR 1 RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS50853; FN3; 3.
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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   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|PROSITE-ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200};
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   TRANSMEM        626..650
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..39
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          182..299
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          303..399
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          525..619
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          691..960
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          987..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         725
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1018 AA;  115405 MW;  CA7772E02FF6A980 CRC64;
     MPDCPSGFTR NETNRMLCSA CNGLCDKVCS SPVIDSVDAA QSLRDCTVIE GNLDINIRRG
     NNIASELESF MGLIQTVTGY VKIRHSHALG SLSFLKSLRY INGQELIDNM YSFSAINNQH
     LQSLWDWSQH NLTIRAGRLF FRRNPKLCMS EIHTMWEKTG ITVKPEEGDF RNNGERASCE
     SHILKFKSNV TSSHTIRISW ERYQPPDYGH LISFIVYYKE SPFQNITEFD GQDGCGSDSW
     HMVDVDLPQE KNTYPKVSLQ QLKPWTQYAI FVKAITLQVE DKHITGAKSD IIYIRTRPSL
     PSVPKDARAF ANSSTKLVVK WSPPVFPNGN LTYYLVRWQQ QPEDRELYQH NYCSKELKIP
     IRIPASGLSD MEDSTKPTKS DLAGAEKGPC CACQKTPEEK DREKDERIFF KVFENFLHNA
     IFLPRPPDRR RRDVFSVANN TLFPDGGRGN TSLGPGDNST DGVPPVREYP FLEDKSPAEF
     LEIGNLRPFT VYRIDIHACN EEVGHCSAGA FVFSRTKPAV KADDIPGKVI SERSDKIQGC
     VVLHWPEPVM PNGLILMYEI KYRLGNEKHG CVSRHQYREY KGARLTNLGS GNYSARVRAT
     SLAGNGSWTD SVFFYVPPPN HDGVTFYLVI IIPIIVILFI ASLTTILFFV NKKRNSDRLG
     NGVLYASVNP EYISAAEMYV PDEWEVAREK ITMHRELGQG SFGMVYEGIA KGVVKDEPET
     RVAIKTVNES ASMRERIEFL NEASVMKEFN CHHVVRLLGV VSQGQPTLVI MELMTRGDLK
     SHLRSLRKEV ILPPLKKMIQ MAGEIADGMA YLNANKFVHR DLAARNCMVA EDFTVKIGDF
     GMTRDIYETD YYRKGGKGLL PVRWMSPESL KDGVFTTMSD VWSFGVVLWE IATLAEQPYQ
     GMSNEQVLRF VMEGGLLDKP DNCPDMLFEL MRMCWQYNPK MRPSFLEIIS SIKDELDPPF
     REMSFFYSEE NKPPDTEELD MEVENMENIP LDPASTSTPL LGPVKNERAL PLPQSSAC
//
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