ID A0A3P8QTP7_ASTCA Unreviewed; 1341 AA.
AC A0A3P8QTP7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000032454.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000032454.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000032454.1}
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 Ensembl; ENSACLT00000033219.1; ENSACLP00000032454.1; ENSACLG00000021919.1.
DR GeneTree; ENSGT00940000156682; -.
DR Proteomes; UP000265100; Chromosome 7.
DR Bgee; ENSACLG00000021919; Expressed in muscle tissue and 5 other cell types or tissues.
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:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
DR CDD; cd00064; FU; 1.
DR CDD; cd05032; PTKc_InsR_like; 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; 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:SF106; INSULIN-LIKE GROWTH FACTOR 1 RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00757; Furin-like; 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; 1.
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; 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|PIRSR:PIRSR000620-
KW 2}; Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000620-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 917..941
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 468..587
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 591..687
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 813..909
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 982..1255
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1285..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1116
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT BINDING 992
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1016
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1063..1069
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1120..1121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ SEQUENCE 1341 AA; 152474 MW; 8992C484C0D6C0EA CRC64;
MKKTVKIFFL CVAVCGPDID LRNDIDQFKR LENCTVVEGY LRILLINEKT SNNSQQEDFR
SVSFPKLTVI TGYLLLFRVS GLDSLSVLFP NLSVIRGHNL FYNYALVIYE MTSLKDIGLY
NLRNITRGAM RIEKNPELCY LDSVDWSFIM NTEFNNVING NKKAKECDNV CPGIMEDNPL
CQQTTFNDNR NYRCWTSNHC QKVCPKQCRL ACTDKGECCH NQCLGSCTEP NNDMSCSACL
HYYHEGRCVP NCPPGTYKFE GWRCITMELC AQVHLASDFH FVIHDGECML DCPSGFTRNE
TNRMLCSACN GPCDKVCRST VIDSVNAAEF LQDCTVIDGN LDINIRRGNN IAPELERFMG
LIQTVTGYVK IRHSDALGSL SFLKSLRYIK GQELIDNMYS FSAINNQNLK YLWNWTEHNL
TISSGRLFFR QNPKLCMSEI YKMWDKTGIA VKPEEGDFRN NGERANCESH ILKFKSNITS
SHVINLTWER YQPPKNGTLI SFIIYYKESP FQNITEFDGQ DGCGSNSWHM VDVDLPKDNN
NDPNVRLQHL KPWTQYAIFV KAITLQESDK DATGAKSDII YIRTHPSLPS VPKDARAYGN
SSTKLVVKWS PPLLPNGNLT YYLVRWQRQA EDRELYQHDY CSKDLKIPIR IPASELTDME
ENTKPTKSDL AGPEKVLCCA CQKTPEEKDR EKDDRVFLKV FENFLHNSIF LARPQERRRR
DLSGTANNTL FYEGGRGNTT LGAGDNSTDG IPPNVEFPFT EDKSTTEYLE IPNLRPFTVY
RIDIHACNEV VGKCSAGAFV FSRTKPAVKA DDIPGKVIFE RCDKIEGCVV LHWPEPVMPN
GLILMYEIKF RLGNEVSWTG CVSRQDYRRY KGARLTNLGS GNYSARVRAT SPAGNGSWTE
SVFFYVSPPK RDDGVTLYVV IIIPIIVTIF VAGLITILFY VNKKRNSDRL GNGVLYASVN
PEYLSATEMY VPDEWEVARE KITMHRELGQ GSFGMVYEGI AKGVVKDEPE TRVAIKTVNE
TASMRERIEF LNEASVMKEF NCHHVVRLLG VVSQGQPTLV IMELMTRGDL KSHLRSLRKE
VSNLQVLPPL KKMIQMAGEI ADGMAYLNAN KFVHRDLAAR NCMVAEDFTV KIGDFGMTRD
IYETDYYRKG GKGLLPVRWM SPESLKDGVF TTMSDVWSFG VVLWEIATLA EQPYQGMSNE
QVLRFVMEGG LLDKPDNCPD MLFELMRMCW QYNPKMRPSF LEIISSIKDE LDPPFREVSF
FYSEENKPPD TEELDMEVEN MENIPLDPSS VRQPSTHSGH ASANGPVVVL RPSFDEIQPY
AHMNGVRKNE RALPLPQSSA C
//
