ID A0A3B3UYM0_9TELE Unreviewed; 1113 AA.
AC A0A3B3UYM0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000017776.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000017776.1}
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A3B3UYM0; -.
DR Ensembl; ENSPLAT00000027103.1; ENSPLAP00000017776.1; ENSPLAG00000022777.1.
DR GeneTree; ENSGT00940000155404; -.
DR Proteomes; UP000261500; 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 CDD; cd00063; FN3; 3.
DR CDD; cd00064; FU; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.80.20.20; Receptor L-domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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 PANTHER; PTHR24416:SF535; INSULIN RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF01030; Recep_L_domain; 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; 1.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 419..515
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 630..724
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 783..1029
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 479..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 817
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1113 AA; 126359 MW; 85960C183DA0A127 CRC64;
YCFWLFLFWV FKISVLSVCL CGLILTNFFL FCFSSACDNC KNGACSRQGQ CCHEQCLGGC
SEPGNATSCV ACRNLQHGNI CMDKCPPGYY VFQGWRCVSF SFCQDLHNQC KKSKNLDANC
HEYVIHNGAC IQECPSGYMS SFTHRLQQLH VLSFFVLHNR LCLAANSTVL LLAANIAAEL
EASLGQIEVI KGYLSIRRAY ALVSLSFLRK LHTIKGEQLE ADSYAFYALD NQNLRQLWDW
SKHNLTIERG RTFFHFNSKL CMSEIRKLEE VTGTKERNQK NDIAARTNGD QASCEMQLLN
FTSVKVRANM IILKWNSFWP SDYRDLLGFM VLYKEAPYKN VTEFDGQDAC GSNSWVIADV
DPPPRANQED PGYLIRSLKP WTQYAIMVRT QLSASDEHQV HGAKSNIMYV RTDASKPSGP
LDPISSSNSS SQIILKWKPP TSPNGNITHY RVICHKQEED SDLYKFDYCL QGMKLPSRTP
THLDSEDEQK WNRTEEPNSG GGCCTCPKTK MELEKQQKEI AYRKTFEDYL HNVVFESKQS
RPRRSVENPE PVESTHFYST MSSLQTTTAS YKEEEKDDKV SESTVISNLQ HFTSYKIEII
ACNHPTEPNR CSMATYVSAR TMPELKADDI PGPVTHEIVN EEPPHVLVKW HEPPSPNGLI
ILYEVTSNYP HSICVSRLSY EKFGGTKLTL LQPGNYSVVV RATSLAGNGS FTETTYFFMP
TLIVSAPIVS SILLLLRLTC FLRLFYRQTE GPLGDLITSP NPEYFSANDM YVPDEWEVPR
EKITLLRELG QGSFGMVYEG IAQDIVKGEP ETRVAVKTVN ESASLRERIE FLNEASVMKA
FNCHHVVRLL GVVSKGQPTL VVMELMTHGD LKSYLRSLRP DSENNPSGSP PPTLKDMLQM
AAEIADGMAY LNAKKFVHRD LAARNCMVAE DFTVKIGGPC WFFSERRRVH RSFGVVLWEI
STLAEQPYQG LSNEQVLKFV MDGGFLDRPD NCPERMHSLM QMCWQYNPKM RPTFLEIIEM
LRDDLHPTFQ EVSFFYSEEN KVPETEDFDL DLDNMESIPL DPSSYSQREE SLSRDSGPSV
ALRGNYEEHV PYTHMNGGKK NGRILSLPRS SPS
//
