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Database: UniProt
Entry: A0A3Q1D394_AMPOC
LinkDB: A0A3Q1D394_AMPOC
Original site: A0A3Q1D394_AMPOC 
ID   A0A3Q1D394_AMPOC        Unreviewed;      1165 AA.
AC   A0A3Q1D394;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000025476.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000025476.1}
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   -!- 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. EGF receptor subfamily. {ECO:0000256|PIRNR:PIRNR000619}.
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DR   AlphaFoldDB; A0A3Q1D394; -.
DR   STRING; 80972.ENSAOCP00000025476; -.
DR   Ensembl; ENSAOCT00000000105.1; ENSAOCP00000025476.1; ENSAOCG00000013304.1.
DR   GeneTree; ENSGT00940000156107; -.
DR   OMA; THEEVCP; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProt.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:UniProtKB-UniRule.
DR   CDD; cd00064; FU; 3.
DR   CDD; cd12095; TM_ErbB3; 1.
DR   Gene3D; 6.10.250.2930; -; 1.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR044912; Egfr_JX_dom.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR032778; GF_recep_IV.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR   PANTHER; PTHR24416:SF88; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-3; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 3.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 4.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000619};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000619};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000619, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000619};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000619};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000619};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000619}.
FT   TRANSMEM        589..615
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          659..916
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          988..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1003
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1033
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1037..1052
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         665..673
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT   BINDING         692
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1165 AA;  130164 MW;  5FD64F89E5B845B3 CRC64;
     ISPRPGLLQV CHGTQNGLSS TGSQENQYNL IKDRYDGCEI IMGNLEITQI ESNWDFSFLK
     TIREVTGYVL IAMNHFQELP LRQLRVIRGN SLYERRFALS VFFNYPKDGS NGLRQLGLTN
     LTDCLFLTSA DCISVSSSLS GPCHKSCGDY CWGPNEDQLT KTVCAPQCNG RCFGTSPRHC
     CHIECAAGCT GPLDVDCFAC RHFNDSGACV PQCPQTLIYN KQTFQMETNP NAKYQYGSIC
     VSQCPTHFVV DGSSCVSVCP LDKMEVEREG QRQCELCSGL CPKVCEGTGA EHRQTVDSSN
     IDSFINCTKI QGSLHFLVTG ILGDDFKNIP PLDAKKLEVF HTVREITDIL NIQSWPKELN
     DLSVFSSLTT IQGRSLYKRY SLMVMHIPTL TSLGLRSLRE ISDGSVYISQ NANLCYHHTV
     NWTQLFRGRR VGVNNLNNNR QLAECVAEGH VCDPLCSDSG CWGPGPDQCL SCRNYSRDGT
     CVGSCNFYTG VTREFASRKG ECVICHPECK PQRGKASCTG PGADECVACA NLRDGPYCMS
     SCPTGVNDGQ KGLIFKYPNR EGHCEPCHHN CTQGCSGPGL HDCLQTARMA ITGIALGVPA
     GLIFCLVLFF LGVLYHRGLA IRRKRAMRRY LESGESFEPL GPGEKGTKVH ARILRPSELK
     KIKALGLGVF GTVHKGFWTP ERETVKIPVA IKTIQDSSGR QTFTEITDHM LSMGSLDHPY
     IVRLLGICPG ASLQLVTQLS SQGSLLEHIR QHKNSLDPQR LLNWCVQIAK GMYYLEEHCM
     VHRNLAARNI LLKNDYQVQI SDYGVADLLY PDDKKYVYTD TKTPIKWMAL ESILFRRYSH
     QSDVWSYGVT VWEMMSFGAE PYASVQPQEV PSLLEKGERL SQPHICTIDV YMVMVKCWMI
     DENIRPTFKE LASDFTRMAR DPPRYLVIKV GSSNYFTSRI SQSTRRNSRL KNNLRLVVMN
     PSQEYEIMNT ECDALPCSAS SVSSHGDDPT AALCQNISPL PSPTEEKTHK ETLTPTSAVR
     SKQVQQACGG NVAEQKDSTE KPNRDFTNEI KSVDDQPEAS QGFGRYEYMD IRRSDVLTAR
     GEMLEEYEEM TRFRVVPGRW EHTEYQNLPA KGRDVSEEMG GGRCAGIGEY IKVCADMGEP
     GSNTSFDNPD YWHSRLFLKP DAVRT
//
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