ID A0A3Q3EAY2_9LABR Unreviewed; 1205 AA.
AC A0A3Q3EAY2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
GN Name=ERBB4 {ECO:0000313|Ensembl:ENSLBEP00000003216.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000003216.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000003216.1}
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; A0A3Q3EAY2; -.
DR STRING; 56723.ENSLBEP00000003216; -.
DR Ensembl; ENSLBET00000003387.1; ENSLBEP00000003216.1; ENSLBEG00000002429.1.
DR GeneTree; ENSGT00940000154695; -.
DR InParanoid; A0A3Q3EAY2; -.
DR Proteomes; UP000261660; 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:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProt.
DR CDD; cd00064; FU; 3.
DR CDD; cd12092; TM_ErbB4; 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; IPR049328; TM_ErbB1.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR PANTHER; PTHR24416:SF90; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-4; 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 Pfam; PF21314; TM_ErbB1; 1.
DR PIRSF; PIRSF000619; TyrPK_EGF-R; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 5.
DR SMART; SM00219; TyrKc; 1.
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.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 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:UP000261660};
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|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000619}.
FT TRANSMEM 623..645
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 688..955
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 813
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-1"
FT BINDING 694..702
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT BINDING 721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1205 AA; 135444 MW; CCBE17333D501D61 CRC64;
MLSLLFPVCA GTENKLSTLS DLEQQYRTLR KYYESCEVVM GNLEITSIDR SRDLTFLRSI
REVTGYVLVA LNQFDYLPLE NLRIIRGTKL YEDRYSLAIF LNYRRDGNFG LRQLGLKNLT
EILSGGVYVD KNKFLCHADT IHWQDIVKNP RQHSVVVPTN SSVTCQKCHR SCNGRCWGPK
EDQCQSLTKT VCAEQCDGRC FGPYVSDCCH RECAGGCYGP KDTDCFACTN FNDSGACVTQ
CPQPFVYNPT TFQLEHNPRA KYSYGAFCVK KCPHNFVVDH SSCVRACPSN KMEVEENRIK
MCIPCTDICP KACDGIGTAS LQTAQTVDSS NIDKFVNCTK INGNLVFLIT GIKGDVYHNI
EALDPEKLNV FRTVREVTGF LNIQSWPDNM TDLSVFSNLV TIGGRALYSG ISLLVLKQQG
ISSLQLQSLR EISAGNVHIA ENSQLCYYNT VNWTRLFRAA NQKVLIRNNR SPQGCSAKHR
MVCDPLCSDA GCWGPGPDQC LSCRYYSRGR TCVDMCNLYE GDIREYANGS VCVECDAQCE
RADNNSLICN GPGPEHCVKC LHFKDGPNCV EKCPDGLQGA NSFIFKYAEA NNECHPCHSN
CTQGCIGPRL QDCIGWMDRT PLIAAWVIGG LFMVVIMVLS VAVSVRRKNI KKKRALRRFL
ETELVEPLTP SGTAPNQAQL RILKETELKR VKILGSGAFG TVYKGIWIPE GETVKIPVAI
KILNEATGPK ANVEFMDEAL IMASMEHPHL VRLLGVCLSP TIQLVTQLMP HGCLLDYVHE
HKDNIGSQLL LNWCVQIAKG MMYLEERRLV HRDLAARNVL VKSPNHIKIT DFGLARLLDV
NEKEYNADGG KMPIKWMALE CIHYRKFTHQ SDVWSYGVTI WEVMTFGGKP FDGISTRDIP
DLLEKGERLP QPPICTIDVY MVMVKCWMID ADSRPKFKEL AAEFTRMARD PQRYLVIQGD
DRMKLPSPND SKFFQSLLDE EELEDLMDAE EYLVPHSFNI PPLAYTPRTR IDSNKVLSIN
HATFSCLKND ISTLKTVLVL GAPLFNANPT IPFLFPDYLN PVEENPFVTR RRNGDAHSAI
NGAGCHTLHM PGAAIATKNQ SSHGDDEYVN EPLYLNTLLN QGDKNGLKGK KATFDNPEYW
QHSLPPKSSL HNPEYLQDCS TRFFYRQNGR IRPAVAENQE YLSEAAMKAG NVLPPPPYRQ
RNTVV
//
