ID A0A3B4GPV7_9CICH Unreviewed; 1193 AA.
AC A0A3B4GPV7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|PIRNR:PIRNR000619};
DE EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000619};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000023518.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000023518.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: In the nucleus is involved in transcriptional regulation.
CC Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter
CC and activates its transcription. Implicated in transcriptional
CC activation of CDKN1A; the function involves STAT3 and SRC. Involved in
CC the transcription of rRNA genes by RNA Pol I and enhances protein
CC synthesis and cell growth. {ECO:0000256|ARBA:ARBA00037619}.
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: Cell projection, ruffle membrane
CC {ECO:0000256|ARBA:ARBA00004199}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004199}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {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; A0A3B4GPV7; -.
DR Ensembl; ENSPNYT00000024091.1; ENSPNYP00000023518.1; ENSPNYG00000017639.1.
DR GeneTree; ENSGT00940000158232; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0032587; C:ruffle 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: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; cd12087; TM_EGFR-like; 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; 2.
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:SF137; RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2; 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; 2.
DR Pfam; PF01030; Recep_L_domain; 2.
DR Pfam; PF21314; TM_ErbB1; 1.
DR PIRSF; PIRSF000619; TyrPK_EGF-R; 2.
DR SMART; SM00261; FU; 3.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
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 616..637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 682..973
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 933..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..958
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 807
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-1"
FT BINDING 688..696
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2"
FT BINDING 715
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1193 AA; 131737 MW; 06DC08AB38DA6231 CRC64;
MHSETLFFCR GTDMKLALPS SLENHYETLR LLYTGCQVVH GNLEITHLHG NPNLSFLQGI
VEVQGYVLVA HVSVSLLPLD SLRIIRGSQL YNSSYALAVL DNTHAGQGLR TLRLRSLTEI
LLGAVYIWGN PQLCFPDPQN INLTDILDEQ NGRAKEHRLQ PRPPNCPSCS PACGKRCWGE
TPQDCQTLTR AKCASGCQRC KGPLPNDCCH LQCAAGCTGP KDSDCLACRH FNDSGVCKEN
CPLPTTYDPV TFQSQSNPHG KFNFGATCVK TCPYNYLALE VACTLSCPPN NQEVVVTQPD
GTETQKCDKC EGDCPKGEVV ILIAVVTPSN VEEFNKCTKI FGSLAFLTFY LFLTPKSPEL
ECFHHLCVIF KLAGYLYIDA WPEQWTNLSV FENLKVIRGT MLYKGVFSLA IQNLHIESLG
LRSLRSVSGG LVLIYNNTQL CYTNSLPWQN LLHPTQGPHR IVSHNQDPAV CEKEGNVCHP
LCKAGCWGPG PSQCVSCQTF QRGTECVDLR AFVECVACDP QCRPLNGSES CHGPGAQHCT
ECRNFQDGEY CVDRCPSGVK GDLHTVWKYS NATGHCLPCK TNLRLTSQTV LFSSSCTVKD
EQGCPIDTRT GPGTSIAAAV GGVVLFIILL ALLVFYLRRQ KKLKRKETMR RILQEHELVE
PLTPSGASPN QAQMRILKET ELKKLRVLGS GAFGTVYKGI WAPDGENVKI PVAIKVLREN
TSPKANKEIL DEAYVMAGVA SPYVCRLLGI CLTSTVQLVT QLMPYGCLLD YVRENKDRIG
SQFLLNWCVQ IAKGMSYLEE VRLVHRDLAA RNVLVKNPNH LMTFGSKPYD TIPARDIPEV
LEGGERLPQP LICTIDVYMI MVKCWMIDPE SRPRFKGLVN DFSAMARDPT RYVVIQNDEE
MSKCSPVDSE FYRMLLREDE NIVEMMDPEE YLVPNTRKGD EPQANGLSRH HRDHSLDMDP
SNTAGPRNLH SSLTGISHAQ YPTLTMGASA SNSVWPQYPM LARSTSAGGQ SDSVFLDAPT
DGHSLAPASP GRYSKDPTFP NGSKDDLETD GWSGFPHPYL HHSLPRRSHA IQNHPLPEYV
NQEIQDLRPG FPERPSTLPR KSRIDRRLPN GLSSGHSVEN PGYLIPVNST SPAFDNPYYL
DLGPKAIPGA VAGDGPAGLE SNGGVTRHMN GFVTPTAENP EYLGLADTWS GNT
//
