ID A0A3Q1CS60_AMPOC Unreviewed; 1287 AA.
AC A0A3Q1CS60;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
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:ENSAOCP00000021906.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000021906.1}
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,
CC ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily.
CC {ECO:0000256|RuleBase:RU000311}.
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DR Ensembl; ENSAOCT00000009358.1; ENSAOCP00000021906.1; ENSAOCG00000007108.1.
DR GeneTree; ENSGT00940000164144; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR InterPro; IPR041348; VEGFR-2_TMD.
DR PANTHER; PTHR24416:SF552; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF21339; VEGFR-1-like_Ig-like; 1.
DR Pfam; PF17988; VEGFR-2_TMD; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 2.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 5.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 3: Inferred from homology;
KW Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000311};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 28..109
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 196..296
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 404..519
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 528..613
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 625..710
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 789..1119
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 925..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 983
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 766
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 823
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 988
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1001
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 1287 AA; 143907 MW; D222B5465E0DD903 CRC64;
GCGRRETTKA LVCWGPLWID LKDVIFILHC FSLSSVRGHG VLHWTLADGQ RSIPSERVKV
EHCNSRHHSH LQCSKLTVTH LSANDTGSYS CKYSKAGSDH ITSTYVYVTD PEQPFVEPHD
PIPYFLGIYR HETSLVVPCR TSSPNATVLL IGEIINGKVW DPKVGFKIPY GPYTAYSMLT
CTTVVNGREF QSVYIPQRQT LVLNNVKITP ERVRVLVGDT LKLNCSGETT YNGRINFTWD
FPKRRENRHY TEKPKLKPEH VLVMSKTLVL PNITMEDRGV YRCKAELEPT KHKNASAKVI
VFEHPFLNVS YRYERQSTIV VNEGRRKLVF EPKVNALPVP DLIAWYKDGV LIQKNSTCYK
MSSFSLAITD VQPKHAGIFT ISLGNRLKGL YRNLSYTLVV DVKPTISEAE LATVDMQPYM
SGKQQQLTCT AYGLPLPTIT WLWQPCNSDP TCLAYTAPVQ VNTDDRSNNA QNWIKSIIVK
PELVKGKNKT ASTLVIGEAR VSGKYSCVAQ NEDGTSTMTM PFYVDDHPEE ITIEPHTAIE
GDDITLTCRA TRYLYTDLQW LDSTNQTVTS NVSSLQLSRY SVSLSLHLYN VSQNSAAGYK
CQAYKLHKKT EIKTAALIVD ARKRPWLSQN LTNQDVNSSS TLVLACYASG VPQPYIIWYK
NGARVEESPG ITLGEDGALT IERVKKDDEG LYECVASNVE GVAKTSAVVT VLGDEGKPNV
EVIILVCTGA AATFLWLMLI LFIRKLRKQP AHYKMGPSII IDPDEYPLDE QNDLLQYDSS
KWEFPRDRLR LGKTLGHGAF GKVVEASAFG IDKLSTCKTV AVKMLKGGAT SNERKALMSE
LKILIHIGHH LNVVNLLGAC TKPGGPLMMI VEFCKYGNLS NYLRGKRDDF IVYKSQDGKV
VSSGSGCQLS ELMKRRLESV ASTGSSASSG FIEDKSYCDS EEEEEESEDL YKRVLTLEDL
ICYSFQVAKG MEFLASRKCI HRDLAARNIL LSENNVVKIC DFGLARDIYK DPDYVRKGDA
RLPLKWMAPE AIFDKIYTTQ SDVWSFGVLM WEIFSLGASP YPGVQIDEEF CCRLKEGTRM
RAPEYSSSEI YQTMLDCWQG EPQERPTFTE LVERLGDLLQ ASVQQEGKHY IPINTALLAK
VGDQTTTVIS EETPTRPVSH RDSGSTWNIK IRPASVKTFD EVTMENGTDE NHEGQSDSGM
GLSSDNMKTL MRFESLAGRP LSIMALAMKA VSKSKESVLS DAEKEKYPST VPPLDLSLDD
SALDASLECH SPPPDYNYVV RYSTPPV
//
