ID A0A3B1KJH3_ASTMX Unreviewed; 1242 AA.
AC A0A3B1KJH3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Vascular endothelial growth factor receptor 3 {ECO:0000256|ARBA:ARBA00022258};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000054842.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000054842.1}
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: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC 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 AlphaFoldDB; A0A3B1KJH3; -.
DR Ensembl; ENSAMXT00000034736.1; ENSAMXP00000054842.1; ENSAMXG00000001322.2.
DR GeneTree; ENSGT00940000159358; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000001322; Expressed in camera-type eye and 14 other cell types or tissues.
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 CDD; cd00096; Ig; 1.
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; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR PANTHER; PTHR24416:SF49; VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 3; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 1.
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; 3.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR PRINTS; PR01835; VEGFRECEPTR3.
DR SMART; SM00409; IG; 5.
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; 6.
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, ECO:0000256|SAM:Phobius};
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:UP000018467};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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 ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1242
FT /note="Vascular endothelial growth factor receptor 3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017305167"
FT TRANSMEM 749..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..121
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 254..340
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 351..436
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 445..573
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 580..674
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 695..733
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 818..1146
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 944..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1010
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 852
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1015
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1028
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 1242 AA; 140576 MW; 2220630C37D99CD5 CRC64;
MKRESRVFCG IWIGLASFSG LVAGFSMTPP TIDSTKDQLV IDANDTLTIT CRGQLILDWA
WPEQSLSKVE LSEREGQQLI THSEDQRVLW VRECQGQPGK PYCKTLVLSK SHSDDTGYYR
CFYQDIKVII DGTTAASVYV FVRDPNNPFV KRRDDMHTIF LRASDTRFEV PCLVSDPELN
VTLFSLQQDP KPLQGKGITW SNKRGWTVPR HAVNHKSVFM GFYCSLISNG KEYSTQLYFL
MEMGAKFYEL KLFPEDSPLE LMQGDILVLN CTALVEFNTG VEFKWTFPGQ KDNRVISVQP
VRQIMDQATE ATSILTIPNV NINDSGVYTC FANSVENSLE RSMLVIVYEE PFISLDYRNG
SVVEANIGQK SVKLSVRVSA FPTPVTHWYK NKTLITRRLS RFKSQDHHLE IRDVRKEDAG
DYTLVLKNTV TEKKLRFILI VNVPPQIHEK EAAAPTNPYR MGSRQTLTCT ATGYPPPTSI
SWQWRPWSPC GPNPTRKPLA RRGQRDKAPE CQDWTDLDLE HTVNVIDSMD TCLESVDGRL
KTVGRVVIRN ANVSAMYKCS AENKVGKDER LIYFYVTTIP EGFGIEVENT EEPLELDAVR
LKCSADNYTY ENLRWYRLDP QAVPPEDCKS LHKFAQALSG ELSFQVAHKN WVLELAFPSL
QLQDEGNYVC EVQNRRSGEK HCLRKYLPVK ALEAPRFQHN PTNQTVNVSA SLQMECDVEG
TPSPKLSWFK DNQPLHLVSG SDDGTNVEIV ILIGTGVIAI FFWVLLILIF CNVKRVNPAD
IKTSYLSIIM DPGEVPLEEQ CEYLPYDSSQ WEIQRDRLRL GKVLGHGAFG KVIEASIYGS
DKKCSFGTVA VKMLKEGATA SEHKALMSEL KILIHIGNHL NVVNLLGACT KPSGPLMVVV
EYCKYGNLSN YLRTKREFFL PYRDRSPKTQ SQVRRMIEAG QMELRDRQTH SNINSTKNLR
GKTSPSSPPS EEKMDDLWKT PLTIEDLICY SFQVARGMEF LASRKCIHRD LAARNILLSE
NNVVKICDFG LARDIYKDPD YVRKGNARLP LKWMAPESIF DKVYTSQSDV WSFGVLLWEI
FSLGASPYPG VQIDEDFCNQ LKDGTRMRSP DTASPEIYGI MLACWQGEPR ERPTFPALVE
ILGDLLQDNS LPDVPFNVSQ SSSDDGFSQA SSRPPSEEEL RLPCNTMSAR YYNCVPFSGC
VMVSSSKTSH SRVKTFEELP MEMTSHKSHH DSQTDSGDGF SV
//
