ID A0A093PWF3_9PASS Unreviewed; 1355 AA.
AC A0A093PWF3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Vascular endothelial growth factor receptor 3 {ECO:0000256|ARBA:ARBA00022258};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE Flags: Fragment;
GN ORFNames=N305_02875 {ECO:0000313|EMBL:KFW78545.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW78545.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW78545.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW78545.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL670300; KFW78545.1; -; Genomic_DNA.
DR STRING; 328815.ENSMVIP00005017136; -.
DR Proteomes; UP000053258; Unassembled WGS sequence.
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; cd05862; IgI_VEGFR; 1.
DR CDD; cd05863; IgI_VEGFR-3; 1.
DR CDD; cd05102; PTKc_VEGFR3; 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; 1.
DR Pfam; PF13927; Ig_3; 3.
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; 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, 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:UP000053258};
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 ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 769..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 237..318
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 323..406
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 413..546
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 549..664
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 671..757
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 838..1165
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1176..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1029
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 872
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1034
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1047
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW78545.1"
FT NON_TER 1355
FT /evidence="ECO:0000313|EMBL:KFW78545.1"
SQ SEQUENCE 1355 AA; 153634 MW; 5ED7DAE94BD0EC7B CRC64;
STDLVSSYSM TPPTLSITEE EHVINAKDTL TITCRGQHPL EWSWPGGKVD PAGKEETELV
ASAAPSSGRA IREEDCEGTG TKPYCKVLVL TETQANDTGY YRCYYKYIDA KIEGTTAVGT
YVFVRDFEQP FINKPETLLI SKKENTWVPC LVSIPDLNVT LTSQNFYIHP DGKSIFWDNK
KGVQVPTHMI RDFLFVQCET VIDKKVFKSN FFIIHIAGSE LYDIQLYPKK AMELLVGEKL
VLNCTVWAEF NSGVRFQWAY PGKQTQRAVV ESERHSLQTH TELSSILTLH NVSQQDLGEY
KCTATTGAQM LEESTDVIVH EKPFINVEWR KGPVIEATTG DEAVKLPVKV VAYPPPDFQW
YKDGKLIPKQ SQSSMQIKDV SEQHAGTYTL VLRNRLAGLE KHISLQLIVN VPPRIHEKET
SSPSIYSKKS PQALTCTVYG IPAPEVIQWQ WRPWMPCRMF SRRSLHRAAR RHQRDRMPEC
KDWKDVTQQD AVNPIESIDT WVEFVEGRNK TVSKLAIQEA NNSAMYKCIA SNKVGRDERL
IYFYVTTIPD GFEIESQPSE EPIEGQDLQL SCNADNYTYE NLQWYRLNLS KLHDEEGNPL
VLDCKNVHHY ATKMQGELRF QPHSNDATLL LTIPNISLNE EGDYVCEVQN RKTREKHCHK
KYISVQALEI PRLKQNLTDI WVNVSDSIEM RCKVDGNHIP AISWYKDEKL VEEVSGIDLA
DFNQRLSIQR VREEDAGLYL CSVCNAKGCV NSSASVSVEG SDDRTNVEIV ILIGTGVIAV
FFWILLILIF CNIKRPAHAD IKTGYLSIIM DPGEVPLEEQ CEYLPYDSSK WEFPRDRLRL
GKVLGHGAFG KVVEASAFGI NKSNSCETVA VKMLKEGATA SEHKALMSEL KILIHIGNHL
NVVNLLGACT KPNGPLMVIV EFCKYGNLSN YLRTKREGFS PYREKSPRLR IQVQSIVEAV
RADRRSRSGT SDSAIFHRFL MHKSQTAHPI QEVDDLWQSP LTMEDLICYS FQVARGMEFL
ASRKCIHRDL AARNILLSEN NVVKICDFGL ARDIYKDPDY VRKGSARLPL KWMAPESIFD
KVYTTQSDVW SFGVLLWEIF SLGASPYPGV QINEEFCQRL KDGTRMRAPE YATAEIYRIM
LSCWHGDPKE RPTFSDLVEI LGNLLQENVQ QEGKDYIPLN DSHSSEDDGF SQVPSSAQQN
SDEEDFDMRI RCHSLAARYY NCVSFPGCLT GGNQIRCPSR IKTFEEFPMT HTMYKAHPDN
QTDSGMVLAS EEFERIENRH RKEGGFSSKG PSRTGEQSDL RGRCRPSYGS QVGGQTFYNS
EYGELSEHSE DGSCTPPGEG ASPPALHASF FSEQY
//
