ID A0A3Q3H2H1_9LABR Unreviewed; 1346 AA.
AC A0A3Q3H2H1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Vascular endothelial growth factor receptor 3 {ECO:0000256|ARBA:ARBA00022258};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
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:ENSLBEP00000037818.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000037818.1}
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; ENSLBET00000039380.1; ENSLBEP00000037818.1; ENSLBEG00000028171.1.
DR GeneTree; ENSGT00940000159358; -.
DR Proteomes; UP000261660; 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 CDD; cd00096; Ig; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 8.
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; 6.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 4.
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:UP000261660};
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 6..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 767..788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..335
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 346..440
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 447..543
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 670..755
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 836..1167
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 962..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1031
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 870
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1036
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1049
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 1346 AA; 150852 MW; 41F4C3194618D219 CRC64;
ISFYTFALLI VWVGGGGAVY VALIQPTVWL YSLVIGFSMT PPILDSSKDD LVIPVHQTLT
ITCRGQRTLA WAWPDQTLLG EELTDRQAQL PVTRGPGLRV ALISECPGQP GRPYCKRLIL
TAARAKDTGY YRCYYKDVKA VIIGTTAVNI YVFVRGDQTN GNNLETILIK RFSKHVIVPC
LVTVPDLNVT LYAYPTPLEK SEMTWDNKRG WSVPRQTIDN VPMVIGVLCV ATLGGKEFQS
ANYLIHTTGS EVYDVKLFPE DPVELIVGEA LTLNCTALVE FNTGVDIKWS YPGKKVQSTL
SHATEAVSIL TIHSVNVTDT GPYSCNVTSM ETTLTQQTQV IVYDKPFISL SYRKGPVVEV
TAGQKSFKLQ VNVSAFPTPE TQWYKDGKLI NQRPEFKMKR IRMHLNHALE IKDVCQEDSG
LYMVVLKNSA ASIERKLNIT LVVNVPPQIH EKEVADPSSP YPSGSSQILT CTAYGLPAPT
VSWQWRAWEK HLSQIQTATH SDVMLFFFFF CKPVRLQIRN ASVSIMYKCS AENKVGKDER
LIYFYVTTIP EGFSLDVQPS ENSLEQEKVS LCCSADNYTY EQLQLYRLDP RALQDEQGSP
QELDCRSVHL YADTLDGQLS FQEPSNSWIL DFNIQAVQLQ DEGHYVCEAQ SRRSGEKQCL
FRYISVKGAP LQRSLTNQTV NVTESLRMEC DVEGRPLPRL SWFKDNRPLH QMSGIQLQDS
NRTLSIQRVR EEDAGLYTCT ACNQRGCVHS SAAVRVIGSS DKANVEIVIL IGTGVIAVFF
WALLILIFCN VKRVNPADIK TGYLSIIMDP GEVPLDEQCE YLPYDSSQWE ISRDKLRLGK
VLGHGAFGKV IEASFYGISK SSSLDTVAVK MLKDGATASE HKALMSELKI LIHIGNHLNV
VNLLGACTKP NGPLMVIVEY CKYGNLSNFL RAKREFFLPY RDRSPKTQSQ VRRMIEAGQI
DQRAHQQLSP SDSRLINPPP PSSNTSIQTP AVEKMEDLWK TPLTIEDLIC YSFQVARGME
FLASRKCIHR DLAARNILLS ENNIVKICDF GLARDIYKDP DYVRKGNARL PLKWMAPESI
FDKVYTSQSD VWSFGVLLWE IFSLGASPYP GVQIDEDFCK RLKDGVRMRA PETASPEIYG
IMLACWHGEP KERPPFPSLV QILGDLLQDN SLPDYVLNSS QSSEDDGFSQ VSSRPPSEEE
LRLACNTLPS SRYYNCVPFA SCVFVGPSKV CQPRVKTFEE LPLEMHQQKA PQDNQTDSGM
VLASEEFERI EHKHRGASSK SSSSTEPLTA SQAHSSDVIS SRHRPHFFSQ LSGQTFYNNE
YGHLSEEGFC DFFSSPDAPC LASSNV
//
