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Database: UniProt
Entry: A0A1S3GCP0_DIPOR
LinkDB: A0A1S3GCP0_DIPOR
Original site: A0A1S3GCP0_DIPOR 
ID   A0A1S3GCP0_DIPOR        Unreviewed;      1364 AA.
AC   A0A1S3GCP0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Vascular endothelial growth factor receptor 3 {ECO:0000256|ARBA:ARBA00022258};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=Flt4 {ECO:0000313|RefSeq:XP_012886470.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012886470.1};
RN   [1] {ECO:0000313|RefSeq:XP_012886470.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012886470.1};
RG   RefSeq;
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   RefSeq; XP_012886470.1; XM_013031016.1.
DR   STRING; 10020.ENSDORP00000012111; -.
DR   GeneID; 105996799; -.
DR   KEGG; dord:105996799; -.
DR   CTD; 2324; -.
DR   InParanoid; A0A1S3GCP0; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000081671; 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:0005021; F:vascular endothelial growth factor receptor activity; IEA:UniProt.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:UniProt.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd05862; IgI_VEGFR; 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; IPR013151; Immunoglobulin.
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; PF00047; ig; 1.
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; 2.
DR   PRINTS; PR01832; VEGFRECEPTOR.
DR   PRINTS; PR01835; VEGFRECEPTR3.
DR   SMART; SM00409; IG; 7.
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}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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..1364
FT                   /note="Vascular endothelial growth factor receptor 3"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010175256"
FT   TRANSMEM        776..798
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          219..326
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          331..415
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          422..552
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          555..671
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          678..764
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          845..1172
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1287..1364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1305..1321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1036
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         879
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1041
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         1054
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ   SEQUENCE   1364 AA;  152781 MW;  248B6B9B300E5138 CRC64;
     MPRLAAPCLR LWLCLGFLDG LVSGYSMTPP TLNITEDQYI IDTSDSLSIS CSGQHPLEWA
     WPGAQEAPAT AEKDSEDTGV VQDCEGTDAR PYCKVLLLTE AHANNTGSYR CYYKYIKARI
     EGTTAASTYV FVRDFEQPFI SKPDTLLVNR KDSMWVPCLV SIPGLNVTLR SQNSVLRPDG
     QEVVWDDRRG MQVPTPLLRD ALYLQCETSW GGQDFLSNPF LVHITGNELY DIQLFPKKSL
     ELLVGEKLVL NCTVWAEFNS GVTFDWDYPG KQEERGKWVP ERRAQQTHTE LSSILTIYNV
     SQHDLGPYVC EANNGIQRFR ESTEVIVHEK PFISVEWLKG PVVEATAGDE LVKLPVKLSA
     YPPPEFQWYK DKKAVAGRHS PHALVFKEVT EANAGVYTLA LWNSAAGLQR NISLELVVNV
     PPHIHEKEAS SPSIYSRHSR QTLTCTAYGV PPPLSIQWHW RPWTPCKTFA QRSLRRRQQR
     DRMPQCRDWR QVTMQDAVNP IESLDTWTEF VEGKNKTVSK LVIQDANVSA MYKCVVFNKV
     GQDERLIYFY VTTIPDGFSI ESEPSEEPLE GQSVRLSCRA DNYTYQHLRW YRLNLSTLHD
     AHGNPLLLDC KNVHLFATPL DANLEEATPG TRHATLSLNI PRVAPEHEGD YVCEVQDRRS
     QDKHCHKKYL SVQALEAPRL TQNLTDLLVN VSDSLEMRCA VAGSHVPSIV WYKDERLLEE
     ESGIDLADSN QKLSIQRVRE EDAGHYLCSV CNAKGCVNSS ASVAVEGSED KGSMEIIILI
     GTGVIAVFFW VLLLLIFCNM RRPAHADIKT GYLSIIMDPG EVPLEEQCEY LSYDTSQWEF
     PRERLHLGRV LGHGAFGKVV EASAFGISKG SSCDTVAVKM LKEGATASEH RALMSELKIL
     IHIGNHLNVV NLLGACTKPS GPLMVIVEFC KYGNLSNFLR AKRDTFSPYA EKSPEQRRRF
     HAMVEGAKID GRRAGSDRAL FARLLIGKGG AGRVPPVQEV EDLWLSPLTM EDLVCYSFQV
     ARGMEFLASR KCIHRDLAAR NILLSESDIV KICDFGLARD IYKDPDYVRK GSARLPLKWM
     APESIFDKVY TTQSDVWSFG VLLWEIFSLG ASPYPGVQIN EEFCQRLKEG TRMRAPELAT
     PAIRRIMLSC WSGDPKARPA FSELVEILGD LLQGGGLQEE EQDCMARCGS QSSEEGGFLQ
     TSTTALHVAE AEAEDSPPSM HRHSLAARYY NCVSFPGCLA RGAQTEGSSR MKTFEEFPMT
     PTTYKASVDN QTDSGMVLAS EEFERIESRH RQEDSFSSCK GPGQDVDDSR AHPDLQGRRR
     RTNRGAGQAG QGFYNTEYGK LSQPCEEADH TPSGGAPFFT DTGY
//
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