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Database: UniProt
Entry: K7G2W2_PELSI
LinkDB: K7G2W2_PELSI
Original site: K7G2W2_PELSI 
ID   K7G2W2_PELSI            Unreviewed;      1333 AA.
AC   K7G2W2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=FLT1 {ECO:0000313|Ensembl:ENSPSIP00000014623.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000014623.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000014623.1}
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   EMBL; AGCU01200914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01200915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01200916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01200917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01200918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01200919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01200920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01200921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01200922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01200923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006138980.1; XM_006138918.2.
DR   STRING; 13735.ENSPSIP00000014623; -.
DR   Ensembl; ENSPSIT00000014691.1; ENSPSIP00000014623.1; ENSPSIG00000012931.1.
DR   GeneID; 102456773; -.
DR   KEGG; pss:102456773; -.
DR   CTD; 2321; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   GeneTree; ENSGT00940000158713; -.
DR   HOGENOM; CLU_000288_49_4_1; -.
DR   OMA; CNENFPV; -.
DR   OrthoDB; 1614410at2759; -.
DR   TreeFam; TF325768; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0036332; F:placental growth factor receptor activity; IEA:Ensembl.
DR   GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0002548; P:monocyte chemotaxis; IEA:Ensembl.
DR   GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
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; 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   InterPro; IPR009135; VEGFR1_rcpt.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   PANTHER; PTHR24416:SF390; VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1; 1.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF00047; ig; 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; 2.
DR   PRINTS; PR01832; VEGFRECEPTOR.
DR   PRINTS; PR01833; VEGFRECEPTR1.
DR   SMART; SM00409; IG; 7.
DR   SMART; SM00408; IGc2; 6.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 7.
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};
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:UP000007267};
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   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1333
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003902470"
FT   DOMAIN          33..121
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          244..327
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          349..421
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          428..549
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          556..648
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          655..741
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          822..1154
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        1018
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         856
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1023
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         1036
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ   SEQUENCE   1333 AA;  149757 MW;  803437C48D445C46 CRC64;
     MGSRALAGAM LCGLLAPALL FAGSSSGSKL KGPELSIKGA QHVIRAGQTL NLTCRGEMVH
     SWSLPEAPSK ESKRLKVIKY ACGRNGKQFC SSLTLIRAQA NDTGYYSCKY ASSSAVKKKI
     ESTVYVFIND TGSPFVQLHS DIPEIIQMTE GREMIIPCRV TAPDIAVTLR KIPLETLIPD
     GKTIIWDSTK GFIIPKATYQ FIGLMSCETT IDGHKYSTKY LTHRQSNTIY DVQLNTPNLV
     KLLKGDMLAI NCTVAADWNT RVQMTWSYPG EADRRASITN RMRQRNTDAN IFYSILVVGK
     VRDIDKGQYT CHVKSGPSIK SVNTTVHVYD KTFITLKHRR KSVLETVAGR KSYRLSMKVK
     AFPSPEVVWL KDGLPAAEKC ARYVAKDYSL IIRDVAEEDA GNYTITLSIR QWNLYKNLTV
     TLIVNVKPQI YEKAVSTFPD PNLYLVGSKQ VLTCTVYGIP QPTVTWIWHP CRQNHSKARY
     DVCSNTEGPF ILKSGSSTGN RIQSITQHMA MLEGKNKTAS ILVVAEAKSS GIYSCVASNK
     VGNVERNISF YVTDVPNGFH INLEKMPIEG ENLILSCSAN KFLYKDIAWI LPRTVNNQTK
     AKKHITKEYS NTLILTIKNV SLEHSGTYAC RARNIYSGEE VLQKKDVTIR AQQAPSFLRN
     LSDQIVNTSH SATLECQAHG IPEPQISWFK NHEEIQQEPG IILGPGSKML LIERVKVEDE
     GFYQCIATNL KGSVESAAYV TVQGTSEKSN LELITLTCTC VAATLFWLLL TLFIRKLKRP
     HSSEMKTNYL SIIMDPDEVP LDEQCQHLPF DASKWEFARE RLKLGKSLGS GAFGKVVQAA
     AFGIKKSPTC RTVAVKMLKE GATASEYKAL MTELKILIHI GHHLNIVNLL GACTKNNGPL
     MVIVEYCKYG NLSNYLKSKR NFFFPNKDES LQVEQMKQKK DTELVGNKKQ RLASVTSTES
     LASSGFQEDK YLSDVEEDEE DSDDFYKWPL TVEDLISYSF QVARGMEFLS SRKCIHRDLA
     ARNVLLSENN VVKICDFGLA RDIYKNPDYV RKGDARLPLK WMAPESIFDK IYNTKSDVWS
     YGVLLWEIFS LGASPYPGVQ IDEDFCSRLK DGTRMRAPEY GTSEIYQIML DCWHGNPNER
     PRFSDLVERL GDLLQANVQQ AGKDYIPLNT IFTADSRFAY SHPTLDNSNL SEDISVPKSN
     HESTENIGYI NTFKMKPFQR VNTFEELSPR DTFAFDDYQA DSGMVLASEE LKRFTWTESK
     QKQTLFGRKA ASRSKESVLS GMIRPSFCSS SCGHLSEVSW QFPYGNTMLD KMRVHRSPPP
     EYNSLGFYSP PPV
//
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