VEGFD_MOUSE
ID VEGFD_MOUSE Reviewed; 358 AA.
AC P97946; A2AIH3;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Vascular endothelial growth factor D {ECO:0000312|MGI:MGI:108037};
DE Short=VEGF-D;
DE AltName: Full=c-Fos-induced growth factor;
DE Short=FIGF;
DE Flags: Precursor;
GN Name=Vegfd {ECO:0000312|MGI:MGI:108037}; Synonyms=Figf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fibroblast;
RX PubMed=8876195; DOI=10.1073/pnas.93.21.11675;
RA Orlandini M., Marconcini L., Ferruzzi R., Oliviero S.;
RT "Identification of a c-fos-induced gene that is related to the platelet-
RT derived growth factor/vascular endothelial growth factor family.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:11675-11680(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=9205122; DOI=10.1006/geno.1997.4774;
RA Yamada Y., Nezu J., Shimane M., Hirata Y.;
RT "Molecular cloning of a novel vascular endothelial growth factor, VEGF-D.";
RL Genomics 42:483-488(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone, and Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=9622638; DOI=10.1016/s0925-4773(98)00049-5;
RA Avantaggiato V., Orlandini M., Acampora D., Oliviero S., Simeone A.;
RT "Embryonic expression pattern of the murine figf gene, a growth factor
RT belonging to platelet-derived growth factor/vascular endothelial growth
RT factor family.";
RL Mech. Dev. 73:221-224(1998).
RN [6]
RP RECEPTOR SPECIFICITY.
RX PubMed=11279005; DOI=10.1074/jbc.m100097200;
RA Baldwin M.E., Catimel B., Nice E.C., Roufail S., Hall N.E., Stenvers K.L.,
RA Karkkainen M.J., Alitalo K., Stacker S.A., Achen M.G.;
RT "The specificity of receptor binding by vascular endothelial growth factor-
RT d is different in mouse and man.";
RL J. Biol. Chem. 276:19166-19171(2001).
CC -!- FUNCTION: Growth factor active in angiogenesis, lymphangiogenesis and
CC endothelial cell growth, stimulating their proliferation and migration
CC and also has effects on the permeability of blood vessels. May function
CC in the formation of the venous and lymphatic vascular systems during
CC embryogenesis, and also in the maintenance of differentiated lymphatic
CC endothelium in adults. Binds and activates VEGFR-3 (Flt4) receptor.
CC -!- SUBUNIT: Homodimer; non-covalent and antiparallel.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal and adult lung.
CC -!- DEVELOPMENTAL STAGE: Expressed in a dynamic pattern in several body
CC structures and organs of the embryo such as limb buds, acoustic
CC ganglion, teeth, heart, anterior pituitary as well as lung and kidney
CC mesenchyme, liver, derma, and periosteum of the vertebral column.
CC {ECO:0000269|PubMed:9622638}.
CC -!- INDUCTION: By the transcription factor c-fos.
CC -!- PTM: Undergoes a complex proteolytic maturation which generates a
CC variety of processed secreted forms with increased activity toward
CC VEGFR-3 and VEGFR-2. VEGF-D first form an antiparallel homodimer linked
CC by disulfide bonds before secretion. The fully processed VEGF-D is
CC composed mostly of two VEGF homology domains (VHDs) bound by non-
CC covalent interactions (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; X99572; CAA67892.1; -; mRNA.
DR EMBL; D89628; BAA14002.1; -; mRNA.
DR EMBL; AL732475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC080770; AAH80770.1; -; mRNA.
DR CCDS; CCDS30521.1; -.
DR RefSeq; NP_001295418.1; NM_001308489.1.
DR RefSeq; NP_034346.1; NM_010216.2.
DR RefSeq; XP_006528763.1; XM_006528700.3.
DR AlphaFoldDB; P97946; -.
DR SMR; P97946; -.
DR BioGRID; 199673; 2.
DR STRING; 10090.ENSMUSP00000033751; -.
DR GlyGen; P97946; 3 sites.
DR iPTMnet; P97946; -.
DR PhosphoSitePlus; P97946; -.
DR PaxDb; P97946; -.
DR PeptideAtlas; P97946; -.
DR PRIDE; P97946; -.
DR ProteomicsDB; 298278; -.
DR Antibodypedia; 8816; 622 antibodies from 37 providers.
DR DNASU; 14205; -.
DR Ensembl; ENSMUST00000033751; ENSMUSP00000033751; ENSMUSG00000031380.
DR GeneID; 14205; -.
DR KEGG; mmu:14205; -.
DR UCSC; uc009uvm.1; mouse.
DR CTD; 2277; -.
DR MGI; MGI:108037; Vegfd.
DR VEuPathDB; HostDB:ENSMUSG00000031380; -.
DR eggNOG; ENOG502QVIH; Eukaryota.
DR GeneTree; ENSGT00940000159726; -.
DR HOGENOM; CLU_061712_0_0_1; -.
DR InParanoid; P97946; -.
DR OMA; FHTRTCA; -.
DR OrthoDB; 1364454at2759; -.
DR PhylomeDB; P97946; -.
DR TreeFam; TF319554; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-194313; VEGF ligand-receptor interactions.
DR Reactome; R-MMU-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR BioGRID-ORCS; 14205; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Vegfd; mouse.
DR PRO; PR:P97946; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P97946; protein.
DR Bgee; ENSMUSG00000031380; Expressed in left lung lobe and 185 other tissues.
DR Genevisible; P97946; MM.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0043185; F:vascular endothelial growth factor receptor 3 binding; IDA:MGI.
DR GO; GO:0005172; F:vascular endothelial growth factor receptor binding; ISO:MGI.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0048144; P:fibroblast proliferation; IDA:MGI.
DR GO; GO:0050930; P:induction of positive chemotaxis; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IBA:GO_Central.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IBA:GO_Central.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0060754; P:positive regulation of mast cell chemotaxis; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
DR GO; GO:0002040; P:sprouting angiogenesis; IBA:GO_Central.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IBA:GO_Central.
DR CDD; cd00135; PDGF; 1.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR004153; CXCXC_repeat.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR023581; PD_growth_factor_CS.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR Pfam; PF03128; CXCXC; 1.
DR Pfam; PF00341; PDGF; 1.
DR SMART; SM00141; PDGF; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00249; PDGF_1; 1.
DR PROSITE; PS50278; PDGF_2; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Cleavage on pair of basic residues; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Growth factor; Mitogen;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..93
FT /evidence="ECO:0000255"
FT /id="PRO_0000023411"
FT CHAIN 94..210
FT /note="Vascular endothelial growth factor D"
FT /id="PRO_0000023412"
FT PROPEP 211..358
FT /evidence="ECO:0000255"
FT /id="PRO_0000023413"
FT REPEAT 227..242
FT /note="1; approximate"
FT REPEAT 263..278
FT /note="2"
FT REPEAT 282..298
FT /note="3"
FT REPEAT 306..323
FT /note="4"
FT REGION 227..323
FT /note="4 X 16 AA repeats of C-X(10)-C-X-C-X(1,3)-C"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..158
FT /evidence="ECO:0000250"
FT DISULFID 141
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 147..194
FT /evidence="ECO:0000250"
FT DISULFID 150
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 151..196
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 40909 MW; 6636B17FBF07037C CRC64;
MYGEWGMGNI LMMFHVYLVQ GFRSEHGPVK DFSFERSSRS MLERSEQQIR AASSLEELLQ
IAHSEDWKLW RCRLKLKSLA SMDSRSASHR STRFAATFYD TETLKVIDEE WQRTQCSPRE
TCVEVASELG KTTNTFFKPP CVNVFRCGGC CNEEGVMCMN TSTSYISKQL FEISVPLTSV
PELVPVKIAN HTGCKCLPTG PRHPYSIIRR SIQTPEEDEC PHSKKLCPID MLWDNTKCKC
VLQDETPLPG TEDHSYLQEP TLCGPHMTFD EDRCECVCKA PCPGDLIQHP ENCSCFECKE
SLESCCQKHK IFHPDTCSCE DRCPFHTRTC ASRKPACGKH WRFPKETRAQ GLYSQENP
