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Vascular endothelial growth factor D (VEGF-D) (c-Fos-induced growth factor) (FIGF)

 VEGFD_HUMAN             Reviewed;         354 AA.
O43915; B2R7Z3;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
12-SEP-2018, entry version 155.
RecName: Full=Vascular endothelial growth factor D {ECO:0000312|HGNC:HGNC:3708};
Short=VEGF-D;
AltName: Full=c-Fos-induced growth factor;
Short=FIGF;
Flags: Precursor;
Name=VEGFD {ECO:0000312|HGNC:HGNC:3708}; Synonyms=FIGF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=9205122; DOI=10.1006/geno.1997.4774;
Yamada Y., Nezu J., Shimane M., Hirata Y.;
"Molecular cloning of a novel vascular endothelial growth factor,
VEGF-D.";
Genomics 42:483-488(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Lung;
PubMed=9479493; DOI=10.1006/geno.1997.5079;
Rocchigiani M., Lestingi M., Luddi A., Orlandini M., Franco B.,
Rossi E., Ballabio A., Zuffardi O., Oliviero S.;
"Human FIGF: cloning, gene structure, and mapping to chromosome Xp22.1
between the PIGA and the GRPR genes.";
Genomics 47:207-216(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9435229; DOI=10.1073/pnas.95.2.548;
Achen M.G., Jeltsch M., Kukk E., Maekinen T., Vitali A., Wilks A.F.,
Alitalo K., Stacker S.A.;
"Vascular endothelial growth factor D (VEGF-D) is a ligand for the
tyrosine kinases VEGF receptor 2 (Flk1) and VEGF receptor 3 (Flt4).";
Proc. Natl. Acad. Sci. U.S.A. 95:548-553(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 89-94; 100-105 AND 206-213, AND PROTEOLYTIC
PROCESSING.
PubMed=10542248; DOI=10.1074/jbc.274.45.32127;
Stacker S.A., Stenvers K.L., Caesar C., Vitali A., Domagala T.,
Nice E.C., Roufail S., Simpson R.J., Moritz R., Karpanen T.,
Alitalo K., Achen M.G.;
"Biosynthesis of vascular endothelial growth factor-D involves
proteolytic processing which generates non-covalent homodimers.";
J. Biol. Chem. 274:32127-32136(1999).
[8]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 92-195 OF MUTANT ALA-117,
FUNCTION, SUBUNIT, GLYCOSYLATION AT ASN-155 AND ASN-185, AND DISULFIDE
BONDS.
PubMed=21148085; DOI=10.1182/blood-2010-08-301549;
Leppanen V.M., Jeltsch M., Anisimov A., Tvorogov D., Aho K.,
Kalkkinen N., Toivanen P., Yla-Herttuala S., Ballmer-Hofer K.,
Alitalo K.;
"Structural determinants of vascular endothelial growth factor-D
- receptor binding and specificity.";
Blood 117:1507-1515(2011).
-!- FUNCTION: Growth factor active in angiogenesis, lymphangiogenesis
and endothelial cell growth, stimulating their proliferation and
migration and also has effects on the permeability of blood
vessels. May function in the formation of the venous and lymphatic
vascular systems during embryogenesis, and also in the maintenance
of differentiated lymphatic endothelium in adults. Binds and
activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors.
{ECO:0000269|PubMed:21148085}.
-!- SUBUNIT: Homodimer; non-covalent and antiparallel.
{ECO:0000269|PubMed:21148085}.
-!- INTERACTION:
Q15836:VAMP3; NbExp=4; IntAct=EBI-11750035, EBI-722343;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Highly expressed in lung, heart, small
intestine and fetal lung, and at lower levels in skeletal muscle,
colon, and pancreas.
-!- PTM: Undergoes a complex proteolytic maturation which generates a
variety of processed secreted forms with increased activity toward
VEGFR-3 and VEGFR-2. VEGF-D first form an antiparallel homodimer
linked by disulfide bonds before secretion. The fully processed
VEGF-D is composed mostly of two VEGF homology domains (VHDs)
bound by non-covalent interactions. {ECO:0000269|PubMed:10542248}.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FIGFID40574chXp22.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; D89630; BAA24264.1; -; mRNA.
EMBL; Y12863; CAA73370.1; -; mRNA.
EMBL; Y12864; CAA73371.1; -; Genomic_DNA.
EMBL; Y12865; CAA73371.1; JOINED; Genomic_DNA.
EMBL; Y12866; CAA73371.1; JOINED; Genomic_DNA.
EMBL; Y12867; CAA73371.1; JOINED; Genomic_DNA.
EMBL; Y12868; CAA73371.1; JOINED; Genomic_DNA.
EMBL; Y12869; CAA73371.1; JOINED; Genomic_DNA.
EMBL; Y12870; CAA73371.1; JOINED; Genomic_DNA.
EMBL; AJ000185; CAA03942.1; -; mRNA.
EMBL; AK313173; BAG35990.1; -; mRNA.
EMBL; CH471074; EAW98885.1; -; Genomic_DNA.
EMBL; BC027948; AAH27948.1; -; mRNA.
CCDS; CCDS14166.1; -.
RefSeq; NP_004460.1; NM_004469.4.
UniGene; Hs.11392; -.
PDB; 2XV7; X-ray; 2.90 A; A=92-195.
PDBsum; 2XV7; -.
ProteinModelPortal; O43915; -.
SMR; O43915; -.
BioGrid; 108567; 12.
CORUM; O43915; -.
IntAct; O43915; 1.
STRING; 9606.ENSP00000297904; -.
iPTMnet; O43915; -.
PhosphoSitePlus; O43915; -.
BioMuta; FIGF; -.
PaxDb; O43915; -.
PeptideAtlas; O43915; -.
PRIDE; O43915; -.
ProteomicsDB; 49231; -.
Ensembl; ENST00000297904; ENSP00000297904; ENSG00000165197.
GeneID; 2277; -.
KEGG; hsa:2277; -.
UCSC; uc004cwt.3; human.
CTD; 2277; -.
DisGeNET; 2277; -.
EuPathDB; HostDB:ENSG00000165197.4; -.
GeneCards; VEGFD; -.
HGNC; HGNC:3708; VEGFD.
HPA; HPA027342; -.
MIM; 300091; gene.
neXtProt; NX_O43915; -.
OpenTargets; ENSG00000165197; -.
PharmGKB; PA28146; -.
eggNOG; ENOG410IVDX; Eukaryota.
eggNOG; ENOG4111ICH; LUCA.
GeneTree; ENSGT00730000110889; -.
HOGENOM; HOG000231512; -.
HOVERGEN; HBG073119; -.
InParanoid; O43915; -.
KO; K05449; -.
OMA; CEDRCPF; -.
OrthoDB; EOG091G07BT; -.
PhylomeDB; O43915; -.
TreeFam; TF319554; -.
BRENDA; 3.4.21.46; 2681.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-194313; VEGF ligand-receptor interactions.
Reactome; R-HSA-195399; VEGF binds to VEGFR leading to receptor dimerization.
SIGNOR; O43915; -.
ChiTaRS; VEGFD; human.
EvolutionaryTrace; O43915; -.
GeneWiki; C-fos_induced_growth_factor; -.
GenomeRNAi; 2277; -.
PRO; PR:O43915; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000165197; Expressed in 125 organ(s), highest expression level in endocervix.
CleanEx; HS_FIGF; -.
Genevisible; O43915; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; TAS:ProtInc.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0043185; F:vascular endothelial growth factor receptor 3 binding; IBA:GO_Central.
GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IPI:UniProtKB.
GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0071542; P:dopaminergic neuron differentiation; IEA:Ensembl.
GO; GO:0050930; P:induction of positive chemotaxis; IDA:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0045766; P:positive regulation of angiogenesis; IBA:GO_Central.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IBA:GO_Central.
GO; GO:0060754; P:positive regulation of mast cell chemotaxis; IDA:UniProtKB.
GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IBA:GO_Central.
CDD; cd00135; PDGF; 1.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR023581; PD_growth_factor_CS.
InterPro; IPR000072; PDGF/VEGF_dom.
Pfam; PF00341; PDGF; 1.
SMART; SM00141; PDGF; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00249; PDGF_1; 1.
PROSITE; PS50278; PDGF_2; 1.
1: Evidence at protein level;
3D-structure; Angiogenesis; Cleavage on pair of basic residues;
Complete proteome; Developmental protein; Differentiation;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Growth factor; Mitogen; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 88 Or 99 (in a minor form).
{ECO:0000269|PubMed:10542248}.
/FTId=PRO_0000023408.
CHAIN 89 205 Vascular endothelial growth factor D.
/FTId=PRO_0000023409.
PROPEP 206 354
/FTId=PRO_0000023410.
REPEAT 222 237 1; approximate.
REPEAT 258 273 2.
REPEAT 277 293 3.
REPEAT 301 318 4.
REGION 222 318 4 X 16 AA repeats of C-X(10)-C-X-C-
X(1,3)-C.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21148085}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21148085}.
CARBOHYD 287 287 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 111 153 {ECO:0000269|PubMed:21148085}.
DISULFID 136 136 Interchain.
{ECO:0000269|PubMed:21148085}.
DISULFID 142 189 {ECO:0000269|PubMed:21148085}.
DISULFID 145 145 Interchain.
{ECO:0000269|PubMed:21148085}.
DISULFID 146 191 {ECO:0000269|PubMed:21148085}.
HELIX 93 108 {ECO:0000244|PDB:2XV7}.
STRAND 110 119 {ECO:0000244|PDB:2XV7}.
HELIX 120 123 {ECO:0000244|PDB:2XV7}.
HELIX 127 129 {ECO:0000244|PDB:2XV7}.
STRAND 133 143 {ECO:0000244|PDB:2XV7}.
STRAND 152 166 {ECO:0000244|PDB:2XV7}.
STRAND 169 171 {ECO:0000244|PDB:2XV7}.
STRAND 178 192 {ECO:0000244|PDB:2XV7}.
SEQUENCE 354 AA; 40444 MW; 2048D769D735173E CRC64;
MYREWVVVNV FMMLYVQLVQ GSSNEHGPVK RSSQSTLERS EQQIRAASSL EELLRITHSE
DWKLWRCRLR LKSFTSMDSR SASHRSTRFA ATFYDIETLK VIDEEWQRTQ CSPRETCVEV
ASELGKSTNT FFKPPCVNVF RCGGCCNEES LICMNTSTSY ISKQLFEISV PLTSVPELVP
VKVANHTGCK CLPTAPRHPY SIIRRSIQIP EEDRCSHSKK LCPIDMLWDS NKCKCVLQEE
NPLAGTEDHS HLQEPALCGP HMMFDEDRCE CVCKTPCPKD LIQHPKNCSC FECKESLETC
CQKHKLFHPD TCSCEDRCPF HTRPCASGKT ACAKHCRFPK EKRAAQGPHS RKNP


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