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Protein

Vascular endothelial growth factor D

Gene

FIGF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • chemoattractant activity Source: UniProtKB
  • platelet-derived growth factor receptor binding Source: ProtInc
  • vascular endothelial growth factor receptor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Keywords - Biological processi

Angiogenesis, Differentiation

Enzyme and pathway databases

BRENDAi3.4.21.46. 2681.
ReactomeiREACT_12380. VEGF ligand-receptor interactions.
REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.
REACT_318. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Vascular endothelial growth factor D
Short name:
VEGF-D
Alternative name(s):
c-Fos-induced growth factor
Short name:
FIGF
Gene namesi
Name:FIGF
Synonyms:VEGFD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:3708. FIGF.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
  • membrane Source: InterPro
  • platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28146.

Polymorphism and mutation databases

BioMutaiFIGF.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 8867Or 99 (in a minor form)1 PublicationPRO_0000023408Add
BLAST
Chaini89 – 205117Vascular endothelial growth factor DPRO_0000023409Add
BLAST
Propeptidei206 – 354149PRO_0000023410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi111 ↔ 1531 Publication
Disulfide bondi136 – 136Interchain1 Publication
Disulfide bondi142 ↔ 1891 Publication
Disulfide bondi145 – 145Interchain1 Publication
Disulfide bondi146 ↔ 1911 Publication
Glycosylationi155 – 1551N-linked (GlcNAc...)1 Publication
Glycosylationi185 – 1851N-linked (GlcNAc...)1 Publication
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO43915.
PRIDEiO43915.

PTM databases

PhosphoSiteiO43915.

Expressioni

Tissue specificityi

Highly expressed in lung, heart, small intestine and fetal lung, and at lower levels in skeletal muscle, colon, and pancreas.

Gene expression databases

BgeeiO43915.
CleanExiHS_FIGF.
GenevisibleiO43915. HS.

Organism-specific databases

HPAiHPA027342.

Interactioni

Subunit structurei

Homodimer; non-covalent and antiparallel.1 Publication

Protein-protein interaction databases

BioGridi108567. 10 interactions.
STRINGi9606.ENSP00000297904.

Structurei

Secondary structure

1
354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi93 – 10816Combined sources
Beta strandi110 – 11910Combined sources
Helixi120 – 1234Combined sources
Helixi127 – 1293Combined sources
Beta strandi133 – 14311Combined sources
Beta strandi152 – 16615Combined sources
Beta strandi169 – 1713Combined sources
Beta strandi178 – 19215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XV7X-ray2.90A92-195[»]
ProteinModelPortaliO43915.
SMRiO43915. Positions 92-194.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43915.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati222 – 237161; approximateAdd
BLAST
Repeati258 – 273162Add
BLAST
Repeati277 – 293173Add
BLAST
Repeati301 – 318184Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni222 – 318974 X 16 AA repeats of C-X(10)-C-X-C-X(1,3)-CAdd
BLAST

Sequence similaritiesi

Belongs to the PDGF/VEGF growth factor family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG77707.
GeneTreeiENSGT00730000110889.
HOGENOMiHOG000231512.
HOVERGENiHBG073119.
InParanoidiO43915.
KOiK05449.
OMAiDTCSCED.
OrthoDBiEOG7J17ZS.
PhylomeDBiO43915.
TreeFamiTF319554.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR023581. PD_growth_factor_CS.
IPR000072. PDGF/VEGF_dom.
[Graphical view]
PfamiPF00341. PDGF. 1 hit.
[Graphical view]
SMARTiSM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O43915-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYREWVVVNV FMMLYVQLVQ GSSNEHGPVK RSSQSTLERS EQQIRAASSL
60 70 80 90 100
EELLRITHSE DWKLWRCRLR LKSFTSMDSR SASHRSTRFA ATFYDIETLK
110 120 130 140 150
VIDEEWQRTQ CSPRETCVEV ASELGKSTNT FFKPPCVNVF RCGGCCNEES
160 170 180 190 200
LICMNTSTSY ISKQLFEISV PLTSVPELVP VKVANHTGCK CLPTAPRHPY
210 220 230 240 250
SIIRRSIQIP EEDRCSHSKK LCPIDMLWDS NKCKCVLQEE NPLAGTEDHS
260 270 280 290 300
HLQEPALCGP HMMFDEDRCE CVCKTPCPKD LIQHPKNCSC FECKESLETC
310 320 330 340 350
CQKHKLFHPD TCSCEDRCPF HTRPCASGKT ACAKHCRFPK EKRAAQGPHS

RKNP
Length:354
Mass (Da):40,444
Last modified:June 1, 1998 - v1
Checksum:i2048D769D735173E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89630 mRNA. Translation: BAA24264.1.
Y12863 mRNA. Translation: CAA73370.1.
Y12864
, Y12865, Y12866, Y12867, Y12868, Y12869, Y12870 Genomic DNA. Translation: CAA73371.1.
AJ000185 mRNA. Translation: CAA03942.1.
AK313173 mRNA. Translation: BAG35990.1.
CH471074 Genomic DNA. Translation: EAW98885.1.
BC027948 mRNA. Translation: AAH27948.1.
CCDSiCCDS14166.1.
RefSeqiNP_004460.1. NM_004469.4.
UniGeneiHs.11392.

Genome annotation databases

EnsembliENST00000297904; ENSP00000297904; ENSG00000165197.
GeneIDi2277.
KEGGihsa:2277.
UCSCiuc004cwt.2. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89630 mRNA. Translation: BAA24264.1.
Y12863 mRNA. Translation: CAA73370.1.
Y12864
, Y12865, Y12866, Y12867, Y12868, Y12869, Y12870 Genomic DNA. Translation: CAA73371.1.
AJ000185 mRNA. Translation: CAA03942.1.
AK313173 mRNA. Translation: BAG35990.1.
CH471074 Genomic DNA. Translation: EAW98885.1.
BC027948 mRNA. Translation: AAH27948.1.
CCDSiCCDS14166.1.
RefSeqiNP_004460.1. NM_004469.4.
UniGeneiHs.11392.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XV7X-ray2.90A92-195[»]
ProteinModelPortaliO43915.
SMRiO43915. Positions 92-194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108567. 10 interactions.
STRINGi9606.ENSP00000297904.

PTM databases

PhosphoSiteiO43915.

Polymorphism and mutation databases

BioMutaiFIGF.

Proteomic databases

PaxDbiO43915.
PRIDEiO43915.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297904; ENSP00000297904; ENSG00000165197.
GeneIDi2277.
KEGGihsa:2277.
UCSCiuc004cwt.2. human.

Organism-specific databases

CTDi2277.
GeneCardsiGC0XM015363.
HGNCiHGNC:3708. FIGF.
HPAiHPA027342.
MIMi300091. gene.
neXtProtiNX_O43915.
PharmGKBiPA28146.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG77707.
GeneTreeiENSGT00730000110889.
HOGENOMiHOG000231512.
HOVERGENiHBG073119.
InParanoidiO43915.
KOiK05449.
OMAiDTCSCED.
OrthoDBiEOG7J17ZS.
PhylomeDBiO43915.
TreeFamiTF319554.

Enzyme and pathway databases

BRENDAi3.4.21.46. 2681.
ReactomeiREACT_12380. VEGF ligand-receptor interactions.
REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.
REACT_318. Platelet degranulation.

Miscellaneous databases

ChiTaRSiFIGF. human.
EvolutionaryTraceiO43915.
GeneWikiiC-fos_induced_growth_factor.
GenomeRNAii2277.
NextBioi9261.
PROiO43915.
SOURCEiSearch...

Gene expression databases

BgeeiO43915.
CleanExiHS_FIGF.
GenevisibleiO43915. HS.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR023581. PD_growth_factor_CS.
IPR000072. PDGF/VEGF_dom.
[Graphical view]
PfamiPF00341. PDGF. 1 hit.
[Graphical view]
SMARTiSM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a novel vascular endothelial growth factor, VEGF-D."
    Yamada Y., Nezu J., Shimane M., Hirata Y.
    Genomics 42:483-488(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  2. "Human FIGF: cloning, gene structure, and mapping to chromosome Xp22.1 between the PIGA and the GRPR genes."
    Rocchigiani M., Lestingi M., Luddi A., Orlandini M., Franco B., Rossi E., Ballabio A., Zuffardi O., Oliviero S.
    Genomics 47:207-216(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Lung.
  3. "Vascular endothelial growth factor D (VEGF-D) is a ligand for the tyrosine kinases VEGF receptor 2 (Flk1) and VEGF receptor 3 (Flt4)."
    Achen M.G., Jeltsch M., Kukk E., Maekinen T., Vitali A., Wilks A.F., Alitalo K., Stacker S.A.
    Proc. Natl. Acad. Sci. U.S.A. 95:548-553(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  7. "Biosynthesis of vascular endothelial growth factor-D involves proteolytic processing which generates non-covalent homodimers."
    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.
    J. Biol. Chem. 274:32127-32136(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 89-94; 100-105 AND 206-213, PROTEOLYTIC PROCESSING.
  8. "Structural determinants of vascular endothelial growth factor-D - receptor binding and specificity."
    Leppanen V.M., Jeltsch M., Anisimov A., Tvorogov D., Aho K., Kalkkinen N., Toivanen P., Yla-Herttuala S., Ballmer-Hofer K., Alitalo K.
    Blood 117:1507-1515(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 92-195 OF MUTANT ALA-117, FUNCTION, SUBUNIT, GLYCOSYLATION AT ASN-155 AND ASN-185, DISULFIDE BONDS.

Entry informationi

Entry nameiVEGFD_HUMAN
AccessioniPrimary (citable) accession number: O43915
Secondary accession number(s): B2R7Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: June 1, 1998
Last modified: July 22, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.