Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot O43915 (VEGFD_HUMAN)

Last modified November 25, 2008. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Vascular endothelial growth factor D
      Short name=VEGF-D
Alternative name(s):
    c-fos-induced growth factor
      Short name=FIGF
Gene names
Name: FIGF
Synonyms: VEGFD
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

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 (Flk1) and VEGFR-3 (Flt4) receptors.

Subunit structure

Homodimer; non-covalent and antiparallel.

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.

Post-translational modification

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.

Sequence similarities

Belongs to the PDGF/VEGF growth factor family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 8867Or 99 (in a minor form)
PRO_0000023408
Chain89 – 205117Vascular endothelial growth factor D
PRO_0000023409
Propeptide206 – 354149
PRO_0000023410

Regions

Repeat222 – 237161; approximate
Repeat258 – 273162
Repeat277 – 293173
Repeat301 – 318184
Region222 – 318974 X 16 AA repeats of C-X(10)-C-X-C-X(1,3)-C

Amino acid modifications

Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Disulfide bond111 ↔ 153 By similarity
Disulfide bond136Interchain By similarity
Disulfide bond142 ↔ 189 By similarity
Disulfide bond145Interchain By similarity
Disulfide bond146 ↔ 191 By similarity

Sequences

Sequence LengthMass (Da)Tools
O43915-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 2048D769D735173E

FASTA35440,444
        10         20         30         40         50         60 
MYREWVVVNV FMMLYVQLVQ GSSNEHGPVK RSSQSTLERS EQQIRAASSL EELLRITHSE 

        70         80         90        100        110        120 
DWKLWRCRLR LKSFTSMDSR SASHRSTRFA ATFYDIETLK VIDEEWQRTQ CSPRETCVEV 

       130        140        150        160        170        180 
ASELGKSTNT FFKPPCVNVF RCGGCCNEES LICMNTSTSY ISKQLFEISV PLTSVPELVP 

       190        200        210        220        230        240 
VKVANHTGCK CLPTAPRHPY SIIRRSIQIP EEDRCSHSKK LCPIDMLWDS NKCKCVLQEE 

       250        260        270        280        290        300 
NPLAGTEDHS HLQEPALCGP HMMFDEDRCE CVCKTPCPKD LIQHPKNCSC FECKESLETC 

       310        320        330        340        350 
CQKHKLFHPD TCSCEDRCPF HTRPCASGKT ACAKHCRFPK EKRAAQGPHS RKNP 

« Hide

References

« Hide 'large scale' references
[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: 9205122] [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: 9479493] [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: 9435229] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[5]"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: 10542248] [Abstract]
Cited for: PROTEIN SEQUENCE OF 89-94; 100-105 AND 206-213, PROTEOLYTIC PROCESSING.
+Additional computationally mapped references.

Cross-references

Sequence databases

D89630 mRNA. Translation: BAA24264.1.
Y12863 mRNA. Translation: CAA73370.1.
Y12864 expand/collapse EMBL AC list , Y12865, Y12866, Y12867, Y12868, Y12869, Y12870 Genomic DNA. Translation: CAA73371.1.
AJ000185 mRNA. Translation: CAA03942.1.
BC027948 mRNA. Translation: AAH27948.1.
RefSeqNP_004460.1.
UniGeneHs.11392

3D structure databases

HSSPHSSP built from PDB template 1PDG based on UniProtKB P01127.
ModBaseSearch...

PTM databases

PhosphoSiteO43915.

Genome annotation databases

EnsemblENSG00000165197. Homo sapiens. [Contig view]
GeneID2277.
KEGGhsa:2277.

Organism-specific databases

H-InvDBHIX0016668.
HGNCHGNC:3708. FIGF.
MIM300091. gene.
PharmGKBPA28146.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMO43915.
HOVERGENO43915.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressO43915.
CleanExHS_FIGF.
GermOnlineENSG00000165197. Homo sapiens.

Family and domain databases

InterProIPR000072. PD_growth_factor.
[Graphical view]
PfamPF00341. PDGF. 1 hit.
[Graphical view]
ProDomPD001629. PD_growth_factor. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00141. PDGF. 1 hit.
[Graphical view]
PROSITEPS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio9261.
SOURCESearch...

Entry information

Entry nameVEGFD_HUMAN
AccessionPrimary (citable) accession number: O43915
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: June 1, 1998
Last modified: November 25, 2008
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents