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Protein

Growth/differentiation factor 2

Gene

Gdf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Potent circulating inhibitor of angiogenesis. Could be involved in bone formation. Signals through the type I activin receptor ACVRL1 but not other Alks. Signaling through SMAD1 in endothelial cells requires TGF-beta coreceptor endoglin/ENG.1 Publication

GO - Molecular functioni

  1. cytokine activity Source: GO_Central
  2. transforming growth factor beta receptor binding Source: GO_Central

GO - Biological processi

  1. activin receptor signaling pathway Source: MGI
  2. angiogenesis Source: UniProtKB
  3. blood vessel morphogenesis Source: MGI
  4. BMP signaling pathway Source: MGI
  5. cell development Source: GO_Central
  6. cellular iron ion homeostasis Source: DFLAT
  7. cellular response to BMP stimulus Source: MGI
  8. glucose metabolic process Source: DFLAT
  9. growth Source: InterPro
  10. negative regulation of cell growth Source: MGI
  11. negative regulation of DNA biosynthetic process Source: MGI
  12. negative regulation of endothelial cell migration Source: MGI
  13. negative regulation of endothelial cell proliferation Source: MGI
  14. neuron differentiation Source: DFLAT
  15. osteoblast differentiation Source: MGI
  16. pathway-restricted SMAD protein phosphorylation Source: MGI
  17. patterning of blood vessels Source: DFLAT
  18. positive regulation of angiogenesis Source: DFLAT
  19. positive regulation of BMP signaling pathway Source: DFLAT
  20. positive regulation of cartilage development Source: UniProtKB
  21. positive regulation of endothelial cell differentiation Source: DFLAT
  22. positive regulation of endothelial cell proliferation Source: DFLAT
  23. positive regulation of gene expression Source: MGI
  24. positive regulation of interleukin-8 production Source: MGI
  25. positive regulation of osteoblast differentiation Source: MGI
  26. positive regulation of pathway-restricted SMAD protein phosphorylation Source: MGI
  27. positive regulation of transcription, DNA-templated Source: DFLAT
  28. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  29. regulation of apoptotic process Source: GO_Central
  30. regulation of MAPK cascade Source: GO_Central
  31. SMAD protein signal transduction Source: GO_Central
  32. vasculogenesis Source: DFLAT
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor

Keywords - Biological processi

Angiogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Growth/differentiation factor 2
Short name:
GDF-2
Alternative name(s):
Bone morphogenetic protein 9
Short name:
BMP-9
Gene namesi
Name:Gdf2
Synonyms:Bmp9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1321394. Gdf2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: GO_Central
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Propeptidei23 – 318296By similarityPRO_0000033904Add
BLAST
Chaini319 – 428110Growth/differentiation factor 2PRO_0000033905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi135 – 1351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi326 ↔ 392By similarity
Disulfide bondi355 ↔ 425By similarity
Disulfide bondi359 ↔ 427By similarity
Disulfide bondi391 – 391InterchainBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9WV56.

PTM databases

PhosphoSiteiQ9WV56.

Expressioni

Gene expression databases

BgeeiQ9WV56.
CleanExiMM_GDF2.
GenevestigatoriQ9WV56.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Interacts with ENG (By similarity).By similarity

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YCGX-ray3.30A/B23-318[»]
4YCIX-ray3.25A/B23-318[»]
ProteinModelPortaliQ9WV56.
SMRiQ9WV56. Positions 324-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG280573.
GeneTreeiENSGT00760000118883.
HOGENOMiHOG000249477.
HOVERGENiHBG106648.
InParanoidiQ9WV56.
KOiK05503.
OMAiENMKVDF.
OrthoDBiEOG7ZD1V3.
TreeFamiTF316134.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR002405. Inhibin_asu.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PRINTSiPR00669. INHIBINA.
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9WV56-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPGAFRVAL LPLFLLVCVT QQKPLQNWEQ ASPGENAHSS LGLSGAGEEG
60 70 80 90 100
VFDLQMFLEN MKVDFLRSLN LSGIPSQDKT RAEPPQYMID LYNRYTTDKS
110 120 130 140 150
STPASNIVRS FSVEDAISTA ATEDFPFQKH ILIFNISIPR HEQITRAELR
160 170 180 190 200
LYVSCQNDVD STHGLEGSMV VYDVLEDSET WDQATGTKTF LVSQDIRDEG
210 220 230 240 250
WETLEVSSAV KRWVRADSTT NKNKLEVTVQ SHRESCDTLD ISVPPGSKNL
260 270 280 290 300
PFFVVFSNDR SNGTKETRLE LKEMIGHEQE TMLVKTAKNA YQVAGESQEE
310 320 330 340 350
EGLDGYTAVG PLLARRKRST GASSHCQKTS LRVNFEDIGW DSWIIAPKEY
360 370 380 390 400
DAYECKGGCF FPLADDVTPT KHAIVQTLVH LKFPTKVGKA CCVPTKLSPI
410 420
SILYKDDMGV PTLKYHYEGM SVAECGCR
Length:428
Mass (Da):47,703
Last modified:July 27, 2011 - v2
Checksum:i82E4475FF8B27F36
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti293 – 2931V → G in AAD40308 (Ref. 1) Curated
Sequence conflicti382 – 3821K → E in AAD56961 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156890 mRNA. Translation: AAD40308.1.
AF188286 mRNA. Translation: AAD56961.1.
AK147029 mRNA. Translation: BAE27621.1.
CH466573 Genomic DNA. Translation: EDL24862.1.
BC103625 mRNA. Translation: AAI03626.1.
BC103679 mRNA. Translation: AAI03680.1.
BC103680 mRNA. Translation: AAI03681.1.
BC103681 mRNA. Translation: AAI03682.1.
CCDSiCCDS26928.1.
RefSeqiNP_062379.3. NM_019506.4.
UniGeneiMm.422844.

Genome annotation databases

EnsembliENSMUST00000100720; ENSMUSP00000098286; ENSMUSG00000072625.
GeneIDi12165.
KEGGimmu:12165.
UCSCiuc007tac.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF156890 mRNA. Translation: AAD40308.1.
AF188286 mRNA. Translation: AAD56961.1.
AK147029 mRNA. Translation: BAE27621.1.
CH466573 Genomic DNA. Translation: EDL24862.1.
BC103625 mRNA. Translation: AAI03626.1.
BC103679 mRNA. Translation: AAI03680.1.
BC103680 mRNA. Translation: AAI03681.1.
BC103681 mRNA. Translation: AAI03682.1.
CCDSiCCDS26928.1.
RefSeqiNP_062379.3. NM_019506.4.
UniGeneiMm.422844.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4YCGX-ray3.30A/B23-318[»]
4YCIX-ray3.25A/B23-318[»]
ProteinModelPortaliQ9WV56.
SMRiQ9WV56. Positions 324-428.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9WV56.

Proteomic databases

PRIDEiQ9WV56.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000100720; ENSMUSP00000098286; ENSMUSG00000072625.
GeneIDi12165.
KEGGimmu:12165.
UCSCiuc007tac.1. mouse.

Organism-specific databases

CTDi2658.
MGIiMGI:1321394. Gdf2.

Phylogenomic databases

eggNOGiNOG280573.
GeneTreeiENSGT00760000118883.
HOGENOMiHOG000249477.
HOVERGENiHBG106648.
InParanoidiQ9WV56.
KOiK05503.
OMAiENMKVDF.
OrthoDBiEOG7ZD1V3.
TreeFamiTF316134.

Miscellaneous databases

NextBioi280527.
PROiQ9WV56.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WV56.
CleanExiMM_GDF2.
GenevestigatoriQ9WV56.

Family and domain databases

Gene3Di2.10.90.10. 1 hit.
InterProiIPR029034. Cystine-knot_cytokine.
IPR002405. Inhibin_asu.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERiPTHR11848. PTHR11848. 1 hit.
PfamiPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PRINTSiPR00669. INHIBINA.
SMARTiSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMiSSF57501. SSF57501. 1 hit.
PROSITEiPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Growth/differentiation factor-2, a new TGF-beta family member with bone promoting activities."
    Zimmers T.A., Koniaris L.G., Sitzmann J.V., Lee S.-J.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
    Tissue: Liver.
  2. Celeste A.J.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
  6. "Endoglin requirement for BMP9 signaling in endothelial cells reveals new mechanism of action for selective anti-endoglin antibodies."
    Nolan-Stevaux O., Zhong W., Culp S., Shaffer K., Hoover J., Wickramasinghe D., Ruefli-Brasse A.
    PLoS ONE 7:E50920-E50920(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiGDF2_MOUSE
AccessioniPrimary (citable) accession number: Q9WV56
Secondary accession number(s): Q3ZAS6, Q9QZE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: July 27, 2011
Last modified: April 29, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.