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Protein

Growth/differentiation factor 3

Gene

Gdf3

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

Functioni

GO - Molecular functioni

GO - Biological processi

  • endoderm development Source: MGI
  • eye development Source: UniProtKB
  • formation of anatomical boundary Source: MGI
  • growth Source: InterPro
  • in utero embryonic development Source: MGI
  • mesoderm development Source: MGI
  • negative regulation of BMP signaling pathway Source: UniProtKB
  • negative regulation of epidermal cell differentiation Source: UniProtKB
  • negative regulation of myoblast differentiation Source: MGI
  • notochord development Source: MGI
  • primitive streak formation Source: MGI
  • regulation of cell fate commitment Source: UniProtKB
  • response to dietary excess Source: MGI
  • signal transduction Source: MGI
  • skeletal system development Source: UniProtKB
  • somite rostral/caudal axis specification Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor

Names & Taxonomyi

Protein namesi
Recommended name:
Growth/differentiation factor 3
Short name:
GDF-3
Alternative name(s):
VG-1-related protein 2
Gene namesi
Name:Gdf3
Synonyms:Gdf-3, Vgr-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:95686. Gdf3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 252230Sequence analysisPRO_0000033910Add
BLAST
Chaini253 – 366114Growth/differentiation factor 3PRO_0000033911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence analysis
Disulfide bondi266 ↔ 331By similarity
Disulfide bondi295 ↔ 363By similarity
Disulfide bondi299 ↔ 365By similarity
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ07104.
PRIDEiQ07104.

PTM databases

iPTMnetiQ07104.
PhosphoSiteiQ07104.

Expressioni

Tissue specificityi

Primarily in adult bone marrow, spleen, thymus and adipose tissue.

Gene expression databases

BgeeiQ07104.
CleanExiMM_GDF3.
GenevisibleiQ07104. MM.

Interactioni

Subunit structurei

Homodimer or heterodimer (Potential). But, in contrast to other members of this family, cannot be disulfide-linked.Curated

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199887. 1 interaction.
STRINGi10090.ENSMUSP00000032211.

Structurei

3D structure databases

ProteinModelPortaliQ07104.
SMRiQ07104. Positions 266-365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3900. Eukaryota.
ENOG410XT8Z. LUCA.
GeneTreeiENSGT00760000118883.
HOGENOMiHOG000249476.
HOVERGENiHBG004860.
InParanoidiQ07104.
KOiK05495.
OMAiYFNLSAI.
OrthoDBiEOG71CFMF.
TreeFamiTF351789.

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.

Q07104-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPYQRLLAL GFLLLTLPWG QTSEFQDSDL LQFLGLEKAP SPHRFQPVPR
60 70 80 90 100
VLRKIIRARE AAAASGASQD LCYVKELGVR GNLLQLLPDQ GFFLNTQKPF
110 120 130 140 150
QDGSCLQKVL YFNLSAIKEK AKLTMAQLTL DLGPRSYYNL RPELVVALSV
160 170 180 190 200
VQDRGVWGRS HPKVGRLLFL RSVPGPQGQL QFNLQGALKD WSSNRLKNLD
210 220 230 240 250
LHLEILVKED RYSRVTVQPE NPCDRLLRSL HASLLVVTLN PKHCHPSSRK
260 270 280 290 300
RRAAISVPKG FCRNFCHRHQ LFINFQDLGW HKWVIAPKGF MANYCHGECP
310 320 330 340 350
FSMTTYLNSS NYAFMQALMH MADPKVPKAV CVPTKLSPIS MLYQDSDKNV
360
ILRHYEDMVV DECGCG
Length:366
Mass (Da):41,586
Last modified:July 27, 2011 - v2
Checksum:i3DCD7CB8F9470293
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651G → R in AAB24876 (PubMed:1480182).Curated
Sequence conflicti167 – 1682LL → FV in AAB24876 (PubMed:1480182).Curated
Sequence conflicti225 – 2251R → P in AAA53034 (PubMed:8429021).Curated
Sequence conflicti225 – 2251R → P in AAB24876 (PubMed:1480182).Curated
Sequence conflicti313 – 3131A → R in AAB24876 (PubMed:1480182).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06443 mRNA. Translation: AAA53034.1.
S52658 mRNA. Translation: AAB24876.1.
AK152457 mRNA. Translation: BAE31235.1.
AK160533 mRNA. Translation: BAE35850.1.
CCDSiCCDS20499.1.
PIRiA45402.
A46607.
RefSeqiNP_032134.2. NM_008108.4.
UniGeneiMm.299742.

Genome annotation databases

EnsembliENSMUST00000032211; ENSMUSP00000032211; ENSMUSG00000030117.
GeneIDi14562.
KEGGimmu:14562.
UCSCiuc009dpm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06443 mRNA. Translation: AAA53034.1.
S52658 mRNA. Translation: AAB24876.1.
AK152457 mRNA. Translation: BAE31235.1.
AK160533 mRNA. Translation: BAE35850.1.
CCDSiCCDS20499.1.
PIRiA45402.
A46607.
RefSeqiNP_032134.2. NM_008108.4.
UniGeneiMm.299742.

3D structure databases

ProteinModelPortaliQ07104.
SMRiQ07104. Positions 266-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199887. 1 interaction.
STRINGi10090.ENSMUSP00000032211.

PTM databases

iPTMnetiQ07104.
PhosphoSiteiQ07104.

Proteomic databases

PaxDbiQ07104.
PRIDEiQ07104.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032211; ENSMUSP00000032211; ENSMUSG00000030117.
GeneIDi14562.
KEGGimmu:14562.
UCSCiuc009dpm.1. mouse.

Organism-specific databases

CTDi9573.
MGIiMGI:95686. Gdf3.

Phylogenomic databases

eggNOGiKOG3900. Eukaryota.
ENOG410XT8Z. LUCA.
GeneTreeiENSGT00760000118883.
HOGENOMiHOG000249476.
HOVERGENiHBG004860.
InParanoidiQ07104.
KOiK05495.
OMAiYFNLSAI.
OrthoDBiEOG71CFMF.
TreeFamiTF351789.

Miscellaneous databases

PROiQ07104.
SOURCEiSearch...

Gene expression databases

BgeeiQ07104.
CleanExiMM_GDF3.
GenevisibleiQ07104. MM.

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. "GDF-3 and GDF-9: two new members of the transforming growth factor-beta superfamily containing a novel pattern of cysteines."
    McPherron A.C., Lee S.-J.
    J. Biol. Chem. 268:3444-3449(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Isolation of Vgr-2, a novel member of the transforming growth factor-beta-related gene family."
    Jones C.M., Simon-Chazottes D., Guenet J.-L., Hogan B.L.
    Mol. Endocrinol. 6:1961-1968(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Bone marrow.

Entry informationi

Entry nameiGDF3_MOUSE
AccessioniPrimary (citable) accession number: Q07104
Secondary accession number(s): Q3TUX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 120 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.