Q9WV56 (GDF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Growth/differentiation factor 2
Short name=GDF-2

Alternative name(s):
Bone morphogenetic protein 9
Short name=BMP-9

Gene names

Name:	Gdf2
Synonyms:	Bmp9

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Potent circulating inhibitor of angiogenesis. Could be involved in bone formation. Signals through the type I activin receptor ACVRL1 but not other Alks By similarity.
Subunit structure	Homodimer; disulfide-linked By similarity.
Subcellular location	Secreted.
Sequence similarities	Belongs to the TGF-beta family.

Ontologies

Keywords
Biological process	Angiogenesis
Cellular component	Secreted
Domain	Signal
Molecular function	Cytokine Growth factor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Inferred from electronic annotation. Source: Compara activin receptor signaling pathway Inferred from electronic annotation. Source: Compara cellular iron ion homeostasis Traceable author statement PubMed 20406889. Source: DFLAT glucose metabolic process Traceable author statement PubMed 20406889. Source: DFLAT growth Inferred from electronic annotation. Source: InterPro negative regulation of DNA biosynthetic process Inferred from electronic annotation. Source: Compara negative regulation of cell growth Inferred from electronic annotation. Source: Compara negative regulation of endothelial cell migration Inferred from electronic annotation. Source: Compara negative regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Compara neuron differentiation Traceable author statement PubMed 20406889. Source: DFLAT osteoblast differentiation Inferred from genetic interaction PubMed 18986983. Source: MGI pathway-restricted SMAD protein phosphorylation Inferred from electronic annotation. Source: Compara patterning of blood vessels Inferred from direct assay PubMed 20406889. Source: DFLAT positive regulation of BMP signaling pathway Inferred from direct assay PubMed 20406889. Source: DFLAT positive regulation of angiogenesis Inferred from direct assay PubMed 20406889. Source: DFLAT positive regulation of endothelial cell differentiation Inferred from direct assay PubMed 20406889. Source: DFLAT positive regulation of endothelial cell proliferation Inferred from direct assay PubMed 20406889. Source: DFLAT positive regulation of interleukin-8 production Inferred from electronic annotation. Source: Compara positive regulation of osteoblast differentiation Inferred from genetic interaction PubMed 15161906. Source: MGI positive regulation of pathway-restricted SMAD protein phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 18986983. Source: MGI vasculogenesis Inferred from direct assay PubMed 20406889. Source: DFLAT
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Propeptide	23 – 318	296	By similarity		PRO_0000033904
	Chain	319 – 428	110	Growth/differentiation factor 2		PRO_0000033905
Amino acid modifications
	Glycosylation	70	1	N-linked (GlcNAc...) Potential
	Glycosylation	135	1	N-linked (GlcNAc...) Potential
	Glycosylation	262	1	N-linked (GlcNAc...) Potential
	Disulfide bond	326 ↔ 392		By similarity
	Disulfide bond	355 ↔ 425		By similarity
	Disulfide bond	359 ↔ 427		By similarity
	Disulfide bond	391		Interchain By similarity
Experimental info
	Sequence conflict	293	1	V → G in AAD40308. Ref.1
	Sequence conflict	382	1	K → E in AAD56961. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9WV56 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 82E4475FF8B27F36	FASTA	428	47,703
	10 20 30 40 50 60 MSPGAFRVAL LPLFLLVCVT QQKPLQNWEQ ASPGENAHSS LGLSGAGEEG VFDLQMFLEN 70 80 90 100 110 120 MKVDFLRSLN LSGIPSQDKT RAEPPQYMID LYNRYTTDKS STPASNIVRS FSVEDAISTA 130 140 150 160 170 180 ATEDFPFQKH ILIFNISIPR HEQITRAELR LYVSCQNDVD STHGLEGSMV VYDVLEDSET 190 200 210 220 230 240 WDQATGTKTF LVSQDIRDEG WETLEVSSAV KRWVRADSTT NKNKLEVTVQ SHRESCDTLD 250 260 270 280 290 300 ISVPPGSKNL PFFVVFSNDR SNGTKETRLE LKEMIGHEQE TMLVKTAKNA YQVAGESQEE 310 320 330 340 350 360 EGLDGYTAVG PLLARRKRST GASSHCQKTS LRVNFEDIGW DSWIIAPKEY DAYECKGGCF 370 380 390 400 410 420 FPLADDVTPT KHAIVQTLVH LKFPTKVGKA CCVPTKLSPI SILYKDDMGV PTLKYHYEGM SVAECGCR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00125268.
RefSeq	NP_062379.3. NM_019506.4.
UniGene	Mm.422844.
3D structure databases
ProteinModelPortal	Q9WV56.
SMR	Q9WV56. Positions 324-428.
ModBase	Search...
PTM databases
PhosphoSite	Q9WV56.
Proteomic databases
PRIDE	Q9WV56.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000100720; ENSMUSP00000098286; ENSMUSG00000072625.
GeneID	12165.
KEGG	mmu:12165.
UCSC	uc007tac.1. mouse.
Organism-specific databases
CTD	2658.
MGI	MGI:1321394. Gdf2.
Phylogenomic databases
eggNOG	NOG280573.
GeneTree	ENSGT00620000087601.
HOGENOM	HOG000249477.
HOVERGEN	HBG106648.
InParanoid	Q3ZAS6.
KO	K05503.
OMA	ENMKVDF.
OrthoDB	EOG48WC29.
Gene expression databases
Bgee	Q9WV56.
CleanEx	MM_GDF2.
Genevestigator	Q9WV56.
GermOnline	ENSMUSG00000072625. Mus musculus.
Family and domain databases
InterPro	IPR002405. Inhibin_asu. IPR001839. TGF-b_C. IPR001111. TGF-b_N. IPR015615. TGF-beta-rel. IPR017948. TGFb_CS. [Graphical view]
PANTHER	PTHR11848. PTHR11848. 1 hit.
Pfam	PF00019. TGF_beta. 1 hit. PF00688. TGFb_propeptide. 1 hit. [Graphical view]
PRINTS	PR00669. INHIBINA.
SMART	SM00204. TGFB. 1 hit. [Graphical view]
PROSITE	PS00250. TGF_BETA_1. 1 hit. PS51362. TGF_BETA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	280527.
SOURCE	Search...

Entry information

Entry name

GDF2_MOUSE

Accession

Primary (citable) accession number: Q9WV56
Secondary accession number(s): Q3ZAS6, Q9QZE0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	July 27, 2011
Last modified:	May 29, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program