GDF9_PAPAN
ID GDF9_PAPAN Reviewed; 455 AA.
AC A9CB18;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Growth/differentiation factor 9;
DE Short=GDF-9;
DE Flags: Precursor;
GN Name=GDF9;
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA Tsipouri V., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SPECIES-SPECIFIC OVULATION RATE DETERMINATION.
RX PubMed=21970812; DOI=10.1016/j.mce.2011.09.033;
RA Crawford J.L., McNatty K.P.;
RT "The ratio of growth differentiation factor 9: bone morphogenetic protein
RT 15 mRNA expression is tightly co-regulated and differs between species over
RT a wide range of ovulation rates.";
RL Mol. Cell. Endocrinol. 348:339-343(2012).
CC -!- FUNCTION: Required for ovarian folliculogenesis. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer or heterodimer (Potential). But, in contrast to
CC other members of this family, cannot be disulfide-linked (By
CC similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Phosphorylated; phosphorylation is critical for GDF9 function.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Ovarian physiology and fertility are controlled by
CC endocrine and paracrine signals. These act in a species-dependent
CC manner and determine the ovulation quota in different mammalian
CC species. While humans, and mammals such as the cow or red deer,
CC normally ovulate only one egg per cycle, other mammals such as mouse
CC and pig can ovulate in excess of ten per cycle. The mechanisms that
CC regulate the species-specific differences in the number of follicles
CC that go onto ovulate during each reproductive cycle are poorly
CC understood. According to PubMed:21970812, mRNA expression levels of
CC GDF9 and BMP15 are tightly coregulated within each species and
CC influence species-specific ovulation-rates.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DP000485; ABW96807.1; -; Genomic_DNA.
DR RefSeq; NP_001162234.1; NM_001168763.1.
DR AlphaFoldDB; A9CB18; -.
DR STRING; 9555.ENSPANP00000010764; -.
DR PRIDE; A9CB18; -.
DR GeneID; 100137225; -.
DR KEGG; panu:100137225; -.
DR CTD; 2661; -.
DR eggNOG; KOG3900; Eukaryota.
DR OrthoDB; 724783at2759; -.
DR Proteomes; UP000028761; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR015617; Growth_differentiation_fac-9.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR PANTHER; PTHR11848:SF19; PTHR11848:SF19; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; Cytokine; Disulfide bond; Glycoprotein;
KW Growth factor; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..320
FT /evidence="ECO:0000255"
FT /id="PRO_0000328805"
FT CHAIN 321..455
FT /note="Growth/differentiation factor 9"
FT /id="PRO_0000328806"
FT REGION 305..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 354..420
FT /evidence="ECO:0000250"
FT DISULFID 383..452
FT /evidence="ECO:0000250"
FT DISULFID 387..454
FT /evidence="ECO:0000250"
SQ SEQUENCE 455 AA; 51713 MW; B0306A60BF747B66 CRC64;
MALPNKFLLW FYCFAWLCFP VSLGSQASGG DAQIAASAEL ESGATPWSLL QPIDERDRAG
LLPPLFKVLS VGRGGAPRLQ PDSRALHYMK NLYKTYATKE GIPKSNRSHL YNTVRLFTPC
TQHKQVPGDQ VTGILPSVDL LFNLDRITTV EHLLKSVLLY TINNSVSFSS AVKCVCNLMI
KEPKFSSKTL HRALYSFTFN SQFEFGKKHK WIEIDVTSLL QPLVASNKRS IHMSINFTCM
KDQLEHPSAQ NGLFNMTLLV PPSLILYLND TSAQAYHRWY SLYYKRRPSQ GPDQERSLSA
YPVGEDAAED GRSSHHRHRR GQETVSSELK KPLVPASFNL SEYFKQFLFP QNECELHDFR
LSFSQLKWDN WIVAPHRYNP RYCKGDCPRA VGHRYGSPVH TMVQNIIYEK LDSSVPRPSC
VPAKYSPLSV LTIEPDGSIA YKEYEDMIAT KCTCR
