GDF9_SHEEP
ID GDF9_SHEEP Reviewed; 453 AA.
AC O77681;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Growth/differentiation factor 9;
DE Short=GDF-9;
DE Flags: Precursor;
GN Name=GDF9;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9916005; DOI=10.1095/biolreprod60.2.381;
RA Bodensteiner K.J., Clay C.M., Moeller C.L., Sawyer H.R.;
RT "Molecular cloning of the ovine Growth/Differentiation factor-9 gene and
RT expression of growth/differentiation factor-9 in ovine and bovine
RT ovaries.";
RL Biol. Reprod. 60:381-386(1999).
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.
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; AF078545; AAC28089.2; -; Genomic_DNA.
DR RefSeq; NP_001136360.2; NM_001142888.2.
DR AlphaFoldDB; O77681; -.
DR SMR; O77681; -.
DR STRING; 9940.ENSOARP00000014175; -.
DR Ensembl; ENSOART00020032535; ENSOARP00020026884; ENSOARG00020021050.
DR GeneID; 100217402; -.
DR KEGG; oas:100217402; -.
DR CTD; 2661; -.
DR eggNOG; KOG3900; Eukaryota.
DR OrthoDB; 724783at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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 GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR GO; GO:0001555; P:oocyte growth; IEA:Ensembl.
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..27
FT /evidence="ECO:0000255"
FT PROPEP 28..318
FT /evidence="ECO:0000255"
FT /id="PRO_0000033984"
FT CHAIN 319..453
FT /note="Growth/differentiation factor 9"
FT /id="PRO_0000033985"
FT REGION 304..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 352..418
FT /evidence="ECO:0000250"
FT DISULFID 381..450
FT /evidence="ECO:0000250"
FT DISULFID 385..452
FT /evidence="ECO:0000250"
SQ SEQUENCE 453 AA; 51776 MW; 1911A66A720E2B85 CRC64;
MALPNKFFLW FCCFAWLCFP ISLDSLPSRG EAQIVARTAL ESEAETWSLL NHLGGRHRPG
LLSPLLEVLY DGHGEPPRLQ PDDRALRYMK RLYKAYATKE GTPKSNRRHL YNTVRLFTPC
AQHKQAPGDL AAGTFPSVDL LFNLDRVTVV EHLFKSVLLY TFNNSISFPF PVKCICNLVI
KEPEFSSKTL PRAPYSFTYN SQFEFRKKYK WMEIDVTAPL EPLVASHKRN IHMSVNFTCA
EDQLQHPSAR DSLFNMTLLV APSLLLYLND TSAQAFHRWH SLHPKRKPSQ GPDQKRGLSA
YPVGEEAAEG VRSSRHRRDQ ESASSELKKP LVPASVNLSE YFKQFLFPQN ECELHDFRLS
FSQLKWDNWI VAPHKYNPRY CKGDCPRAVG HRYGSPVHTM VQNIIHEKLD SSVPRPSCVP
AKYSPLSVLA IEPDGSIAYK EYEDMIATKC TCR
