ID   GDF9_CAPHI              Reviewed;         453 AA.
AC   Q66NC0;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Growth/differentiation factor 9;
DE            Short=GDF-9;
DE   Flags: Precursor;
GN   Name=GDF9;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Wu Z.-H., Chu M.-X., Li X.-W.;
RT   "Single nucleotide polymorphism analysis in goat growth differentiation
RT   factor 9.";
RL   Submitted (JUL-2004) 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}.
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DR   EMBL; AY681349; AAU09020.1; -; Genomic_DNA.
DR   EMBL; AY682555; AAU09020.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q66NC0; -.
DR   STRING; 9925.ENSCHIP00000003958; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
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..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..318
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033978"
FT   CHAIN           319..453
FT                   /note="Growth/differentiation factor 9"
FT                   /id="PRO_0000033979"
FT   REGION          282..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;  51875 MW;  FA632736E0D638C3 CRC64;
     MALPNKFFLW FCCFAWLCFP ISLDSLPSRG EAQIVARTAL ESEAETWSLL NHLGGRHRPG
     LLSPLLKVLY DGHGEPPRLQ PDDRALRYMK RLYKAYATKE GTPKSNRRHL YNTVRLFTPC
     AQHKQAPGDL AAGTFPSVDL LFNLDRVTVV EHLFKSVLLY TFNNSISFPF PVKCICNLVI
     KEPEFSSKTL PRAPYSFTYN SQFEFRKKYK WMEIDVTAPL EPLVASHKRN IHMSVNFTCA
     KDQLQHPSAR DSLFNMTLLV APSLLLYLND TSAQAFHRWH SLHPKRKPSQ GPDQRRELSA
     YPVGEEAAEG VRSSRHRRDQ ESVSSELKKP LVPASANLSE YFKQFLFPQN ECELHDFRLS
     FSQLKWDNWI VAPHKYNPRY CKGDCPRAVG HRYGSPVHTM VQNIIHEKLD SSVPRPSCVP
     AKYSPLSVLA IEPDGSIAYK EYEDMIATKC TCR