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GDF9_BOVIN
ID   GDF9_BOVIN              Reviewed;         453 AA.
AC   Q9GK68;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Growth/differentiation factor 9;
DE            Short=GDF-9;
DE   Flags: Precursor;
GN   Name=GDF9;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11918837; DOI=10.1089/152045501300189286;
RA   Sendai Y., Itoh T., Yamashita S., Hoshi H.;
RT   "Molecular cloning of a cDNA encoding a bovine growth differentiation
RT   factor-9 (GDF-9) and expression of GDF-9 in bovine ovarian oocytes and in
RT   vitro-produced embryos.";
RL   Cloning 3:3-10(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Smith T.P.L., Kappes S.M.;
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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; AB058416; BAB39768.1; -; mRNA.
DR   EMBL; AF307092; AAG38106.1; -; mRNA.
DR   RefSeq; NP_777106.1; NM_174681.2.
DR   AlphaFoldDB; Q9GK68; -.
DR   SMR; Q9GK68; -.
DR   STRING; 9913.ENSBTAP00000012476; -.
DR   PaxDb; Q9GK68; -.
DR   PRIDE; Q9GK68; -.
DR   Ensembl; ENSBTAT00000012476; ENSBTAP00000012476; ENSBTAG00000009478.
DR   GeneID; 282574; -.
DR   KEGG; bta:282574; -.
DR   CTD; 2661; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009478; -.
DR   VGNC; VGNC:29306; GDF9.
DR   eggNOG; KOG3900; Eukaryota.
DR   GeneTree; ENSGT00940000159784; -.
DR   HOGENOM; CLU_055377_1_0_1; -.
DR   InParanoid; Q9GK68; -.
DR   OMA; CAQHKQA; -.
DR   OrthoDB; 724783at2759; -.
DR   TreeFam; TF351788; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000009478; Expressed in oocyte and 79 other tissues.
DR   ExpressionAtlas; Q9GK68; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0070698; F:type I activin receptor binding; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0001555; P:oocyte growth; IEA:Ensembl.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Cytokine; Disulfide bond; Glycoprotein;
KW   Growth factor; Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..318
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000244403"
FT   CHAIN           319..453
FT                   /note="Growth/differentiation factor 9"
FT                   /id="PRO_0000244404"
FT   REGION          281..300
FT                   /note="Disordered"
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        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;  51933 MW;  2A581B89FA144185 CRC64;
     MALPNKFFLW FCCFAWLCFP ISLDSQPSRG EAQIVARTAL ESEAETWSLL KHLDGRHRPG
     LLSPLLNVLY DGHREPPRLQ PDDRALSYMK RLYKAYATKE GTPKSNRSHL YNTVRLFTPC
     AQHKQAPGDQ AAGTLPSVDL LFNLDRVTVV EHLFKSVLLY TFNNSISFPF PVKCICNLVI
     KEPEFSSKTL PRAPYSFTFN SQFEFRKKYK WIEIDVTAPL EPLVASHKRN IHMSVNFTCV
     KDQLQHPSAR DSLFNMTLLL APSLLLYLND TSAQAFHRWH SLHPKRKPSQ DPDQKRGLSA
     CPMGEEAAEG VRLSRHRRDQ ESVSSELKKP LVPASFNLSE YFKQFLFPQN ECELHDFRLS
     FSQLKWDNWI VAPHKYNPRY CKGDCPRAVG HRYGSPVHTM VMNIIHEKLD SSVPRPSCVP
     AKYSPLSVLA IEPDGSIAYK EYEDMIATKC TCR
 
 
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