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GDF9_MOUSE
ID   GDF9_MOUSE              Reviewed;         441 AA.
AC   Q07105;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Growth/differentiation factor 9;
DE            Short=GDF-9;
DE   Flags: Precursor;
GN   Name=Gdf9; Synonyms=Gdf-9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8429021; DOI=10.1016/s0021-9258(18)53714-5;
RA   McPherron A.C., Lee S.-J.;
RT   "GDF-3 and GDF-9: two new members of the transforming growth factor-beta
RT   superfamily containing a novel pattern of cysteines.";
RL   J. Biol. Chem. 268:3444-3449(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvEv;
RX   PubMed=8186260; DOI=10.1016/0167-4889(94)90034-5;
RA   Incerti B., Dong J., Borsani G., Matzuk M.M.;
RT   "Structure of the mouse growth/differentiation factor 9 gene.";
RL   Biochim. Biophys. Acta 1222:125-128(1994).
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.
CC   -!- SUBUNIT: Homodimer or heterodimer (Potential). But, in contrast to
CC       other members of this family, cannot be disulfide-linked.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ovary.
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; L06444; AAA53035.1; -; mRNA.
DR   EMBL; X77112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X77113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS24679.1; -.
DR   PIR; S45284; S45284.
DR   RefSeq; NP_032136.2; NM_008110.2.
DR   AlphaFoldDB; Q07105; -.
DR   IntAct; Q07105; 1.
DR   STRING; 10090.ENSMUSP00000018382; -.
DR   GlyGen; Q07105; 4 sites.
DR   iPTMnet; Q07105; -.
DR   PhosphoSitePlus; Q07105; -.
DR   PaxDb; Q07105; -.
DR   PRIDE; Q07105; -.
DR   Antibodypedia; 26178; 566 antibodies from 31 providers.
DR   DNASU; 14566; -.
DR   Ensembl; ENSMUST00000018382; ENSMUSP00000018382; ENSMUSG00000018238.
DR   GeneID; 14566; -.
DR   KEGG; mmu:14566; -.
DR   UCSC; uc007iwa.2; mouse.
DR   CTD; 2661; -.
DR   MGI; MGI:95692; Gdf9.
DR   VEuPathDB; HostDB:ENSMUSG00000018238; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   GeneTree; ENSGT00940000159784; -.
DR   HOGENOM; CLU_055377_1_0_1; -.
DR   InParanoid; Q07105; -.
DR   OMA; CAQHKQA; -.
DR   OrthoDB; 724783at2759; -.
DR   PhylomeDB; Q07105; -.
DR   TreeFam; TF351788; -.
DR   BioGRID-ORCS; 14566; 0 hits in 72 CRISPR screens.
DR   ChiTaRS; Gdf9; mouse.
DR   PRO; PR:Q07105; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q07105; protein.
DR   Bgee; ENSMUSG00000018238; Expressed in secondary oocyte and 68 other tissues.
DR   ExpressionAtlas; Q07105; baseline and differential.
DR   Genevisible; Q07105; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
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; IMP:MGI.
DR   GO; GO:0001555; P:oocyte growth; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR   GO; GO:2000870; P:regulation of progesterone secretion; ISO:MGI.
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..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..306
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033982"
FT   CHAIN           307..441
FT                   /note="Growth/differentiation factor 9"
FT                   /id="PRO_0000033983"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        340..406
FT                   /evidence="ECO:0000250"
FT   DISULFID        369..438
FT                   /evidence="ECO:0000250"
FT   DISULFID        373..440
FT                   /evidence="ECO:0000250"
FT   CONFLICT        296
FT                   /note="I -> T (in Ref. 1; AAA53035)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   441 AA;  49649 MW;  43B47ADD41B99C29 CRC64;
     MALPSNFLLG VCCFAWLCFL SSLSSQASTE ESQSGASENV ESEADPWSLL LPVDGTDRSG
     LLPPLFKVLS DRRGETPKLQ PDSRALYYMK KLYKTYATKE GVPKPSRSHL YNTVRLFSPC
     AQQEQAPSNQ VTGPLPMVDL LFNLDRVTAM EHLLKSVLLY TLNNSASSSS TVTCMCDLVV
     KEAMSSGRAP PRAPYSFTLK KHRWIEIDVT SLLQPLVTSS ERSIHLSVNF TCTKDQVPED
     GVFSMPLSVP PSLILYLNDT STQAYHSWQS LQSTWRPLQH PGQAGVAARP VKEEAIEVER
     SPRRRRGQKA IRSEAKGPLL TASFNLSEYF KQFLFPQNEC ELHDFRLSFS QLKWDNWIVA
     PHRYNPRYCK GDCPRAVRHR YGSPVHTMVQ NIIYEKLDPS VPRPSCVPGK YSPLSVLTIE
     PDGSIAYKEY EDMIATRCTC R
 
 
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