BMP15_MOUSE
ID BMP15_MOUSE Reviewed; 392 AA.
AC Q9Z0L4; Q3UT46;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Bone morphogenetic protein 15;
DE Short=BMP-15;
DE AltName: Full=Growth/differentiation factor 9B;
DE Short=GDF-9B;
DE Flags: Precursor;
GN Name=Bmp15; Synonyms=Gdf9b;
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].
RC STRAIN=C57BL/6 X 129/Sv; TISSUE=Ovary;
RX PubMed=9849956; DOI=10.1210/mend.12.12.0206;
RA Dube J.L., Wang P., Elvin J., Lyons K.M., Celeste A.J., Matzuk M.M.;
RT "The bone morphogenetic protein 15 gene is X-linked and expressed in
RT oocytes.";
RL Mol. Endocrinol. 12:1809-1817(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 139-392.
RC STRAIN=NMRI; TISSUE=Ovary;
RX PubMed=9858711; DOI=10.1016/s0925-4773(98)00161-0;
RA Laitinen M., Vuojolainen K., Jaatinen R., Ketola I., Aaltonen J.,
RA Lehtonen E., Heikinheimo M., Ritvos O.;
RT "A novel growth differentiation factor-9 (GDF-9) related factor is co-
RT expressed with GDF-9 in mouse oocytes during folliculogenesis.";
RL Mech. Dev. 78:135-140(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NMRI; TISSUE=Ovary;
RX PubMed=10612437; DOI=10.1016/s0303-7207(99)00100-8;
RA Jaatinen R., Laitinen M.P., Vuojolainen K., Aaltonen J., Louhio H.,
RA Heikinheimo K., Lehtonen E., Ritvos O.;
RT "Localization of growth differentiation factor-9 (GDF-9) mRNA and protein
RT in rat ovaries and cDNA cloning of rat GDF-9 and its novel homolog GDF-
RT 9B.";
RL Mol. Cell. Endocrinol. 156:189-193(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May be involved in follicular development. Oocyte-specific
CC growth/differentiation factor that stimulates folliculogenesis and
CC granulosa cell (GC) growth (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). But, in contrast to other members
CC of this family, cannot be disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Ovary specific.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; AF082348; AAC99766.1; -; mRNA.
DR EMBL; AJ010259; CAA09053.1; -; mRNA.
DR EMBL; AJ132406; CAB40966.1; -; mRNA.
DR EMBL; AK028735; BAC26090.1; -; mRNA.
DR EMBL; AK135757; BAE22642.1; -; mRNA.
DR EMBL; AK139773; BAE24134.1; -; mRNA.
DR EMBL; BC055363; AAH55363.1; -; mRNA.
DR CCDS; CCDS29958.1; -.
DR RefSeq; NP_033887.1; NM_009757.5.
DR AlphaFoldDB; Q9Z0L4; -.
DR STRING; 10090.ENSMUSP00000024049; -.
DR GlyGen; Q9Z0L4; 5 sites.
DR iPTMnet; Q9Z0L4; -.
DR PhosphoSitePlus; Q9Z0L4; -.
DR PaxDb; Q9Z0L4; -.
DR PRIDE; Q9Z0L4; -.
DR Antibodypedia; 26314; 358 antibodies from 37 providers.
DR DNASU; 12155; -.
DR Ensembl; ENSMUST00000024049; ENSMUSP00000024049; ENSMUSG00000023279.
DR GeneID; 12155; -.
DR KEGG; mmu:12155; -.
DR UCSC; uc009skx.2; mouse.
DR CTD; 9210; -.
DR MGI; MGI:1316745; Bmp15.
DR VEuPathDB; HostDB:ENSMUSG00000023279; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000160940; -.
DR HOGENOM; CLU_055377_0_0_1; -.
DR InParanoid; Q9Z0L4; -.
DR OMA; VYRHQLH; -.
DR OrthoDB; 724783at2759; -.
DR PhylomeDB; Q9Z0L4; -.
DR TreeFam; TF316134; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 12155; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9Z0L4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9Z0L4; protein.
DR Bgee; ENSMUSG00000023279; Expressed in secondary oocyte and 39 other tissues.
DR Genevisible; Q9Z0L4; 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:0060016; P:granulosa cell development; IEA:InterPro.
DR GO; GO:0001541; P:ovarian follicle development; IEA:InterPro.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR015923; BMP-15.
DR InterPro; IPR029034; Cystine-knot_cytokine.
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:SF22; PTHR11848:SF22; 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 Cytokine; Disulfide bond; Glycoprotein; Growth factor; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..267
FT /evidence="ECO:0000250"
FT /id="PRO_0000033894"
FT CHAIN 268..392
FT /note="Bone morphogenetic protein 15"
FT /id="PRO_0000033895"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
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 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 291..357
FT /evidence="ECO:0000250"
FT DISULFID 320..389
FT /evidence="ECO:0000250"
FT DISULFID 324..391
FT /evidence="ECO:0000250"
SQ SEQUENCE 392 AA; 44898 MW; CA9467FD0AA5737E CRC64;
MALLTILRIL LWGVVLFMEQ RVQMAKPGWP STALLADDPT LPSILDLAKE APGKEMKQWP
QGYPLRYMLK LYHRSADPHG HPRENRTIGA KMVRLVKPSA NTVRPPRGSW HVQTLDFPLA
SNQVAYELIR ATVVYRHQLH LVNYHLSCHV ETWVPKCRTK HLPSSKSGSS KPSPMSKAWT
EIDITHCIQQ KLWNRKGRSV LRLRFMCQQQ KGNETREFRW HGMTSLDVAF LLLYFNDTDD
RVQGKLLARG QEELTDRESS FLMRSVRQAC SIESDASCPS QEHDGSVNNQ CSLHPYKVSF
HQLGWDHWII APRLYTPNYC KGICTRVLPY GLNSPNHAII QSLVNELVNH SVPQPSCVPY
NFLPMSILLI ETNGSILYKE YEGMIAQSCT CR
