BMP15_BOVIN
ID BMP15_BOVIN Reviewed; 394 AA.
AC Q6PX77;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Bone morphogenetic protein 15;
DE Short=BMP-15;
DE Flags: Precursor;
GN Name=BMP15;
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=15189828; DOI=10.1095/biolreprod.104.030288;
RA Pennetier S., Uzbekova S., Perreau C., Papillier P., Mermillod P.,
RA Dalbies-Tran R.;
RT "Spatio-temporal expression of the germ cell marker genes MATER, ZAR1,
RT GDF9, BMP15, and VASA in adult bovine tissues, oocytes, and preimplantation
RT embryos.";
RL Biol. Reprod. 71:1359-1366(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Liu Y.B., Qi Y., Wang F., Rong W.;
RT "Cloning of the cattle BMP15 gene.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in follicular development. Seems to be an
CC oocyte-specific growth/differentiation factor that stimulates
CC folliculogenesis and granulosa cell (GC) growth (By similarity).
CC {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 -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; AY572412; AAS99651.1; -; mRNA.
DR EMBL; DQ463368; ABE97096.1; -; mRNA.
DR RefSeq; NP_001026922.1; NM_001031752.1.
DR AlphaFoldDB; Q6PX77; -.
DR SMR; Q6PX77; -.
DR STRING; 9913.ENSBTAP00000056137; -.
DR PaxDb; Q6PX77; -.
DR PRIDE; Q6PX77; -.
DR Ensembl; ENSBTAT00000064918; ENSBTAP00000056137; ENSBTAG00000045782.
DR GeneID; 353351; -.
DR KEGG; bta:353351; -.
DR CTD; 9210; -.
DR VEuPathDB; HostDB:ENSBTAG00000045782; -.
DR VGNC; VGNC:26516; BMP15.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000160940; -.
DR HOGENOM; CLU_055377_0_0_1; -.
DR InParanoid; Q6PX77; -.
DR OMA; VYRHQLH; -.
DR OrthoDB; 724783at2759; -.
DR TreeFam; TF316134; -.
DR Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000045782; Expressed in oocyte and 3 other tissues.
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: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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..269
FT /evidence="ECO:0000250"
FT /id="PRO_0000244399"
FT CHAIN 270..394
FT /note="Bone morphogenetic protein 15"
FT /id="PRO_0000244400"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 293..359
FT /evidence="ECO:0000250"
FT DISULFID 322..391
FT /evidence="ECO:0000250"
FT DISULFID 326..393
FT /evidence="ECO:0000250"
SQ SEQUENCE 394 AA; 45025 MW; 27B560E210ECF034 CRC64;
MVLLSILRIL LLWGLVLFME HRVQMTQVGQ PSIAHLPEAP TLPLIQELLE EAPGKQQRKP
RILGHPLRYM LELYQRSADA SGHPRENRTI GATMVRLVRP LASVARPLRG SWHIQTLDFP
LRPNRVAYQL VRATVVYRHQ LHLTHSHLSC HVEPWVQKSP TNHFPSSGRG SSKPSLLPKA
WTEMDIMEHV GQKLWNHKGR RVLRLRFVCQ QPRGSEVREF WWHGTSSLDT VFLLLYFNDT
QSVQKTKPLP KGLKEFTEKD PSLLLRRARQ AGSIASEVPG PSREHDGPES NLCSLHPFQV
SFQQLGWDHW IIAPHLYTPN YCKGVCPRVL HYGLNSPNHA IIQNLVNELV DQSVPQPSCV
PYKYVPISIL LIEANGSILY KEYEGMIAQS CTCR