BMP5_MOUSE
ID BMP5_MOUSE Reviewed; 452 AA.
AC P49003; Q8CCE0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Bone morphogenetic protein 5;
DE Short=BMP-5;
DE Flags: Precursor;
GN Name=Bmp5; Synonyms=Bmp-5;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=C3H/KW;
RX PubMed=7958439; DOI=10.1006/dbio.1994.1300;
RA King J.A., Marker P.C., Seung K.J., Kingsley D.M.;
RT "BMP5 and the molecular, skeletal, and soft-tissue alterations in short ear
RT mice.";
RL Dev. Biol. 166:112-122(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29321139; DOI=10.1523/jneurosci.1540-17.2018;
RA Jovanovic V.M., Salti A., Tilleman H., Zega K., Jukic M.M., Zou H.,
RA Friedel R.H., Prakash N., Blaess S., Edenhofer F., Brodski C.;
RT "BMP/SMAD Pathway Promotes Neurogenesis of Midbrain Dopaminergic Neurons In
RT Vivo and in Human Induced Pluripotent and Neural Stem Cells.";
RL J. Neurosci. 38:1662-1676(2018).
CC -!- FUNCTION: Growth factor of the TGF-beta superfamily that plays
CC essential roles in many developmental processes, including cartilage
CC and bone formation or neurogenesis (PubMed:7958439, PubMed:29321139).
CC Initiates the canonical BMP signaling cascade by associating with type
CC I receptor BMPR1A and type II receptor BMPR2. In turn, BMPR1A
CC propagates signal by phosphorylating SMAD1/5/8 that travel to the
CC nucleus and act as activators and repressors of transcription of target
CC genes. Can also signal through non-canonical pathway such as MAPK p38
CC signaling cascade to promote chondrogenic differentiation (By
CC similarity). {ECO:0000250|UniProtKB:P22003,
CC ECO:0000269|PubMed:29321139, ECO:0000269|PubMed:7958439}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49003-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49003-2; Sequence=VSP_044321;
CC -!- DISRUPTION PHENOTYPE: Deletion mutant mice show a number of skeletal
CC defects, including small ears, several reduced vertebral processes, and
CC a reduced number of ribs and sesamoid bones (PubMed:7958439). BMP5/7-
CC deficient mice lack midbrain dopaminergic neurons due to reduced
CC neurogenesis in the midbrain dopaminergic progenitor domain
CC (PubMed:29321139). {ECO:0000269|PubMed:29321139,
CC ECO:0000269|PubMed:7958439}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; L41145; AAA64612.1; -; mRNA.
DR EMBL; AK033362; BAC28247.1; -; mRNA.
DR EMBL; AC079245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23348.1; -. [P49003-2]
DR PIR; I49542; I49542.
DR RefSeq; NP_031581.2; NM_007555.4. [P49003-2]
DR AlphaFoldDB; P49003; -.
DR SMR; P49003; -.
DR BioGRID; 198365; 1.
DR STRING; 10090.ENSMUSP00000012281; -.
DR GlyGen; P49003; 4 sites.
DR PhosphoSitePlus; P49003; -.
DR MaxQB; P49003; -.
DR PaxDb; P49003; -.
DR PRIDE; P49003; -.
DR ProteomicsDB; 281696; -. [P49003-1]
DR ProteomicsDB; 281697; -. [P49003-2]
DR Antibodypedia; 17340; 469 antibodies from 35 providers.
DR DNASU; 12160; -.
DR Ensembl; ENSMUST00000012281; ENSMUSP00000012281; ENSMUSG00000032179. [P49003-2]
DR GeneID; 12160; -.
DR KEGG; mmu:12160; -.
DR UCSC; uc009qsu.1; mouse. [P49003-2]
DR CTD; 653; -.
DR MGI; MGI:88181; Bmp5.
DR VEuPathDB; HostDB:ENSMUSG00000032179; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000158644; -.
DR HOGENOM; CLU_020515_4_1_1; -.
DR InParanoid; P49003; -.
DR OMA; HQESSRM; -.
DR TreeFam; TF316134; -.
DR BioGRID-ORCS; 12160; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Bmp5; mouse.
DR PRO; PR:P49003; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P49003; protein.
DR Bgee; ENSMUSG00000032179; Expressed in ureter smooth muscle and 232 other tissues.
DR Genevisible; P49003; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0070700; F:BMP receptor binding; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:1905069; P:allantois development; IGI:BHF-UCL.
DR GO; GO:0097065; P:anterior head development; IMP:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0048738; P:cardiac muscle tissue development; IGI:BHF-UCL.
DR GO; GO:0060411; P:cardiac septum morphogenesis; IGI:BHF-UCL.
DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR GO; GO:0060710; P:chorio-allantoic fusion; IGI:BHF-UCL.
DR GO; GO:0043583; P:ear development; IMP:MGI.
DR GO; GO:0003272; P:endocardial cushion formation; IGI:BHF-UCL.
DR GO; GO:0061384; P:heart trabecula morphogenesis; IGI:BHF-UCL.
DR GO; GO:0030902; P:hindbrain development; IGI:BHF-UCL.
DR GO; GO:0030539; P:male genitalia development; IGI:MGI.
DR GO; GO:0032348; P:negative regulation of aldosterone biosynthetic process; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000065; P:negative regulation of cortisol biosynthetic process; ISO:MGI.
DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0010894; P:negative regulation of steroid biosynthetic process; ISO:MGI.
DR GO; GO:0021502; P:neural fold elevation formation; IGI:BHF-UCL.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0003344; P:pericardium morphogenesis; IGI:BHF-UCL.
DR GO; GO:0060037; P:pharyngeal system development; IGI:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR GO; GO:0003323; P:type B pancreatic cell development; ISO:MGI.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 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 Alternative splicing; Chondrogenesis; Cleavage on pair of basic residues;
KW Cytokine; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Growth factor; Osteogenesis; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..314
FT /evidence="ECO:0000255"
FT /id="PRO_0000033868"
FT CHAIN 315..452
FT /note="Bone morphogenetic protein 5"
FT /id="PRO_0000033869"
FT REGION 316..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 351..417
FT /evidence="ECO:0000250"
FT DISULFID 380..449
FT /evidence="ECO:0000250"
FT DISULFID 384..451
FT /evidence="ECO:0000250"
FT DISULFID 416
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 95
FT /note="E -> EES (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_044321"
SQ SEQUENCE 452 AA; 51512 MW; AAD9521EC94A78D5 CRC64;
MHWTVFLLRG IVGFLWSGWV QVGYAKGGLG DNHVHSSFIY RRLRNHERRE IQREILSILG
LPHRPRPFSP GKQASSAPLF MLDLYNAMAS EDNPEEYLVR VSLAGEAKET RKGYPASPNG
YAHRLHLPPR TPLTTQSPPL ASLHDTNFLN DADMVMSFVN LVERDKDFSH QRRHYKEFRF
DLTQIPHGEA VTAAEFRIYK DKGNHRFENE TIKISIYQII KEYTNRDADL FLLDTRKTQA
LDVGWLVFDI TVTSNHWVIN PQNNLGLQLC AETGDGRSIN VKSAGLVGRH GPQSKQPFMV
AFFKASEVLL RSVRAASKRK NQNRNKSNSH QDPSRMPSAG DYNTSEQKQA CKKHELYVSF
RDLGWQDWII APEGYAAFYC DGECSFPLNA HMNATNHAIV QTLVHLMFPD HVPKPCCAPT
KLNAISVLYF DDSSNVILKK YRNMVVRSCG CH
