BMP2_DAMDA
ID BMP2_DAMDA Reviewed; 396 AA.
AC O19006;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Bone morphogenetic protein 2;
DE Short=BMP-2;
DE Flags: Precursor;
GN Name=BMP2;
OS Dama dama (Fallow deer) (Cervus dama).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Cervinae; Dama.
OX NCBI_TaxID=30532;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Antler;
RX PubMed=9003457; DOI=10.1016/s0167-4781(96)00178-9;
RA Feng J.Q., Chen D., Ghosh-Choudhury N., Esparza J., Mundy G.R.,
RA Harris S.E.;
RT "Bone morphogenetic protein 2 transcripts in rapidly developing deer antler
RT tissue contain an extended 5' non-coding region arising from a distal
RT promoter.";
RL Biochim. Biophys. Acta 1350:47-52(1997).
CC -!- FUNCTION: Growth factor of the TGF-beta superfamily that plays
CC essential roles in many developmental processes, including
CC cardiogenesis, neurogenesis, and osteogenesis. Induces cartilage and
CC bone formation. Initiates the canonical BMP signaling cascade by
CC associating with type I receptor BMPR1A and type II receptor BMPR2.
CC Once all three components are bound together in a complex at the cell
CC surface, BMPR2 phosphorylates and activates BMPR1A. 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 pathways such as ERK/MAP
CC kinase signaling cascade that regulates osteoblast differentiation.
CC Stimulates also the differentiation of myoblasts into osteoblasts via
CC the EIF2AK3-EIF2A-ATF4 pathway by stimulating EIF2A phosphorylation
CC which leads to increased expression of ATF4 which plays a central role
CC in osteoblast differentiation. {ECO:0000250|UniProtKB:P12643}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with SOSTDC1 (By
CC similarity). Interacts with GREM2, RGMA, RGMB and RGMC. Interacts with
CC ASPN (By similarity). Interacts with MAFP5 (By similarity). Interacts
CC with FBN1 (via N-terminal domain) and FBN2. Interacts with type I
CC receptor BMPR1A. Interacts with type II receptor BMPR2 (By similarity).
CC {ECO:0000250|UniProtKB:P12643, ECO:0000250|UniProtKB:P21274}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P12643}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; AJ001817; CAA05033.1; -; mRNA.
DR AlphaFoldDB; O19006; -.
DR SMR; O19006; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
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 Chondrogenesis; Cleavage on pair of basic residues; Cytokine;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Growth factor; Osteogenesis; Phosphoprotein; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..282
FT /note="Cleaved by PCSK5"
FT /evidence="ECO:0000250"
FT /id="PRO_0000033822"
FT CHAIN 283..396
FT /note="Bone morphogenetic protein 2"
FT /id="PRO_0000033823"
FT REGION 272..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..293
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12644"
FT CARBOHYD 135
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 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 296..361
FT /evidence="ECO:0000250"
FT DISULFID 325..393
FT /evidence="ECO:0000250"
FT DISULFID 329..395
FT /evidence="ECO:0000250"
FT DISULFID 360
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 44646 MW; 5FE23A0AC7F91572 CRC64;
MVAGTRCLLA LLLPQVLLGG AAGLIPELGR RKFAASWPGR SSSQPSDDVL SEFELRLLSM
FGLKQRPTPS RDPVVPPYML DLYRLHSGQP GAPAPGHRLE RAASLANTVR TFHHEESLEE
LPEMSGKTTR RFFFNLTSIP TEEFITSAEL QVFGKHMPEA LENNSSFHHR INIFEIIKPA
TANSKFPVTR LLDTRLVTQN ASRWESFDVT PAVMRWTAQG LTNHGFVVEV AHPEDSYGAS
KRHVRISRSL HQDEHSWSQI RPLLVTFGHD GKGHPLHRRE KRQAKHKQRK RLKSSCKRHP
LYVDFSDVGW NDWIVAPPGY HAFYCHGECP FPLADHLNST NHAIVQTLVN SVNSKIPKAC
CVPTELSAIS MLYLDENEKV VLKNYQDMVV EGCGCR
