BMP2_CHICK
ID BMP2_CHICK Reviewed; 353 AA.
AC Q90751;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Bone morphogenetic protein 2;
DE Short=BMP-2;
DE Flags: Precursor; Fragment;
GN Name=BMP2; Synonyms=BMP-2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn;
RX PubMed=8119128; DOI=10.1242/dev.120.1.209;
RA Francis P.H., Richardson M.K., Brickell P.M., Tickle C.;
RT "Bone morphogenetic proteins and a signalling pathway that controls
RT patterning in the developing chick limb.";
RL Development 120:209-218(1994).
RN [2]
RP FUNCTION.
RX PubMed=9927590; DOI=10.1242/dev.126.5.883;
RA Pizette S., Niswander L.;
RT "BMPs negatively regulate structure and function of the limb apical
RT ectodermal ridge.";
RL Development 126:883-894(1999).
CC -!- FUNCTION: Negatively regulates the structure and function of the limb
CC apical ectodermal ridge. {ECO:0000269|PubMed:9927590}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P12643}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; X75914; CAA53513.1; -; mRNA.
DR PIR; I50607; I50607.
DR AlphaFoldDB; Q90751; -.
DR SMR; Q90751; -.
DR STRING; 9031.ENSGALP00000014334; -.
DR PaxDb; Q90751; -.
DR VEuPathDB; HostDB:geneid_378779; -.
DR eggNOG; KOG3900; Eukaryota.
DR InParanoid; Q90751; -.
DR PhylomeDB; Q90751; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0070700; F:BMP receptor binding; 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:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:DFLAT.
DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:DFLAT.
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; 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; Reference proteome; Secreted.
FT PROPEP <1..239
FT /evidence="ECO:0000250"
FT /id="PRO_0000033820"
FT CHAIN 240..353
FT /note="Bone morphogenetic protein 2"
FT /id="PRO_0000033821"
FT REGION 228..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..248
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 253..318
FT /evidence="ECO:0000250"
FT DISULFID 282..350
FT /evidence="ECO:0000250"
FT DISULFID 286..352
FT /evidence="ECO:0000250"
FT DISULFID 317
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 353 AA; 40347 MW; 8DBB46CD0EBD769B CRC64;
GSLKRPEDLL GEFELRLLHM FGLKRRPSPG KDVVIPPYML DLYRLHAGQQ LGYPLERAAC
RANTVCSFHH EEVLEELPET SGKTARRFFF NLTSIPNEES VTSAELQIFP GEQVHEAFES
NSSYHHRINI YEIMKPATAT SKDPVTRLLD TRLVHHNASK WESSDVTPAV LRWIAHGQPN
HGFVVEVVHL DKENSASKRH VRISRSLHQD EDSWSQLRPL LVTFGHDGKG HPLHKREKRQ
AKHKQRKRHK YSCKRHPLYV DFNDVGWNDW IVAPPGYSAF YCHGECPFPL ADHLNSTNHA
IVQTLVNSVN SKIPKACCVP TELSAISMLY LDENEKVVLK NYQDMVVEGC GCR
