ID   BMP4_CHICK              Reviewed;         405 AA.
AC   Q90752;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Bone morphogenetic protein 4;
DE            Short=BMP-4;
DE   Flags: Precursor;
GN   Name=BMP4; Synonyms=BMP-4;
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).
RN   [3]
RP   IDENTIFICATION IN A COMPLEX WITH CHRD AND TSKU.
RX   PubMed=15363410; DOI=10.1016/j.devcel.2004.08.014;
RA   Ohta K., Lupo G., Kuriyama S., Keynes R., Holt C.E., Harris W.A.,
RA   Tanaka H., Ohnuma S.;
RT   "Tsukushi functions as an organizer inducer by inhibition of BMP activity
RT   in cooperation with chordin.";
RL   Dev. Cell 7:347-358(2004).
RN   [4]
RP   INTERACTION WITH TSKU.
RX   PubMed=16943268; DOI=10.1242/dev.02579;
RA   Ohta K., Kuriyama S., Okafuji T., Gejima R., Ohnuma S., Tanaka H.;
RT   "Tsukushi cooperates with VG1 to induce primitive streak and Hensen's node
RT   formation in the chick embryo.";
RL   Development 133:3777-3786(2006).
CC   -!- FUNCTION: Negatively regulates the structure and function of the limb
CC       apical ectodermal ridge. {ECO:0000269|PubMed:9927590}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Part of a complex consisting of
CC       TWSG1 and CHRD (By similarity). Forms a ternary complex with
CC       chordin/CHRD and TSKU (PubMed:15363410, PubMed:16943268).
CC       {ECO:0000250|UniProtKB:P12644, ECO:0000269|PubMed:15363410,
CC       ECO:0000269|PubMed:16943268}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X75915; CAA53514.1; -; mRNA.
DR   PIR; I50608; I50608.
DR   AlphaFoldDB; Q90752; -.
DR   SMR; Q90752; -.
DR   STRING; 9031.ENSGALP00000020289; -.
DR   PaxDb; Q90752; -.
DR   PRIDE; Q90752; -.
DR   VEuPathDB; HostDB:geneid_396165; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   InParanoid; Q90752; -.
DR   PhylomeDB; Q90752; -.
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:0071730; P:beak formation; IMP:AgBase.
DR   GO; GO:0071729; P:beak morphogenesis; IMP:AgBase.
DR   GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR   GO; GO:0060197; P:cloacal septation; IEP:UniProtKB.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:AgBase.
DR   GO; GO:0048392; P:intermediate mesodermal cell differentiation; NAS:AgBase.
DR   GO; GO:0072198; P:mesenchymal cell proliferation involved in ureter development; IEP:UniProtKB.
DR   GO; GO:0072138; P:mesenchymal cell proliferation involved in ureteric bud development; IEP:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:AgBase.
DR   GO; GO:0072179; P:nephric duct formation; IMP:AgBase.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0009951; P:polarity specification of dorsal/ventral axis; NAS:AgBase.
DR   GO; GO:0045606; P:positive regulation of epidermal cell differentiation; ISS:CAFA.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR   GO; GO:2000872; P:positive regulation of progesterone secretion; TAS:AgBase.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:AgBase.
DR   GO; GO:0010453; P:regulation of cell fate commitment; ISS:CAFA.
DR   GO; GO:2000290; P:regulation of myotome development; NAS:AgBase.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR   GO; GO:0060675; P:ureteric bud morphogenesis; IEP: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   1: Evidence at protein level;
KW   Chondrogenesis; Cleavage on pair of basic residues; Cytokine;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Growth factor; Osteogenesis; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..291
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000033852"
FT   CHAIN           292..405
FT                   /note="Bone morphogenetic protein 4"
FT                   /id="PRO_0000033853"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        305..370
FT                   /evidence="ECO:0000250"
FT   DISULFID        334..402
FT                   /evidence="ECO:0000250"
FT   DISULFID        338..404
FT                   /evidence="ECO:0000250"
FT   DISULFID        369
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  46057 MW;  544302DBA0A40F81 CRC64;
     MIPGNRMLMV ILLCQVLLGG TNHASLIPET GRKKVAELQG QAGSGRRSAQ SHELLRGFET
     TLLQMFGLRR RPQPSKSAVI PSYMLDLYRL QSGEEEERSL QEISLQYPER SASRANTVRS
     FHHEEHLESV PGPSEAPRIR FVFNLSSVPD NEVISSEELR LYREQVEEPS AAWERGFHRI
     NIYEVMKPLS ERSQAITRLL DTRLVHHNVT RWETFDVSPA VIRWTKDKQP NHGLVIEVTH
     LHQAQTHQGK HVRISRSLPQ GHGGDWAQLR PLLVTFGHDG RGHALTRRAR RSPKHHGSRK
     NKKNCRRHAL YVDFSDVGWN DWIVAPPGYQ AFYCHGDCPF PLADHLNSTN HAIVQTLVNS
     VNSSIPKACC VPTELSAISM LYLDEYDKVV LKNYQEMVVE GCGCR