BMP4_XENLA
ID BMP4_XENLA Reviewed; 401 AA.
AC P30885;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Bone morphogenetic protein 4;
DE Short=BMP-4;
DE Flags: Precursor;
GN Name=bmp4; Synonyms=dvr-4;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=1510675; DOI=10.1016/s0006-291x(05)81574-8;
RA Nishimatsu S., Suzuki A., Shoda A., Murakami K., Ueno N.;
RT "Genes for bone morphogenetic proteins are differentially transcribed in
RT early amphibian embryos.";
RL Biochem. Biophys. Res. Commun. 186:1487-1495(1992).
RN [2]
RP FUNCTION.
RX PubMed=1425343; DOI=10.1242/dev.115.2.639;
RA Jones C.M., Lyons K.M., Lapan P.M., Wright C.V., Hogan B.L.;
RT "DVR-4 (bone morphogenetic protein-4) as a posterior-ventralizing factor in
RT Xenopus mesoderm induction.";
RL Development 115:639-647(1992).
RN [3]
RP INTERACTION WITH TWSG1 AND CHRD.
RX PubMed=10866189; DOI=10.1038/35015500;
RA Oelgeschlager M., Larrain J., Geissert D., De Robertis E.M.;
RT "The evolutionarily conserved BMP-binding protein Twisted gastrulation
RT promotes BMP signalling.";
RL Nature 405:757-763(2000).
RN [4]
RP INTERACTION WITH DERRIERE.
RX PubMed=12070085; DOI=10.1242/dev.129.13.3089;
RA Eimon P.M., Harland R.M.;
RT "Effects of heterodimerization and proteolytic processing on Derriere and
RT Nodal activity: implications for mesoderm induction in Xenopus.";
RL Development 129:3089-3103(2002).
RN [5]
RP INTERACTION WITH TSKU.
RX PubMed=16319115; DOI=10.1242/dev.02178;
RA Kuriyama S., Lupo G., Ohta K., Ohnuma S., Harris W.A., Tanaka H.;
RT "Tsukushi controls ectodermal patterning and neural crest specification in
RT Xenopus by direct regulation of BMP4 and X-delta-1 activity.";
RL Development 133:75-88(2006).
CC -!- FUNCTION: Posterior-ventralizing factor in Xenopus mesoderm induction.
CC Induces posteroventral mesoderm and counteracts dorsalizing signals
CC such as activin. {ECO:0000269|PubMed:1425343,
CC ECO:0000269|PubMed:1510675}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms
CC heterodimers with the TGF-beta family member derriere. Part of a
CC complex consisting of twsg1 and chrd. Interacts with tsku
CC (PubMed:16319115). {ECO:0000250, ECO:0000269|PubMed:16319115}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed at a low level maternally with expression levels increasing
CC rapidly after stage 9. Expression is maintained throughout development
CC and in a range of adult tissues including the ovary and testis.
CC {ECO:0000269|PubMed:1510675}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; X63426; CAA45020.1; -; mRNA.
DR PIR; JH0689; JH0689.
DR RefSeq; NP_001095263.1; NM_001101793.1.
DR AlphaFoldDB; P30885; -.
DR SMR; P30885; -.
DR GeneID; 399322; -.
DR KEGG; xla:399322; -.
DR CTD; 399322; -.
DR Xenbase; XB-GENE-6254046; bmp4.S.
DR OMA; HEEHMEQ; -.
DR OrthoDB; 962484at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 399322; Expressed in gastrula and 19 other tissues.
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 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;
KW Extracellular matrix; Glycoprotein; Growth factor; Osteogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..287
FT /evidence="ECO:0000250"
FT /id="PRO_0000033864"
FT CHAIN 288..401
FT /note="Bone morphogenetic protein 4"
FT /id="PRO_0000033865"
FT REGION 279..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
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 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 301..366
FT /evidence="ECO:0000250"
FT DISULFID 330..398
FT /evidence="ECO:0000250"
FT DISULFID 334..400
FT /evidence="ECO:0000250"
FT DISULFID 365
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 401 AA; 45988 MW; 3580DEC4B9890047 CRC64;
MIPGNRMLMV ILLSQVLLGG TNYASLIPDT GKKKVAADIQ GGGRRSPQSN ELLRDFEVTL
LQMFGLRKRP QPSKDVVVPA YMRDLYRLQS AEEEDELHDI SMEYPETPTS RANTVRSFHH
EEHLENLPGT EENGNFRFVF NLSSIPENEV ISSAELRLYR EQIDHGPAWD EGFHRINIYE
VMKPITANGH MINRLLDTRV IHHNVTQWES FDVSPAIMRW TLDKQINHGL AIEVIHLNQT
KTYQGKHVRI SRSLLPQKDA DWSQMRPLLI TFSHDGRGHA LTRRSKRSPK QQRPRKKNKH
CRRHSLYVDF SDVGWNDWIV APPGYQAFYC HGDCPFPLAD HLNSTNHAIV QTLVNSVNSS
IPKACCVPTE LSAISMLYLD EYDKVVLKNY QEMVVEGCGC R
