BMP7_XENLA
ID BMP7_XENLA Reviewed; 426 AA.
AC P30886; Q91645;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Bone morphogenetic protein 7;
DE Short=BMP-7;
DE Short=xBMP7;
DE AltName: Full=Osteogenic protein 1;
DE Short=OP-1;
DE Flags: Precursor;
GN Name=bmp7;
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].
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 NUCLEOTIDE SEQUENCE [MRNA].
RA Hawley S.H.B., Wunnenberg-Stapleton K., Hashimoto C., Laurent M.N.,
RA Watabe T., Blumberg B.W., Cho K.W.Y.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH TWSG1.
RX PubMed=15843411; DOI=10.1242/dev.01822;
RA Zakin L., Reversade B., Kuroda H., Lyons K.M., De Robertis E.M.;
RT "Sirenomelia in Bmp7 and Tsg compound mutant mice: requirement for Bmp
RT signaling in the development of ventral posterior mesoderm.";
RL Development 132:2489-2499(2005).
CC -!- FUNCTION: Growth factor of the TGF-beta superfamily that plays
CC important role in various biological processes, including
CC embryogenesis, hematopoiesis, neurogenesis and skeletal morphogenesis.
CC Initiates the canonical BMP signaling cascade by associating with type
CC I receptor ACVR1 and type II receptor ACVR2A. Once all three components
CC are bound together in a complex at the cell surface, ACVR2A
CC phosphorylates and activates ACVR1. In turn, ACVR1 propagates signal by
CC phosphorylating SMAD1/5/8 that travel to the nucleus and act as
CC activators and repressors of transcription of target genes.
CC {ECO:0000250|UniProtKB:P18075}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with twsg1.
CC {ECO:0000269|PubMed:15843411}.
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; X63427; CAA45021.1; -; mRNA.
DR EMBL; U38559; AAA82616.1; -; mRNA.
DR PIR; JH0690; JH0690.
DR RefSeq; NP_001079934.1; NM_001086465.1.
DR RefSeq; XP_018106162.1; XM_018250673.1.
DR AlphaFoldDB; P30886; -.
DR SMR; P30886; -.
DR DNASU; 379625; -.
DR GeneID; 379625; -.
DR KEGG; xla:379625; -.
DR CTD; 379625; -.
DR Xenbase; XB-GENE-856288; bmp7.2.L.
DR OMA; IGEHYEN; -.
DR OrthoDB; 1063560at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 379625; Expressed in gastrula and 6 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; Cytokine; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Growth factor; Osteogenesis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..282
FT /evidence="ECO:0000250"
FT /id="PRO_0000033880"
FT CHAIN 283..426
FT /note="Bone morphogenetic protein 7"
FT /id="PRO_0000033881"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 325..391
FT /evidence="ECO:0000250"
FT DISULFID 354..423
FT /evidence="ECO:0000250"
FT DISULFID 358..425
FT /evidence="ECO:0000250"
FT DISULFID 390
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 317..319
FT /note="KRR -> NVV (in Ref. 2; AAA82616)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="D -> E (in Ref. 2; AAA82616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 48965 MW; 6401D5151AC97117 CRC64;
MNALTVKRRL PVLLFLFHIS LSSISSNTIL ENDFHSSFVQ RRLKGHERRE IQKEILTILG
LQHRPRPYLP EKKKSAPLFM MDLYNAVNIE EMHAEDVSYS NKPISLNEAF SLATDQENGF
LAHADTVMSF ANLVDNDNEL HKNSYRQKFK FDLTDIPLGD ELTAAEFRIY KDYVQNNETY
QVTIYQVLKK QADKDPYLFQ VDSRTIWGTE KGWLTFDITA TGNHWVMNPH YNLGLQLSVE
SMDMQNVNPR LVGLVGKNGP QDKQPFMVAF FKTSDIHLRS VRSTSNKHWN QERAKTYKEQ
DNLPPANITD GIMPPGKRRF LKQACKKHEL FVSFRDLGWQ DWIIAPEGYA AYYCDGECAF
PLNSFMNATN HAIVQTLVHF INPETVPKPC CAPTQLNGIS VLYFDDSANV ILKKYKNMVV
QACGCH
