ID   TWS1B_XENLA             Reviewed;         218 AA.
AC   Q9I8M9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Twisted gastrulation protein homolog 1-B;
DE   Flags: Precursor;
GN   Name=twsg1-b; Synonyms=tsg;
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, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, AND INTERACTION WITH CHRD AND BMP4.
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11420619; DOI=10.1007/s0033501-0005-x;
RA   Graf D., Timmons P.M., Hitchins M., Episkopou V., Moore G., Ito T.,
RA   Fujiyama A., Fisher A.G., Merkenschlager M.;
RT   "Evolutionary conservation, developmental expression, and genomic mapping
RT   of mammalian Twisted gastrulation.";
RL   Mamm. Genome 12:554-560(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   KNOCKDOWN, FUNCTION, AND INTERACTION WITH BMP7.
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: Involved in dorsal-ventral patterning, permitting peak BMP
CC       signaling by antagonizing the residual anti-BMP activity of the
CC       cleavage products of chrd. Functions to promote the formation of
CC       ventral mesoderm by increasing the activity of bmp7 and other BMPS.
CC       Seems to antagonize BMP signaling by forming ternary complexes with
CC       chrd and BMPs, thereby preventing BMPs from binding to their receptors.
CC       In addition to the anti-BMP function, also has pro-BMP activity, partly
CC       mediated by cleavage and degradation of chrd, which releases BMPs from
CC       ternary complexes. May be an important modulator of BMP-regulated
CC       cartilage development and chondrocyte differentiation.
CC       {ECO:0000269|PubMed:10866189, ECO:0000269|PubMed:15843411}.
CC   -!- SUBUNIT: Binds directly to bmp2, bmp4 and bmp7 and can form a ternary
CC       complex with bmps and chordin, thus preventing the binding of bmps to
CC       their cell surface receptors. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10866189}.
CC   -!- DEVELOPMENTAL STAGE: Maternal transcripts are distributed throughout
CC       animal half of the embryo during cleavage stages. At the late gastrula
CC       stage, maternal transcripts decrease and zygotic transcripts appear
CC       specifically in the ventral region of the embryo. After neurulation,
CC       expressed ventrally in the closed blastopore slit and the neural tube.
CC       At the tailbud stage, detected in the postanal region, heart and dorsal
CC       eye. {ECO:0000269|PubMed:10866189}.
CC   -!- DOMAIN: The N-terminal domain is sufficient to interact with bmp4.
CC   -!- MISCELLANEOUS: Knockdown of tsg and bmp7 results in the siren phenotype
CC       with loss of posteroventral cell fates associated with decreased BMP
CC       activity.
CC   -!- SIMILARITY: Belongs to the twisted gastrulation protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF245221; AAF77182.1; -; mRNA.
DR   EMBL; AJ297392; CAC05629.1; -; mRNA.
DR   EMBL; BC056070; AAH56070.1; -; mRNA.
DR   RefSeq; NP_001079870.1; NM_001086401.1.
DR   AlphaFoldDB; Q9I8M9; -.
DR   MaxQB; Q9I8M9; -.
DR   DNASU; 379560; -.
DR   GeneID; 379560; -.
DR   KEGG; xla:379560; -.
DR   CTD; 379560; -.
DR   Xenbase; XB-GENE-483449; twsg1.L.
DR   OMA; SCVDLCP; -.
DR   OrthoDB; 1254178at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 379560; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006761; Tsg.
DR   PANTHER; PTHR12312; PTHR12312; 1.
DR   Pfam; PF04668; Tsg; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..218
FT                   /note="Twisted gastrulation protein homolog 1-B"
FT                   /id="PRO_0000278814"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   218 AA;  24403 MW;  3EA2D1BC8D18BA4F CRC64;
     MKPSFLHIPA AALLLCSLWI LPIHCCNKAL CASDVSKCLI QELCQCRPTD GNCSCCKECM
     LCLGTLWDEC CDCVGMCNPR NYSDTPPTSK STVEELHEPI PSLFRALTEG DTQLNWNIVT
     FPVVEELSHH ENLVSFLETV NQPQQQNVSV QVSHSNEKEH MCTVVYFDDC MSIHQCKVSC
     ESMGASKYRW FHNACCECVG PECIDYGSKT VKCVNCMV