ID   TWS1A_XENLA             Reviewed;         216 AA.
AC   Q98T88;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Twisted gastrulation protein homolog 1-A;
DE   Flags: Precursor;
GN   Name=twsg1-a; 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, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=11260715; DOI=10.1038/35068572;
RA   Scott I.C., Blitz I.L., Pappano W.N., Maas S.A., Cho K.W.Y.,
RA   Greenspan D.S.;
RT   "Homologues of Twisted gastrulation are extracellular cofactors in
RT   antagonism of BMP signalling.";
RL   Nature 410:475-478(2001).
RN   [2]
RP   ERRATUM OF PUBMED:11260715.
RA   Scott I.C., Blitz I.L., Pappano W.N., Maas S.A., Cho K.W.Y.,
RA   Greenspan D.S.;
RL   Nature 411:720-720(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:11260715,
CC       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:0000250}.
CC   -!- TISSUE SPECIFICITY: Posterior defects are induced by overexpression.
CC       This may arise through alteration of bmp4 or chrd function in the
CC       developing tailbud region. {ECO:0000269|PubMed:11260715}.
CC   -!- DEVELOPMENTAL STAGE: Maternal transcripts detected in eggs. Uniform
CC       expression across the entire animal hemisphere and marginal zone of the
CC       early gastrula. At tailbud stage, expressed in the developing tail,
CC       anterior brain, eye and heart. {ECO:0000269|PubMed:11260715}.
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}.
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; AF279246; AAK27327.1; -; mRNA.
DR   EMBL; BC068634; AAH68634.1; -; mRNA.
DR   RefSeq; NP_001084240.1; NM_001090771.1.
DR   RefSeq; XP_018124139.1; XM_018268650.1.
DR   RefSeq; XP_018124140.1; XM_018268651.1.
DR   AlphaFoldDB; Q98T88; -.
DR   DNASU; 399387; -.
DR   GeneID; 399387; -.
DR   KEGG; xla:399387; -.
DR   CTD; 399387; -.
DR   Xenbase; XB-GENE-6254023; twsg1.S.
DR   OMA; EKMCTVV; -.
DR   OrthoDB; 1254178at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 399387; Expressed in brain 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..216
FT                   /note="Twisted gastrulation protein homolog 1-A"
FT                   /id="PRO_0000278813"
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        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   216 AA;  24200 MW;  88F0C6592362702E CRC64;
     MKPSFLHIPA AALLLCSLWI LPIYCCNKAL CASDVSKCLI QELCQCRPTD GNCSCCKECM
     LCLGTLWDEC CDCVGMCKPR NYSDTPPTSK STVEELHEPI PSLFRALTEG DTQLNWNIVT
     FPVVEELSHH ENLVSFLENV NQPQNVSVQV SHSNEKEHMC TVVYFDDCMS IHQCKVSCES
     MGASKYRWFH NACCECVGPE CIDYGSKTVK CVNCMV