ID   TWS1A_DANRE             Reviewed;         217 AA.
AC   Q9DGH0;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Twisted gastrulation protein homolog 1-A;
DE   Flags: Precursor;
GN   Name=twsg1a; Synonyms=tsg, twsg1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in dorsal-ventral patterning. Appears to function
CC       predominantly as a ventralizing factor, through its actions as a BMP
CC       signaling agonist, acting through both chd-dependent and chd-
CC       independent mechanisms. May also antagonize BMP signaling, probably via
CC       formation of ternary complexes with chd and BMPs, resulting in
CC       dorsalization (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the twisted gastrulation protein family.
CC       {ECO:0000305}.
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DR   EMBL; AJ297393; CAC05526.1; -; mRNA.
DR   EMBL; AF261692; AAK13255.1; -; mRNA.
DR   EMBL; BC051451; AAH51451.1; -; mRNA.
DR   AlphaFoldDB; Q9DGH0; -.
DR   STRING; 7955.ENSDARP00000049962; -.
DR   PaxDb; Q9DGH0; -.
DR   ZFIN; ZDB-GENE-010509-2; twsg1a.
DR   eggNOG; ENOG502QRE9; Eukaryota.
DR   InParanoid; Q9DGH0; -.
DR   PhylomeDB; Q9DGH0; -.
DR   PRO; PR:Q9DGH0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0001568; P:blood vessel development; IGI:ZFIN.
DR   GO; GO:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central.
DR   InterPro; IPR006761; Tsg.
DR   PANTHER; PTHR12312; PTHR12312; 1.
DR   Pfam; PF04668; Tsg; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..217
FT                   /note="Twisted gastrulation protein homolog 1-A"
FT                   /id="PRO_0000278812"
FT   CARBOHYD        53
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   217 AA;  23925 MW;  94C351F2CD829EDE CRC64;
     MRPALFLCPV LISVLFLLSS LSLISGCNKA LCASDVSKCL LQGLCQCRPQ EGNCSCCKEC
     MLCLSSLWEE CCDCVGMCNP RSYNDSPATS KSTVEELYRP IPSLFRALTE GDAPINMMVV
     SFPVAEELSH HENLVSFLET LDSQSQNISL PTSSAQDDAL CTVVYFDDCV SIRQCKQYCE
     SMGGSKYRWF HNACCECIGP ECLDYGSKTV KCMNCLI