TWS1B_DANRE
ID TWS1B_DANRE Reviewed; 222 AA.
AC Q98SR9; Q3SYN9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Twisted gastrulation protein homolog 1-B;
DE Flags: Precursor;
GN Name=twsg1b {ECO:0000312|ZFIN:ZDB-GENE-020812-3};
GN Synonyms=tsg1 {ECO:0000312|EMBL:AAK19520.1},
GN tsgb {ECO:0000312|ZFIN:ZDB-GENE-020812-3};
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] {ECO:0000305, ECO:0000312|EMBL:AAK19520.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC TISSUE=Embryo {ECO:0000269|PubMed:11260716};
RX PubMed=11260716; DOI=10.1038/35068578;
RA Ross J.J., Shimmi O., Vilmos P., Petryk A., Kim H., Gaudenz K.,
RA Hermanson S., Ekker S.C., O'Connor M.B., Marsh J.L.;
RT "Twisted gastrulation is a conserved extracellular BMP antagonist.";
RL Nature 410:479-483(2001).
RN [2] {ECO:0000312|EMBL:AAI18681.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Embryo {ECO:0000312|EMBL:AAI18681.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15525664; DOI=10.1242/dev.01464;
RA Little S.C., Mullins M.C.;
RT "Twisted gastrulation promotes BMP signaling in zebrafish dorsal-ventral
RT axial patterning.";
RL Development 131:5825-5835(2004).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15604098; DOI=10.1242/dev.01577;
RA Xie J., Fisher S.;
RT "Twisted gastrulation enhances BMP signaling through chordin dependent and
RT independent mechanisms.";
RL Development 132:383-391(2005).
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. {ECO:0000269|PubMed:11260716,
CC ECO:0000269|PubMed:15525664, ECO:0000269|PubMed:15604098}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed uniformly in early embryos.
CC {ECO:0000269|PubMed:11260716}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown in embryos exhibits variable
CC outcome. It may result in a weak ventralized phenotype
CC (PubMed:11260716) or in dorsalization (PubMed:15525664 and
CC PubMed:15604098). {ECO:0000269|PubMed:11260716,
CC ECO:0000269|PubMed:15525664, ECO:0000269|PubMed:15604098}.
CC -!- SIMILARITY: Belongs to the twisted gastrulation protein family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI03720.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF332096; AAK19520.1; -; mRNA.
DR EMBL; BC103719; AAI03720.1; ALT_INIT; mRNA.
DR EMBL; BC118680; AAI18681.1; -; mRNA.
DR RefSeq; NP_705958.1; NM_153672.2.
DR AlphaFoldDB; Q98SR9; -.
DR STRING; 7955.ENSDARP00000059298; -.
DR PaxDb; Q98SR9; -.
DR GeneID; 259304; -.
DR KEGG; dre:259304; -.
DR CTD; 259304; -.
DR ZFIN; ZDB-GENE-020812-3; twsg1b.
DR eggNOG; ENOG502QRE9; Eukaryota.
DR InParanoid; Q98SR9; -.
DR OrthoDB; 1254178at2759; -.
DR PhylomeDB; Q98SR9; -.
DR PRO; PR:Q98SR9; -.
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; IMP:ZFIN.
DR GO; GO:0048264; P:determination of ventral identity; IMP:ZFIN.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:ZFIN.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IGI:ZFIN.
DR GO; GO:0045765; P:regulation of angiogenesis; IMP:ZFIN.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IMP:ZFIN.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..222
FT /note="Twisted gastrulation protein homolog 1-B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000284725"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 8
FT /note="S -> SS (in Ref. 2; AAI03720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 24540 MW; B853F4E39EB9B0ED CRC64;
MGSSSSSSVV LLLLLLSSLS IALACNKALC ASDVSKCLIQ ELCQCRPADG NCSCCKECML
CLGSLWEECC DCVGMCNPRS MSESPATGRS TVEDLFQPIP SLFRALTEGD APTHTLVLTL
PLAEELQYQH NLHNYLETLH NTQHNNTTSV PENSIHSSYH TQDKQCTVVY FDECVSIRQC
KQYCESMGGS KYRWFHNACC QCIGPECVDY GSKSVRCLNC LY
