ID   DERR_XENTR              Reviewed;         350 AA.
AC   Q66KL4; Q28D13;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Derriere protein;
DE   AltName: Full=Growth/differentiation factor 3;
DE            Short=Gdf-3;
DE   Flags: Precursor;
GN   Name=derriere {ECO:0000250|UniProtKB:Q9YGV1};
GN   Synonyms=gdf3 {ECO:0000312|EMBL:AAH80341.1}; ORFNames=TGas141f11.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAH80341.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tail bud {ECO:0000312|EMBL:AAH80341.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAH80341.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-350.
RC   TISSUE=Gastrula {ECO:0000312|EMBL:CAJ81634.1};
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for posterior mesoderm formation during
CC       embryogenesis. Acts indirectly to suppress head formation by altering
CC       mesodermal patterning. Also involved in the establishment of left-right
CC       axis asymmetry, acting upstream of nodal/nr-1. Can exert long-range
CC       effects in the embryo (By similarity). {ECO:0000250|UniProtKB:Q9YGV1}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Also forms heterodimers with
CC       other TGF-beta family members including nodal2/nr-2 and bmp4 (By
CC       similarity). {ECO:0000250|UniProtKB:Q9YGV1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000255}.
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DR   EMBL; BC080341; AAH80341.1; -; mRNA.
DR   EMBL; CR855767; CAJ81634.1; -; mRNA.
DR   RefSeq; NP_001007905.1; NM_001007904.1.
DR   AlphaFoldDB; Q66KL4; -.
DR   SMR; Q66KL4; -.
DR   STRING; 8364.ENSXETP00000004454; -.
DR   PaxDb; Q66KL4; -.
DR   DNASU; 493288; -.
DR   GeneID; 493288; -.
DR   KEGG; xtr:493288; -.
DR   CTD; 9573; -.
DR   Xenbase; XB-GENE-487309; gdf3.
DR   eggNOG; KOG3900; Eukaryota.
DR   HOGENOM; CLU_020515_4_0_1; -.
DR   InParanoid; Q66KL4; -.
DR   OrthoDB; 919690at2759; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016015; F:morphogen activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; ISS:UniProtKB.
DR   GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0007368; P:determination of left/right symmetry; ISS:UniProtKB.
DR   GO; GO:0001707; P:mesoderm formation; ISS:UniProtKB.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Cytokine; Developmental protein;
KW   Disulfide bond; Glycoprotein; Growth factor; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..236
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000274251"
FT   CHAIN           237..350
FT                   /note="Derriere protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000274252"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        249..315
FT                   /evidence="ECO:0000250|UniProtKB:P09534"
FT   DISULFID        278..347
FT                   /evidence="ECO:0000250|UniProtKB:P09534"
FT   DISULFID        282..349
FT                   /evidence="ECO:0000250|UniProtKB:P09534"
FT   DISULFID        314
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P09534"
FT   CONFLICT        108..109
FT                   /note="NK -> RG (in Ref. 2; CAJ81634)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   350 AA;  39881 MW;  B042A540179C1ABF CRC64;
     MLSLACFFSF LLMVKSSPLT FQERMLLKAL GLNTRPNPIA PGPVPKSLRD IFEKGINKDN
     PCMMEGFGVP GNIVRSYRDQ GPVAAMEEPQ ESLCLKKFLF FDLSAVENKE QLTLGQLEIK
     FKHNSYYGQQ FHLRLYRTLQ LSLKGMRESK MNRKLLVSQS FRLLHKSLYF NLTKVAKDWK
     TPEKNMGLLL EIYASSKLAG DNRSFAVCEP IQSFIYTSLL TVSLDPSSCK TPRAKRSTHS
     SPPTPSNICK KRRLYIDFKD VGWQNWVIAP RGYMANYCYG ECPYPLTEML RGTNHAVLQT
     LVHSVEPEST PLPCCAPTKL SPISMLYYDN NDNVVLRHYE DMVVDECGCK