ID   NODAL_XENTR             Reviewed;         403 AA.
AC   Q28GB8;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Nodal homolog;
DE   AltName: Full=Nodal-related protein 1;
DE   Flags: Precursor;
GN   Name=nodal {ECO:0000250|UniProtKB:P43021}; Synonyms=nr1;
GN   ORFNames=TGas124h10.1;
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:0000312|EMBL:CAJ82560.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula {ECO:0000312|EMBL:CAJ82560.1};
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cooperation and regulatory loops of multiple nodals are
CC       essential for mesendoderm patterning in early embryos. Essential for
CC       mesoderm formation and axial patterning during embryonic development.
CC       Activates the activin-like signaling pathway to induce dorsal and
CC       ventral mesoderm in animal cap ectoderm. In addition, also dorsalizes
CC       ventral marginal zone (VMZ) tissues during gastrulation. Acts in a
CC       downstream signaling cascade via cripto and cer1 to mediate
CC       cardiogenesis in embryonic mesoderm. Directs the orientation of the
CC       left-right axis by driving the left-specific gene cascade in the left
CC       lateral plate mesoderm (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with, and is inhibited
CC       by cer1 and gdf10/bmp3b. {ECO:0000250|UniProtKB:P43021,
CC       ECO:0000250|UniProtKB:Q91619}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000255}.
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DR   EMBL; CR761456; CAJ82560.1; -; mRNA.
DR   RefSeq; NP_001016321.1; NM_001016321.2.
DR   AlphaFoldDB; Q28GB8; -.
DR   SMR; Q28GB8; -.
DR   STRING; 8364.ENSXETP00000019726; -.
DR   PaxDb; Q28GB8; -.
DR   GeneID; 549075; -.
DR   KEGG; xtr:549075; -.
DR   CTD; 549075; -.
DR   Xenbase; XB-GENE-487169; nodal1.
DR   eggNOG; KOG3900; Eukaryota.
DR   InParanoid; Q28GB8; -.
DR   OrthoDB; 1518399at2759; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
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:0070698; F:type I activin receptor binding; IBA:GO_Central.
DR   GO; GO:0048320; P:axial mesoderm formation; 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:0007507; P:heart development; 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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..278
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000273276"
FT   CHAIN           279..403
FT                   /note="Nodal homolog"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000273277"
FT   REGION          195..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        303..369
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   DISULFID        332..400
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   DISULFID        336..402
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   DISULFID        366
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
SQ   SEQUENCE   403 AA;  46169 MW;  178AB3D34878C8FD CRC64;
     MAFLTAVLCF GFACMVQGVP SWLESRIPLL GSSVASKHPS LLDGNRHHRD MKYPFYMMQL
     YQNLVMANDT GLARGHNTAT KEYDTVLSLF AKRCMESEKR WTLSFDMSAV SKSSELKLAE
     LRIQLPHIEM SHNVTVDVYH TRDGEENLYL GSFEANPFST KGSPWKVFNV TRILQHYFKE
     GQDIKSEYLR TKDRAERGSG MSSAEFLDSP GDSPQYNPHH TPLRRYLSTE GVMLVLFTKV
     KPSVNHIGFP SLIKTAESSK YVDMEKASRM PGIRRHRRNK NEKHHLSMGS IPSRHVDNGK
     PLCRRVDMIV NFEDIGWGNW IVYPKKYNAY RCEGACPIPL NETFKPTNHA YMKSVVKLYQ
     PEKVECPLCV PIKMSPLSML YYEGDEVVLR HHQEMIVEEC GCS