ID   NOD3B_XENLA             Reviewed;         401 AA.
AC   Q91621;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Nodal homolog 3-B;
DE   AltName: Full=Fugacin;
DE   AltName: Full=Nodal-related protein 3-B;
DE   AltName: Full=Xnr3-B;
DE   Flags: Precursor;
GN   Name=nodal3-b; Synonyms=fug {ECO:0000312|EMBL:AAC59735.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAC59735.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Blastopore lip {ECO:0000269|PubMed:8612984}, and
RC   Gastrula {ECO:0000312|EMBL:AAC59735.1};
RX   PubMed=8612984; DOI=10.1006/dbio.1995.8052;
RA   Ecochard V., Cayrol C., Foulquier F., Zaraisky A., Duprat A.-M.;
RT   "A novel TGF-beta-like gene, fugacin, specifically expressed in the Spemann
RT   organizer of Xenopus.";
RL   Dev. Biol. 172:699-703(1995).
CC   -!- FUNCTION: Exhibits mesoderm-dorsalizing activity and neural-inducing
CC       activity, but lacks mesoderm-inducing activity. Regulates the
CC       expression of specific mesodermal and neural genes. Induces convergent
CC       extension movements at the embryonic midline by activating the fgf
CC       signaling pathway to induce t/bra expression in the organizer region.
CC       Acts with wnt11 to induce Spemann organizer cells and induce axis
CC       formation. The unprocessed protein antagonizes bmp-signaling (By
CC       similarity). {ECO:0000250|UniProtKB:Q800C0,
CC       ECO:0000250|UniProtKB:Q91609}.
CC   -!- SUBUNIT: Monomer. The propeptide region interacts with bmp4 in a non-
CC       covalent manner (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q91620}.
CC   -!- TISSUE SPECIFICITY: Expressed in the dorsal marginal region of late
CC       blastula, becoming restricted to the dorsal blastopore lip (Spemann
CC       organizer) at the early gastrula stage. {ECO:0000269|PubMed:8612984}.
CC   -!- DOMAIN: The propeptide region is both necessary and sufficient for bmp-
CC       inhibitory activity. The propeptide region and the N- and C-terminal
CC       thirds of the mature protein are necessary for neural induction
CC       activity. Although cleavage doesn't appear essential for activity,
CC       residues surrounding the cleavage site are necessary for activity (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC59735.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U29588; AAC59735.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001079065.1; NM_001085596.1.
DR   AlphaFoldDB; Q91621; -.
DR   GeneID; 373597; -.
DR   KEGG; xla:373597; -.
DR   CTD; 373597; -.
DR   Xenbase; XB-GENE-864903; nodal3.2.L.
DR   OrthoDB; 1518399at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 373597; Expressed in blastula and 1 other tissue.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
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   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; PS51362; TGF_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Developmental protein; Disulfide bond;
KW   Gastrulation; Glycoprotein; Growth factor; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..274
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338452"
FT   CHAIN           275..401
FT                   /note="Nodal homolog 3-B"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000338453"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        299..365
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   DISULFID        328..396
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   CONFLICT        94..95
FT                   /note="TT -> IY (in Ref. 1; AAC59735)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   401 AA;  46044 MW;  3BDE4D8E5E2D8D02 CRC64;
     MALLNLFFCL VFSSPLMAMP PVLQGRKSMS PDSILKDTST DDGARDFQGR KFPQFMMQLY
     QNIIRGRDKD LSNLEHPTLQ ESDTVQSFIT KSYTTVGNHW TLFFDMSSIS RSNELKLAEL
     RFSLPSFRKS HSVTVDIYHT NDGKEKLFMG SFKTKPSAAL DADCKVFNLT ILLQNFLTRG
     KRLIKDEYIQ AKGLHLKDLE KSATEKGTEN VDTLKQDQYH VSDFAAERIM LVVFAKEQSH
     AKSDPPSLGK KLFPSKYGID DNANKVNGFR RLRRNKKEKT QIHVSTGPPK PIEEIKPKCK
     KVDMFVDFQK IGWGSWIVYP KAYNAYRCES TCAVPLNETE NATNHSYIKS LLPLSDMERK
     ECPSCVPVKM MSMSMLYYEN EDFILRHHEE MIVEECGFKD M