ID   NOD2B_XENLA             Reviewed;         384 AA.
AC   Q90XB7;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Nodal homolog 2-B;
DE   AltName: Full=Nodal-related protein 2-B;
DE   AltName: Full=Xnr2-B;
DE   Flags: Precursor; Fragment;
GN   Name=nodal2-b;
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:AAL02115.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=11934150;
RA   Rex M., Hilton E., Old R.W.;
RT   "Multiple interactions between maternally-activated signalling pathways
RT   control Xenopus nodal-related genes.";
RL   Int. J. Dev. Biol. 46:217-226(2002).
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. Induces muscle
CC       actin. Appears to act as both a short-range and long-range morphogen.
CC       The unprocessed protein inhibits bmp- and wnt-signaling (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Forms heterodimers with the TGF-
CC       beta family member derriere. Interacts with tsku; enhances nodal2
CC       activity. {ECO:0000250|UniProtKB:P43021, ECO:0000250|UniProtKB:Q91620}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: By dorsal-mesoderm inducing signals including activin, vegt
CC       and other nodal-related proteins. Beta-catenin potentiates the response
CC       to activin and vegt. Not induced by wnt8 alone, but wnt8 potentiates
CC       the response to activin. {ECO:0000269|PubMed:11934150}.
CC   -!- DOMAIN: The pro-region is necessary but not sufficient for wnt-
CC       inhibitory activity. The central region is required for muscle
CC       induction activity (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000255}.
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DR   EMBL; AF410801; AAL02115.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q90XB7; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016015; F:morphogen activity; ISS:UniProtKB.
DR   GO; GO:0048320; P:axial mesoderm formation; ISS:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; ISS:UniProtKB.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; ISS:UniProtKB.
DR   GO; GO:0001707; P:mesoderm formation; ISS:UniProtKB.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; ISS:UniProtKB.
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; Developmental protein; Disulfide bond;
KW   Glycoprotein; Growth factor; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..283
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000274255"
FT   CHAIN           284..>384
FT                   /note="Nodal homolog 2-B"
FT                   /id="PRO_0000274256"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
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        306..372
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   DISULFID        369
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   NON_TER         384
FT                   /evidence="ECO:0000312|EMBL:AAL02115.1"
SQ   SEQUENCE   384 AA;  43542 MW;  91A1954F6A838BAD CRC64;
     MASLGAILLF AIASLMHGRP IHSDRKGAKI PLAGSNLGYK KSSNMYGSRL FQGMRYPPSM
     IQLYQTLILG NDTDLSILEY PVLQESDAVL SFLQKVSCVV VGNRWTLSFD MSSISSTNEL
     KLAELRIRLP SFERPQDVTV EIYHTKKGQE NLFMGSFKTN PSVAMGSSWK VFNLTRMLQY
     YLHQGEQFTN DEYIEVKNLH EGAKPQVIKR RARTEVEEGL QGNKDNTPTS SFPTERVVLV
     VFTRDKPTAN HFGSPSLIHT VESSKYVMSE STVRVADARR HRRNQKTKNT IIMNTIPSRS
     AGNPLCRRVD MIVDFEKIKW GDRIVYPKRF NAYRCEGACP IPLNETFKPT NHAYIKSLVK
     LYDQEKVECS SCVPVKMSPL SMLL