NOD3A_XENTR
ID NOD3A_XENTR Reviewed; 401 AA.
AC Q800C0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Nodal homolog 3-A;
DE AltName: Full=Nodal-related protein 3-A;
DE AltName: Full=Xtnr3-A;
DE Flags: Precursor;
GN Name=nodal3-A {ECO:0000250|UniProtKB:Q91620};
GN Synonyms=nr3-A {ECO:0000312|EMBL:BAC75530.1};
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:BAC75530.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH BMP4, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula {ECO:0000269|PubMed:14697360};
RX PubMed=14697360; DOI=10.1016/j.ydbio.2003.09.015;
RA Haramoto Y., Tanegashima K., Onuma Y., Takahashi S., Sekizaki H.,
RA Asashima M.;
RT "Xenopus tropicalis nodal-related gene 3 regulates BMP signaling: an
RT essential role for the pro-region.";
RL Dev. Biol. 265:155-168(2004).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH BMP4, AND DOMAIN.
RX PubMed=16762322; DOI=10.1016/j.bbrc.2006.05.121;
RA Haramoto Y., Takahashi S., Asashima M.;
RT "Two distinct domains in pro-region of Nodal-related 3 are essential for
RT BMP inhibition.";
RL Biochem. Biophys. Res. Commun. 346:470-478(2006).
RN [3] {ECO:0000305}
RP FUNCTION, MONOMER, AND MUTAGENESIS OF PHE-398 AND 398-PHE--ILE-401.
RX PubMed=17089091; DOI=10.1007/s00427-006-0115-2;
RA Haramoto Y., Takahashi S., Asashima M.;
RT "Monomeric mature protein of Nodal-related 3 activates Xbra expression.";
RL Dev. Genes Evol. 217:29-37(2007).
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 (By similarity). The unprocessed protein antagonizes bmp-
CC signaling. {ECO:0000250|UniProtKB:Q91609, ECO:0000269|PubMed:14697360,
CC ECO:0000269|PubMed:16762322, ECO:0000269|PubMed:17089091}.
CC -!- SUBUNIT: Monomer. The propeptide region interacts with bmp4 in a non-
CC covalent manner. {ECO:0000269|PubMed:14697360,
CC ECO:0000269|PubMed:16762322}.
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 Spemann organizer at the early
CC gastrula stage. {ECO:0000269|PubMed:14697360}.
CC -!- DEVELOPMENTAL STAGE: First detected at the blastula stage (stage 8).
CC Expression peaks through the mid-blastula (stage 8.5) to early gastrula
CC (stage 10) and then decreases during gastrulation.
CC {ECO:0000269|PubMed:14697360}.
CC -!- DOMAIN: The propeptide region and the N- and C-terminal thirds of the
CC mature protein are necessary for neural induction activity. Although
CC cleavage doesn't appear essential for activity, residues surrounding
CC the cleavage site are necessary for activity (By similarity). The
CC propeptide region is both necessary and sufficient for bmp-inhibitory
CC activity. {ECO:0000250, ECO:0000269|PubMed:16762322}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000255}.
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DR EMBL; AB093327; BAC75530.1; -; mRNA.
DR RefSeq; NP_001297040.1; NM_001310111.1.
DR AlphaFoldDB; Q800C0; -.
DR PaxDb; Q800C0; -.
DR GeneID; 101732995; -.
DR KEGG; xtr:101732995; -.
DR eggNOG; KOG3900; Eukaryota.
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:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
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 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 1: Evidence at protein 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_0000338454"
FT CHAIN 275..401
FT /note="Nodal homolog 3-A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338455"
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 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 MUTAGEN 398..401
FT /note="FKDI->CY: Still unable to dimerize."
FT /evidence="ECO:0000269|PubMed:17089091"
FT MUTAGEN 398
FT /note="F->C: Still unable to dimerize."
FT /evidence="ECO:0000269|PubMed:17089091"
SQ SEQUENCE 401 AA; 45802 MW; 4F05B296131ADD0C CRC64;
MAFLSLFLCL VFSSPLMAMP PALQGRKAIS PASILKGPST DNGARDFHGR KFPHFMMQLY
QNIISRRDKD LSNLEHPTLQ ESDTVQSFIA KSYTTVGNHW TLFFDMSSIS TSNELKLAEL
RICLPSFGKS HSVTVEIYHT KDTKEKLFMG SFKTKISSAL DADCKVFNLT MVLHNYLIRG
KRLIKDEYIQ AKGLLLRDLE KSAAEKGAEN VDTLKQDKYH VSDFAAERII LVVFAKERSQ
AKPDPPSLGK QLFPLKYGMA DNANKVNGFR RLRRNKKEKT RIDVGTTPPK PVEEIKPKCR
KVDMFVDFQK IGWGSWIVYP KAYNAYRCES ACAVPLNETD DATNYSYIKS LLPLSDTERR
ECPSCVPVKM RSMSMLYYEN EDFVLRHHEE MIVEECGFKD I