NOD3C_XENTR
ID NOD3C_XENTR Reviewed; 401 AA.
AC Q800B8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Nodal homolog 3-C;
DE AltName: Full=Nodal-related protein 3-C;
DE AltName: Full=Xtnr3-C;
DE Flags: Precursor;
GN Name=nodal3-C {ECO:0000250|UniProtKB:Q91620};
GN Synonyms=nr3-C {ECO:0000312|EMBL:BAC75532.1};
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:BAC75532.1}
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).
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 -!- SUBUNIT: Monomer (By similarity). The propeptide region interacts with
CC bmp4 in a non-covalent manner. {ECO:0000250,
CC ECO:0000269|PubMed:14697360}.
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 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}.
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DR EMBL; AB093329; BAC75532.1; -; mRNA.
DR RefSeq; NP_001106377.1; NM_001112906.1.
DR AlphaFoldDB; Q800B8; -.
DR STRING; 8364.ENSXETP00000019730; -.
DR GeneID; 100127175; -.
DR CTD; 100127175; -.
DR InParanoid; Q800B8; -.
DR Proteomes; UP000008143; Genome assembly.
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_0000338458"
FT CHAIN 275..401
FT /note="Nodal homolog 3-C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000338459"
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"
SQ SEQUENCE 401 AA; 45788 MW; ECF55E5BE2B99F6F CRC64;
MAFLSLFLCL VFSSPLMAMP PALQGRKAIS PASILKGPST DNGARDFHGR KFPHFMMQLY
QNIISRRDKD LSNLEHPTLQ ESDTVQSFIA KSYTTKGNHW TLFFDMSSIS TSNELKSAEL
RICLPSFGKS HSVTVEIYHT KDDKEKLFMG SFKTKISSAL DADCKVFNLT MVLHNYLTKG
KRLIKDEYIQ AKGLLLRDLE KSATETGAER VDIVKQDKHH VSDFSAERII LVVFAKEKDH
AKPDPPSLGK KLFPSKYGMA DSANKVNGFR RLRRNKKEKT RMDVGTTPPK PVEEIKPKCR
KVDMFVDFQK IGWGSWIVYP KAYNAYRCES ACAVPLNETD DATNYSYIKS LLPLSDTDRR
ECPSCVPVKM RSMSMLYYEN EDFVLRHHEE MIVEECGYKD I
