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NOD4B_XENLA
ID   NOD4B_XENLA             Reviewed;         352 AA.
AC   Q90XB8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Nodal homolog 4-B;
DE   AltName: Full=Nodal-related protein 4-B;
DE   AltName: Full=Xnr4;
DE   Flags: Precursor; Fragment;
GN   Name=nodal4-b; Synonyms=nr4 {ECO:0000303|PubMed:11934150};
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:AAL02114.1}
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. Plays a role in
CC       mesoderm formation and may be required for neural development (By
CC       similarity). {ECO:0000250|UniProtKB:O13048}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P43021}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q91620}.
CC   -!- INDUCTION: By dorsal mesoderm-inducing signals including activin and
CC       vegt. Not induced by wnt8 alone, but wnt8 potentiates the response to
CC       activin and vegt. {ECO:0000269|PubMed:11934150}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000255}.
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DR   EMBL; AF410800; AAL02114.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q90XB8; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR001839; TGF-b_C.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848; PTHR11848; 1.
DR   Pfam; PF00019; TGF_beta; 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..278
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000334507"
FT   CHAIN           279..>352
FT                   /note="Nodal homolog 4-B"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000334508"
FT   REGION          197..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        302..?
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   DISULFID        331..?
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   DISULFID        335..?
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   NON_TER         352
FT                   /evidence="ECO:0000312|EMBL:AAL02114.1"
SQ   SEQUENCE   352 AA;  40519 MW;  80EB478CBB4D3D57 CRC64;
     MHLYFSCFIL LFVPGGKSLG INSHLKHMSN KSQDQVNRTR TVGSKDVAAL PLSSYMFNLY
     QSFHHSELNH GMEAAPSLSL NHRADIIRSL AVKSYDHGGS LWTFLFDFSS LSQEEEHQFA
     EVRFDFRAFS DAILVGMEVI VDFFHQSSTC QSISGFCQSY LYVGSLTSTL WPRSSDTWVT
     FEATDIIHKW FERNDKGKNH SEGHMKQPKK LHRAKSAERR YQQRSTENPQ ILMMVYSNIS
     KKEKLSGTAT LLQDAAHSKY LAVMPGIQTI ANSRRHRRSH IFNEHIMGMK HVPSADSSRT
     LCRRVDFFVD FKQIGWDSWI IHPVKYNAYR CEGECPSPVN ERLKPNNHAY MQ
 
 
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