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