DAND5_XENLA
ID DAND5_XENLA Reviewed; 217 AA.
AC Q800X4;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=DAN domain family member 5;
DE AltName: Full=Cerberus-like 2 protein;
DE Short=Cerl-2;
DE Flags: Precursor;
GN Name=dand5; Synonyms=cerl2, coco; ORFNames=S10-51-B6;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12403722; DOI=10.1242/dev.00097;
RA Munoz-Sanjuan I., Bell E., Altmann C.R., Vonica A., Brivanlou A.H.;
RT "Gene profiling during neural induction in Xenopus laevis: regulation of
RT BMP signaling by post-transcriptional mechanisms and TAB3, a novel TAK1-
RT binding protein.";
RL Development 129:5529-5540(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12588853; DOI=10.1242/dev.00344;
RA Bell E., Munoz-Sanjuan I., Altmann C.R., Vonica A., Brivanlou A.H.;
RT "Cell fate specification and competence by Coco, a maternal BMP, TGFbeta
RT and Wnt inhibitor.";
RL Development 130:1381-1389(2003).
RN [4]
RP INTERACTION WITH NR1-A.
RX PubMed=15466485; DOI=10.1101/gad.306504;
RA Marques S., Borges A.C., Silva A.C., Freitas S., Cordenonsi M., Belo J.A.;
RT "The activity of the Nodal antagonist Cerl-2 in the mouse node is required
RT for correct L/R body axis.";
RL Genes Dev. 18:2342-2347(2004).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17239842; DOI=10.1016/j.ydbio.2006.09.039;
RA Vonica A., Brivanlou A.H.;
RT "The left-right axis is regulated by the interplay of Coco, Xnr1 and
RT derriere in Xenopus embryos.";
RL Dev. Biol. 303:281-294(2007).
CC -!- FUNCTION: Plays an important role in regulating the left-right axis by
CC blocking a tgfb1 cascade in the right posterior paraxial mesoderm.
CC Functions as an inhibitor of bmp, tgfb1, nodal, activin and wnt
CC signaling in the ectoderm. May inhibit mesodermal signals, probably
CC through an inhibition of nodal/activin pathways. Seems to regulates
CC cell fate specification and competence before the onset of neural
CC induction. Expression in the entire ectodermal region prior to
CC gastrulation might act to prevent fate specification in the ectoderm
CC and ensure the maintenance of the stem-cell-like properties exhibited
CC by ectodermal cells. {ECO:0000269|PubMed:12588853,
CC ECO:0000269|PubMed:17239842}.
CC -!- SUBUNIT: Interacts with nr1-A. {ECO:0000269|PubMed:15466485}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally in an animal to vegetal
CC gradient, and later on was restricted to the animal region of the
CC embryo. Expressed in the posterior paraxial mesoderm, adjacent to the
CC notochord, from stages 13 to 24. Expression declined rapidly following
CC gastrulation. {ECO:0000269|PubMed:12588853,
CC ECO:0000269|PubMed:17239842}.
CC -!- SIMILARITY: Belongs to the DAN family. {ECO:0000305}.
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DR EMBL; AF549938; AAO48743.1; -; mRNA.
DR EMBL; BC099052; AAH99052.1; -; mRNA.
DR RefSeq; NP_001092196.1; NM_001098726.1.
DR AlphaFoldDB; Q800X4; -.
DR DNASU; 594864; -.
DR GeneID; 594864; -.
DR KEGG; xla:594864; -.
DR CTD; 594864; -.
DR Xenbase; XB-GENE-865412; dand5.S.
DR OrthoDB; 1134947at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 594864; Expressed in egg cell and 9 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016015; F:morphogen activity; IMP:BHF-UCL.
DR GO; GO:0003127; P:detection of nodal flow; IMP:BHF-UCL.
DR GO; GO:0070986; P:left/right axis specification; IMP:BHF-UCL.
DR GO; GO:1900146; P:negative regulation of nodal signaling pathway involved in determination of left/right asymmetry; IMP:BHF-UCL.
DR GO; GO:0048339; P:paraxial mesoderm development; IEP:BHF-UCL.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR016860; Cerberus.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR004133; DAN.
DR PANTHER; PTHR15273; PTHR15273; 1.
DR Pfam; PF03045; DAN; 1.
DR PIRSF; PIRSF027807; Cerberus; 1.
DR SMART; SM00041; CT; 1.
DR PROSITE; PS01225; CTCK_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..217
FT /note="DAN domain family member 5"
FT /id="PRO_0000311806"
FT DOMAIN 116..196
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 116..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 130..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 140..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 144..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
SQ SEQUENCE 217 AA; 24974 MW; C199241DD29BB567 CRC64;
MLLFQATSLL ALLCFTVRAF PFMEEEGSAS FAQNVLHSRS FPVSHHGAFM DLPLFRQNRR
KISQNFILHS DPREHMDEEA LRRKLVWESA IRRDKMRSQP DQVLPIGQDA LKRSRCHALP
FIQNVFRKNC FPVRLPNKFC FGQCNSFYVP GWPAGLSQPC TSCAPSRSRR ISLPLRCRSG
HLAWQEVELV EECECETRYD RNTVEPAGSG EDYLPVS
