ID   SDC4B_XENLA             Reviewed;         205 AA.
AC   Q1AGV6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Syndecan 4-B;
DE   AltName: Full=Syndecan-4.2;
DE            Short=xSyn4.2;
DE   Flags: Precursor;
GN   Name=sdc4-b; Synonyms=sdc4.2 {ECO:0000303|PubMed:16604063};
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:ABA12132.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DVL2 AND FZD7,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16604063; DOI=10.1038/ncb1399;
RA   Munoz R., Moreno M., Oliva C., Orbenes C., Larrain J.;
RT   "Syndecan-4 regulates non-canonical Wnt signalling and is essential for
RT   convergent and extension movements in Xenopus embryos.";
RL   Nat. Cell Biol. 8:492-500(2006).
RN   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=17041718; DOI=10.1100/tsw.2006.230;
RA   Munoz R., Larrain J.;
RT   "xSyndecan-4 regulates gastrulation and neural tube closure in Xenopus
RT   embryos.";
RL   ScientificWorldJournal 6:1298-1301(2006).
CC   -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC       Regulates non-canonical Wnt signaling, being necessary and sufficient
CC       for fibronectrin-mediated translocation of dvl2/dsh to the plasma
CC       membrane. Required for proper convergent extension movements during
CC       gastrulation, which shape the neural plate, and for subsequent neural
CC       tube closure. {ECO:0000269|PubMed:16604063,
CC       ECO:0000269|PubMed:17041718, ECO:0000305}.
CC   -!- SUBUNIT: Interacts with the Wnt receptor fzd7 and its signal transducer
CC       dvl2/dsh. {ECO:0000269|PubMed:16604063}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in the animal hemisphere from the 4-cell
CC       to the blastula stage. During gastrulation, expressed in the involuting
CC       dorsal mesoderm and ectoderm. After involution, localized mainly to the
CC       anterior neuroectoderm. At later stages, expressed in the brain,
CC       branchial arches, pronephros, tailbud, and at low levels in the
CC       somites. {ECO:0000269|PubMed:16604063}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       {ECO:0000269|PubMed:16604063}.
CC   -!- SIMILARITY: Belongs to the syndecan proteoglycan family. {ECO:0000255}.
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DR   EMBL; DQ116029; ABA12132.1; -; mRNA.
DR   RefSeq; NP_001089177.1; NM_001095708.1.
DR   AlphaFoldDB; Q1AGV6; -.
DR   SMR; Q1AGV6; -.
DR   GeneID; 734219; -.
DR   KEGG; xla:734219; -.
DR   CTD; 734219; -.
DR   Xenbase; XB-GENE-6251681; sdc4.L.
DR   OrthoDB; 1780343at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 734219; Expressed in zone of skin and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
DR   GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:UniProtKB.
DR   GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IPI:UniProtKB.
DR   InterPro; IPR001050; Syndecan.
DR   PANTHER; PTHR10915; PTHR10915; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Gastrulation; Glycoprotein; Heparan sulfate;
KW   Membrane; Proteoglycan; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Wnt signaling pathway.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..205
FT                   /note="Syndecan 4-B"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000283777"
FT   TOPO_DOM        18..162
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..205
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          26..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..96
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        37
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   205 AA;  22929 MW;  46BAFFF08F0EF2BD CRC64;
     MNRLLLLLAL VLSGVAAESI RETETMDPTS MLEYESSGSF TDEVFVDEDD DDDYEDGVDY
     EIDSESDNDE DYSGSGDDDF DDEDNVEDED EEETTTLGNQ IPEHDFDETK TGRKFDTFNE
     NNEIDNDIRH PAKPKTLEPS NEIPMASIGS SGFFQRTEVI VAIIAGTLVG LVVAVSFIVF
     LVIRRNQNGD LVKKPIYKKT STMEV