SDC4A_XENLA
ID SDC4A_XENLA Reviewed; 193 AA.
AC Q1AGV7; A2RRX5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Syndecan 4-A;
DE AltName: Full=Syndecan-4.1;
DE Short=xSyn4.1;
DE Flags: Precursor;
GN Name=sdc4-a; Synonyms=sdc4.1 {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:ABA12131.1}
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:0000312|EMBL:AAI31895.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:AAI31895.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI31895.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ116028; ABA12131.1; -; mRNA.
DR EMBL; BC131894; AAI31895.1; ALT_INIT; mRNA.
DR RefSeq; NP_001089176.1; NM_001095707.1.
DR AlphaFoldDB; Q1AGV7; -.
DR SMR; Q1AGV7; -.
DR GeneID; 734218; -.
DR KEGG; xla:734218; -.
DR CTD; 734218; -.
DR Xenbase; XB-GENE-6251682; sdc4.S.
DR OMA; GSWVPTE; -.
DR OrthoDB; 1780343at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 734218; Expressed in egg cell 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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..193
FT /note="Syndecan 4-A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000283776"
FT TOPO_DOM 17..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 23..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 193 AA; 21547 MW; D207A679C6E96D16 CRC64;
MSPTLMFVLL LCGVAAESIR ETETMDPTSM LEYESSGSFP DEVFDDDEID EDDDYAIDED
DEDYSGSGTD KFDIDDNDED EEEEETATLG NQIPELDFDQ TKTGRKIETN EIDNEIWSPT
KPKILEPSNE ISMASTGSEG FFQRTEVIVA IVAGTLVGLV VAISFIVFLV IRRNQNGDLV
KKPIYKKTST MEV
