SHSA3_XENLA
ID SHSA3_XENLA Reviewed; 232 AA.
AC Q7T0Z7; Q2WFL7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Protein shisa-3;
DE Flags: Precursor;
GN Name=shisa3;
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].
RA Nagano T., Takehara S., Aizawa S., Yamamoto A.;
RT "Shisa family gene.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH FZD8 AND FGFR1, AND SUBCELLULAR LOCATION.
RX PubMed=17065233; DOI=10.1242/dev.02657;
RA Nagano T., Takehara S., Takahashi M., Aizawa S., Yamamoto A.;
RT "Shisa2 promotes the maturation of somitic precursors and transition to the
RT segmental fate in Xenopus embryos.";
RL Development 133:4643-4654(2006).
CC -!- FUNCTION: Plays an essential role in the maturation of presomitic
CC mesoderm cells by individual attenuation of both fgf and wnt signaling.
CC Regulates head and somite developmen. Inhibits both wnt and fgf
CC signaling through the regulation of protein maturation and cell surface
CC transportation of their receptors within the endoplasmic reticulum.
CC {ECO:0000269|PubMed:17065233}.
CC -!- SUBUNIT: Interacts with fzd8 and fgfr1. {ECO:0000269|PubMed:17065233}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250,
CC ECO:0000269|PubMed:17065233}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: 'Shisa' was named after a sculpture form, common to
CC southern Japan, with a large head similar to the Egyptian sphinx.
CC -!- SIMILARITY: Belongs to the shisa family. {ECO:0000305}.
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DR EMBL; AB242598; BAE53532.1; -; mRNA.
DR EMBL; BC055970; AAH55970.1; -; mRNA.
DR RefSeq; NP_001079833.1; NM_001086364.1.
DR AlphaFoldDB; Q7T0Z7; -.
DR SMR; Q7T0Z7; -.
DR GeneID; 379523; -.
DR KEGG; xla:379523; -.
DR CTD; 379523; -.
DR Xenbase; XB-GENE-939879; shisa3.S.
DR OMA; YTSGCLQ; -.
DR OrthoDB; 1325567at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 379523; Expressed in brain and 9 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR026910; Shisa.
DR PANTHER; PTHR31395; PTHR31395; 1.
DR Pfam; PF13908; Shisa; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..232
FT /note="Protein shisa-3"
FT /id="PRO_0000330027"
FT TOPO_DOM 20..93
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 146..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 200
FT /note="N -> D (in Ref. 1; BAE53532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 25241 MW; 83EADC7102E24E21 CRC64;
MRLLGCFFLI FLTWGSARAQ GEYCHGWLDS AGNYQAGFQC PEDFDTADAN ICCGSCALRY
CCAAADARLE QGSCTNHREL EKSGVSAQPV YVPFLIVGSI FIAFIIVGSL VAVYCCTCLR
PKQTSQQPMR FTLRSYPPET LPMILTSGNL RTPSRQSSTA TSSTSTGGSV RRLSSSRADP
GYLVSSPPPP YSSAHSIHLN PSSTFLVSNQ YFPYPLQPEA IANKSCPDFR QS