ID   SHSA1_XENLA             Reviewed;         269 AA.
AC   A2RV66; Q6E4B2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Protein shisa-1;
DE   Flags: Precursor;
GN   Name=shisa1; Synonyms=shisa;
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], SUBCELLULAR LOCATION, FUNCTION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15680328; DOI=10.1016/j.cell.2004.11.051;
RA   Yamamoto A., Nagano T., Takehara S., Hibi M., Aizawa S.;
RT   "Shisa promotes head formation through the inhibition of receptor protein
RT   maturation for the caudalizing factors, Wnt and FGF.";
RL   Cell 120:223-235(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for head formation during gastrulation. Functions as
CC       an inhibitor for the caudalizing signals wnt and fgf, does not inhibit
CC       bmp, activin and nodal signaling in head formation process. Induces
CC       retention of fzd8 in the endoplasmic reticulum and inhibits trafficking
CC       of fzd8 to the cell surface. {ECO:0000269|PubMed:15680328}.
CC   -!- SUBUNIT: Interacts with immature forms of fzd8 and fgfr.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:15680328}. Membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the prospective head ectoderm and the
CC       Spemann organizer at gastrula stage. Expression increases during
CC       gastrulation and decreases during early neurulation. As gastrulation
CC       progresses, expression occurs in the anterior neuroectoderm, after mid-
CC       gastrulation, expressed in the superficial layer. The expression in
CC       endomesoderm concomitantly becomes restricted to the future prechordal
CC       plate territory. At the mid-neurula stage, the ectodermal expression
CC       declines, while that in the prechordal plate persists until the late-
CC       neurula stage. {ECO:0000269|PubMed:15680328}.
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; AY579372; AAT64430.1; -; mRNA.
DR   EMBL; BC133198; AAI33199.1; -; mRNA.
DR   RefSeq; NP_001085264.1; NM_001091795.2.
DR   AlphaFoldDB; A2RV66; -.
DR   SMR; A2RV66; -.
DR   TCDB; 8.A.83.1.5; the shisa6 regulator of short-term neuronal synaptic plasticity (shisa) family.
DR   GeneID; 443566; -.
DR   KEGG; xla:443566; -.
DR   CTD; 443566; -.
DR   Xenbase; XB-GENE-5937902; shisa1.1.L.
DR   OrthoDB; 1317782at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 443566; Expressed in blastula and 9 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; 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   2: Evidence at transcript level;
KW   Developmental protein; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..269
FT                   /note="Protein shisa-1"
FT                   /id="PRO_0000330022"
FT   TOPO_DOM        19..98
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..269
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          129..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        47
FT                   /note="P -> S (in Ref. 1; AAT64430)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="V -> A (in Ref. 1; AAT64430)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   269 AA;  29184 MW;  E9275AC5AB0CD202 CRC64;
     MEFIVLLTVC ALLGLSCGQH GEYCHGWTDS YGIWRPGFQC PERYDPPEAT FCCGSCGLKY
     CCSTVESRLD QGLCPNEEDL RDGVPSIELP PTVPTYFPFL LVGSIFVSFV ILGSLVGLCC
     CKCLKPEDDT QVSGPAPIQS RLLDQDPSTD TSRHSSSSSA SMPRPPIGAR PQNLCSLGAE
     NINLYMNMPP TFPMMGCPQN AQFMHPGTAG PSFMQPPFIN YAVPAEHAII MAPAPYIDAR
     NCYGQTSNIY CQVPQQNDQT VCSGSPSKC