ID   XLRS1_TAKRU             Reviewed;         280 AA.
AC   Q9W6R5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Retinoschisin;
DE   AltName: Full=X-linked juvenile retinoschisis protein homolog;
DE   Flags: Precursor;
GN   Name=xlrs1;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10330123;
RA   Brunner B., Todt T., Lenzner S., Stout K., Schulz U., Ropers H.-H.,
RA   Kalscheuer V.M.;
RT   "Genomic structure and comparative analysis of nine Fugu genes:
RT   conservation of synteny with human chromosome Xp22.2-p22.1.";
RL   Genome Res. 9:437-448(1999).
CC   -!- FUNCTION: Binds negatively charged membrane lipids, such as
CC       phosphatidylserine and phosphoinositides. May play a role in cell-cell
CC       adhesion processes in the retina, via homomeric interaction between
CC       octamers present on the surface of two neighboring cells. Required for
CC       normal structure and function of the retina (By similarity).
CC       {ECO:0000250|UniProtKB:O15537, ECO:0000250|UniProtKB:Q9Z1L4}.
CC   -!- SUBUNIT: Homooctamer of 4 homodimers; disulfide-linked. The homooctamer
CC       has a flat, cogwheel structure with a diameter of about 14 nm. Two
CC       stacked octamers can assemble to form a hexadecamer.
CC       {ECO:0000250|UniProtKB:O15537}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O15537}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q9Z1L4}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9Z1L4}; Extracellular side
CC       {ECO:0000250|UniProtKB:Q9Z1L4}. Note=Binds to phosphatidylserine-
CC       containing lipid membranes and embeds itself partially into the lipid
CC       bilayer. Lipid-binding requires the presence of Ca(2+) ions.
CC       {ECO:0000250|UniProtKB:Q9Z1L4}.
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DR   EMBL; AF146687; AAD28797.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9W6R5; -.
DR   SMR; Q9W6R5; -.
DR   STRING; 31033.ENSTRUP00000043697; -.
DR   eggNOG; ENOG502QU6Y; Eukaryota.
DR   InParanoid; Q9W6R5; -.
DR   OMA; IRIHAQE; -.
DR   TreeFam; TF352191; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd00057; FA58C; 1.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   SMART; SM00231; FA58C; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   3: Inferred from homology;
KW   Cell adhesion; Cell membrane; Disulfide bond; Lipid-binding; Membrane;
KW   Reference proteome; Secreted; Sensory transduction; Signal; Vision.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..280
FT                   /note="Retinoschisin"
FT                   /id="PRO_0000022694"
FT   DOMAIN          119..275
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DISULFID        89
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DISULFID        115
FT                   /note="Interchain (with C-279)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DISULFID        119..275
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DISULFID        166..198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DISULFID        279
FT                   /note="Interchain (with C-115)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
SQ   SEQUENCE   280 AA;  32033 MW;  A0DF9A3222ED0167 CRC64;
     MHLPREAFLL ALAGAFIFPS SQQEKRTQRD LRVVCFYQKD FRNGTKAEQW GKKTPTQIWR
     GCMSVCNAIV VCLFELGVSE TWNSKSCKCD CEGGESPTEF PSIRTGSSMV RGVDCMPECP
     YHRPLGFEAG SISPDQITCS NQDQYTAWFS SWLPSKARLN TQGFGCAWLS KFQDNTQWLQ
     IDLIDAKVVS GILTQGRCDA DEWITKYSLQ YRTDEKLNWI YYKDQTGNNR VFYGNSDRSS
     SVQNLLRPPI VARYIRILPL GWHTRIALRL ELLLCMNKCS