ID   VSIG1_XENLA             Reviewed;         318 AA.
AC   Q91664; Q91665;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=V-set and immunoglobulin domain-containing protein 1;
DE   AltName: Full=Cortical thymocyte marker CTX;
DE   Flags: Precursor;
GN   Name=vsig1; Synonyms=ctx;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Thymus;
RX   PubMed=8625968; DOI=10.1002/eji.1830260409;
RA   Chretien I., Robert J., Marcuz A., Garcia-Sanz J.A., Courtet M.,
RA   Du Pasquier L.;
RT   "CTX, a novel molecule specifically expressed on the surface of cortical
RT   thymocytes in Xenopus.";
RL   Eur. J. Immunol. 26:780-791(1996).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in thymocytes.
CC       {ECO:0000269|PubMed:8625968}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC59860.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U43330; AAC59899.1; -; mRNA.
DR   EMBL; U43393; AAC59860.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; NP_001079275.1; NM_001085806.1.
DR   AlphaFoldDB; Q91664; -.
DR   SMR; Q91664; -.
DR   GeneID; 378558; -.
DR   KEGG; xla:378558; -.
DR   CTD; 378558; -.
DR   Xenbase; XB-GENE-865058; vsig1.L.
DR   OrthoDB; 841952at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 378558; Expressed in stomach and 9 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0003382; P:epithelial cell morphogenesis; IEA:InterPro.
DR   GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR029861; VSIG1.
DR   PANTHER; PTHR44974; PTHR44974; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Immunoglobulin domain; Membrane; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..318
FT                   /note="V-set and immunoglobulin domain-containing protein
FT                   1"
FT                   /id="PRO_0000313576"
FT   TOPO_DOM        20..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..318
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          20..131
FT                   /note="Ig-like V-type"
FT   DOMAIN          136..223
FT                   /note="Ig-like C2-type"
FT   REGION          261..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        41..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        157..207
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        226..227
FT                   /note="Missing (in Ref. 1; AAC59860)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237..241
FT                   /note="GGLLA -> ERTVG (in Ref. 1; AAC59860)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   318 AA;  34429 MW;  6231D24B0B806C09 CRC64;
     MSFLLFITLG LSLTALSHCV QVTIQNPIIN VTSGQNATLY CTYILNNQNK NNLVIQWNIF
     QAKSQNQETV FFYQNGQSLS GPSYKNRVTA AMSPGNATIT ISNMQSQDTG IYTCEVLNLP
     ESSGQGKILL TVLVPPSVPH CSIRGAVETG HFISLLCYSE EGMPRPIYSW NRVENGLLKS
     TPSQMNQQKG SLIIGNLTDF EEGYYRCTAS NNLGNATCEL NLHTGGEGGV IAAAVIGGLL
     AAAIIIAIVW FLVVKRKQKK QLPPTKEMKT GGNQYMAVSG EANEPPKENL GASEPTETIQ
     FHDHAENAAN GETEEPTA