ID   VSIG1_CHICK             Reviewed;         335 AA.
AC   Q9PWR4; Q9YGH1; Q9YGV5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=V-set and immunoglobulin domain-containing protein 1;
DE   AltName: Full=ChT1 thymocyte antigen;
DE   Flags: Precursor;
GN   Name=VSIG1; Synonyms=ChT1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thymus;
RA   Katevuo K.H., Boyd R., Gobel T.T., Bean A., Dunon D., Imhof B.A.,
RA   Vainio O.;
RT   "ChT1, a new IgSF member inhibits thymocyte differentiation at the double
RT   positive stage.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=9862345;
RX   DOI=10.1002/(sici)1521-4141(199812)28:12<4094::aid-immu4094>3.0.co;2-2;
RA   Chretien I., Marcuz A., Courtet M., Katevuo K., Vainio O., Heath J.K.,
RA   White S.J., Du Pasquier L.;
RT   "CTX, a Xenopus thymocyte receptor, defines a molecular family conserved
RT   throughout vertebrates.";
RL   Eur. J. Immunol. 28:4094-4104(1998).
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:9862345}.
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DR   EMBL; Y14063; CAA74390.1; -; mRNA.
DR   EMBL; Y14064; CAA74391.1; -; mRNA.
DR   EMBL; AF061023; AAD17523.1; -; Genomic_DNA.
DR   RefSeq; NP_001001745.1; NM_001001745.1.
DR   AlphaFoldDB; Q9PWR4; -.
DR   SMR; Q9PWR4; -.
DR   STRING; 9031.ENSGALP00000013480; -.
DR   PaxDb; Q9PWR4; -.
DR   GeneID; 414795; -.
DR   KEGG; gga:414795; -.
DR   CTD; 340547; -.
DR   VEuPathDB; HostDB:geneid_414795; -.
DR   eggNOG; ENOG502QU0R; Eukaryota.
DR   InParanoid; Q9PWR4; -.
DR   OrthoDB; 841952at2759; -.
DR   PhylomeDB; Q9PWR4; -.
DR   PRO; PR:Q9PWR4; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003382; P:epithelial cell morphogenesis; IEA:InterPro.
DR   GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IBA:GO_Central.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..335
FT                   /note="V-set and immunoglobulin domain-containing protein
FT                   1"
FT                   /id="PRO_5000147194"
FT   TOPO_DOM        22..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..335
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..136
FT                   /note="Ig-like V-type"
FT   DOMAIN          139..226
FT                   /note="Ig-like C2-type"
FT   REGION          266..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        43..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        160..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        20
FT                   /note="H -> R (in Ref. 2; AAD17523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="P -> S (in Ref. 2; AAD17523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        246
FT                   /note="A -> D (in Ref. 1; CAA74390)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293..294
FT                   /note="AT -> QP (in Ref. 2; AAD17523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314
FT                   /note="P -> S (in Ref. 2; AAD17523)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   335 AA;  36509 MW;  AA6159598079B438 CRC64;
     MFPTMLKIFP ILATLAGHVH GVVVTVPEKT VNVKTGGNAT LLCTYTSSQP LGNFFIQWSF
     YSAKESQLHT IYYYSEGQSY SYGEFKDRIT AATSPGNASI TISNMQPSDT GSYTCEVFSP
     QDDAGQSQKS VIVNVLVKPS KPFCKIEGTP EKGHLIYLLC KCDQGLPHPT YRWYKVDENT
     LTPVTEYFNP DTGILYIGNL TTFETGHYRC IASNIMGNST CELDLTSMHS DGNIVAGALI
     GAILAAVIIC AIVWVLTKKA KKKKSSSNEM QVMAQKQSNA EYAQVPNEEN TPATAVLPSN
     ATNEQPSADE AAAPETPEND EKHEVQKEET AGSSF