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Database: UniProt
Entry: A0A093CZX9_TAUER
LinkDB: A0A093CZX9_TAUER
Original site: A0A093CZX9_TAUER 
ID   A0A093CZX9_TAUER        Unreviewed;       161 AA.
AC   A0A093CZX9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Thy-1 membrane glycoprotein {ECO:0000256|ARBA:ARBA00019731};
DE   AltName: Full=Thy-1 antigen {ECO:0000256|ARBA:ARBA00032696};
GN   ORFNames=N340_06428 {ECO:0000313|EMBL:KFV20028.1};
OS   Tauraco erythrolophus (Red-crested turaco).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX   NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV20028.1, ECO:0000313|Proteomes:UP000053661};
RN   [1] {ECO:0000313|EMBL:KFV20028.1, ECO:0000313|Proteomes:UP000053661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV20028.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in cell-cell or cell-ligand interactions
CC       during synaptogenesis and other events in the brain.
CC       {ECO:0000256|ARBA:ARBA00003467}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
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DR   EMBL; KL474265; KFV20028.1; -; Genomic_DNA.
DR   RefSeq; XP_009988027.1; XM_009989725.1.
DR   AlphaFoldDB; A0A093CZX9; -.
DR   GeneID; 104381896; -.
DR   KEGG; teo:104381896; -.
DR   CTD; 7070; -.
DR   OrthoDB; 5304893at2759; -.
DR   Proteomes; UP000053661; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005178; F:integrin binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR033292; THY1.
DR   PANTHER; PTHR19226; THY-1 MEMBRANE GLYCOPROTEIN; 1.
DR   PANTHER; PTHR19226:SF2; THY-1 MEMBRANE GLYCOPROTEIN; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053661};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..161
FT                   /note="Thy-1 membrane glycoprotein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001882872"
FT   DOMAIN          33..106
FT                   /note="Immunoglobulin V-set"
FT                   /evidence="ECO:0000259|SMART:SM00406"
SQ   SEQUENCE   161 AA;  18102 MW;  4FBB2EC665F1B59B CRC64;
     MNPTLGIAVI LTVLQAAHCQ MIKDLSACLL GQSLRVDCRY ENKTSNPLTY EFSITKDNRK
     HVIHSTISVS ENIYRSRANV TMHKNLVCLY LQSFTTSDEG VYMCELKATN DYTGNQIKNI
     TVIKDKLEKC AGFSLLIQNT SWLLLLLLSL PLLQAVDFVS L
//
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