ID   L5M8L7_MYODS            Unreviewed;       191 AA.
AC   L5M8L7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Thy-1 membrane glycoprotein {ECO:0000256|ARBA:ARBA00019731};
DE   AltName: Full=Thy-1 antigen {ECO:0000256|ARBA:ARBA00032696};
GN   ORFNames=MDA_GLEAN10008942 {ECO:0000313|EMBL:ELK34058.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK34058.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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; KB103369; ELK34058.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5M8L7; -.
DR   eggNOG; ENOG502S18P; Eukaryota.
DR   Proteomes; UP000010556; 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; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR033292; THY1.
DR   PANTHER; PTHR19226; THY-1 MEMBRANE GLYCOPROTEIN; 1.
DR   PANTHER; PTHR19226:SF2; THY-1 MEMBRANE GLYCOPROTEIN; 1.
DR   Pfam; PF00047; ig; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 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:UP000010556};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          35..151
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
SQ   SEQUENCE   191 AA;  21044 MW;  19747CF221250AA1 CRC64;
     MACVAGSPWH TGLISWLTPC SHPQILNQAL GTMNPALSIA LLLTGLQVAG GQKVTSLTAC
     LEDQSLRLDC RHENTTTVPM QFEFSLTRDA KKHVLFGTIP EHTYRSRTNL TNRSTLKVLY
     LSGFTSRDEG LYTCELYVPG QPPSFSNRNV SVLRDKLVKC RGVGLLAQDA SWLLLLLLSL
     PLLQAMDFVS L
//