ID   THY1_MACMU              Reviewed;         161 AA.
AC   O62643;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   07-OCT-2020, entry version 114.
DE   RecName: Full=Thy-1 membrane glycoprotein;
DE   AltName: Full=Thy-1 antigen;
DE   AltName: CD_antigen=CD90;
DE   Flags: Precursor;
GN   Name=THY1;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thymus;
RA   Margulies B.J., Clements J.E.;
RT   "Rhesus macaque CD90.";
RL   Submitted (MAR-1997) 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
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DR   EMBL; U93310; AAC05640.1; -; mRNA.
DR   STRING; 9544.ENSMMUP00000011701; -.
DR   PRIDE; O62643; -.
DR   eggNOG; ENOG502S18P; Eukaryota.
DR   InParanoid; O62643; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0034235; F:GPI anchor binding; ISS:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR   GO; GO:0050870; P:positive regulation of T cell activation; ISS:UniProtKB.
DR   GO; GO:0046549; P:retinal cone cell development; ISS:UniProtKB.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 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; PTHR19226; 1.
DR   Pfam; PF00047; ig; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Phosphoprotein;
KW   Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT   SIGNAL          1..19
FT   CHAIN           20..130
FT                   /note="Thy-1 membrane glycoprotein"
FT                   /id="PRO_0000014975"
FT   PROPEP          131..161
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000014976"
FT   DOMAIN          20..126
FT                   /note="Ig-like V-type"
FT   MOD_RES         20
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P01831"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01830"
FT   LIPID           130
FT                   /note="GPI-anchor amidated cysteine; alternate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..130
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        38..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   161 AA;  18011 MW;  326B135498BA401B CRC64;
     MNLAISIALL LTVLQVSRGQ KVTSLTACLV DQSLRLDCRH ENTTSSPIQY EFSLTRETKK
     HVLFGTVGVP EHTYRSRTNF TSKYNMKVLY LSAFTXKDEG TYTCXLHHSG HSPPISSQNV
     TVLRDKLVKC EGISLLAQNT SWLXLLLLSL SLLQATDFMS L