THY1_CHICK
ID THY1_CHICK Reviewed; 160 AA.
AC Q07212;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Thy-1 membrane glycoprotein;
DE AltName: Full=Thy-1 antigen;
DE Flags: Precursor;
GN Name=THY1;
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], AND PROTEIN SEQUENCE OF 43-55; 59-79 AND
RP 81-101.
RC STRAIN=White leghorn; TISSUE=Brain;
RX PubMed=1359371; DOI=10.1016/0169-328x(92)90180-j;
RA Dowsing B.J., Gooley A.A., Gunning P., Cunningham A., Jeffrey P.L.;
RT "Molecular cloning and primary structure of the avian Thy-1 glycoprotein.";
RL Brain Res. Mol. Brain Res. 14:250-260(1992).
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}.
CC -!- TISSUE SPECIFICITY: Forebrain, cerebellum and tectum.
CC -!- DEVELOPMENTAL STAGE: It is detected at embryonic day 4 (E4) in
CC forebrain and tectum. There is an increase in levels between E16 and
CC the first few days post-hatch. During E19 to hatch a rapid reduction in
CC the levels is seen with a general increase in expression in adulthood.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:1359371}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S47368; AAA11889.1; -; mRNA.
DR EMBL; L14924; AAC42216.1; -; mRNA.
DR PIR; A48975; A48975.
DR AlphaFoldDB; Q07212; -.
DR SMR; Q07212; -.
DR BioGRID; 675315; 1.
DR IntAct; Q07212; 1.
DR STRING; 9031.ENSGALP00000040036; -.
DR VEuPathDB; HostDB:geneid_378897; -.
DR eggNOG; ENOG502S18P; Eukaryota.
DR InParanoid; Q07212; -.
DR PhylomeDB; Q07212; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
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; 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.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..129
FT /note="Thy-1 membrane glycoprotein"
FT /id="PRO_0000014971"
FT PROPEP 130..160
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000014972"
FT DOMAIN 20..120
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P01831"
FT LIPID 129
FT /note="GPI-anchor amidated cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..129
FT /evidence="ECO:0000250"
FT DISULFID 38..103
FT /evidence="ECO:0000250"
FT CONFLICT 76
FT /note="R -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="H -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 160 AA; 18165 MW; E378D241CC2D4739 CRC64;
MNPTVSIAVI LTVLQAAHCQ MIRDLSACLL GQSLRVDCRY ENKTSNPLTY EFSLTRQQKH
IIQSTISVSE NVYRNRANVT MHKNLVCLYL HSFTTSDEGV YMCELKATND YTGNQIKNIT
VIKDKLEKCV RLSLLIQNTS WLLLLLLSLP LLQAVDFVSL
