ID   ICOS_CANLF              Reviewed;         208 AA.
AC   Q7YR73;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Inducible T-cell costimulator;
DE   AltName: Full=Activation-inducible lymphocyte immunomediatory molecule;
DE   AltName: CD_antigen=CD278;
DE   Flags: Precursor;
GN   Name=ICOS; Synonyms=AILIM;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lee J.-H., Kuhr C., Storb R.;
RT   "Cloning and characterization of canine ICOS gene.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Enhances all basic T-cell responses to a foreign antigen,
CC       namely proliferation, secretion of lymphokines, up-regulation of
CC       molecules that mediate cell-cell interaction, and effective help for
CC       antibody secretion by B-cells. Essential both for efficient interaction
CC       between T and B-cells and for normal antibody responses to T-cell
CC       dependent antigens. Does not up-regulate the production of interleukin-
CC       2, but superinduces the synthesis of interleukin-10. Prevents the
CC       apoptosis of pre-activated T-cells. Plays a critical role in CD40-
CC       mediated class switching of immunoglobin isotypes (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
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DR   EMBL; AY342349; AAQ20845.1; -; mRNA.
DR   RefSeq; NP_001002972.1; NM_001002972.2.
DR   AlphaFoldDB; Q7YR73; -.
DR   SMR; Q7YR73; -.
DR   STRING; 9612.ENSCAFP00000018974; -.
DR   PaxDb; Q7YR73; -.
DR   Ensembl; ENSCAFT00030041709; ENSCAFP00030036390; ENSCAFG00030022677.
DR   Ensembl; ENSCAFT00040047502; ENSCAFP00040041463; ENSCAFG00040025457.
DR   Ensembl; ENSCAFT00845032572; ENSCAFP00845025476; ENSCAFG00845018403.
DR   GeneID; 403456; -.
DR   KEGG; cfa:403456; -.
DR   CTD; 29851; -.
DR   VEuPathDB; HostDB:ENSCAFG00845018403; -.
DR   eggNOG; ENOG502S59F; Eukaryota.
DR   GeneTree; ENSGT00390000000801; -.
DR   HOGENOM; CLU_1315009_0_0_1; -.
DR   InParanoid; Q7YR73; -.
DR   OMA; QDKEDCF; -.
DR   OrthoDB; 1298290at2759; -.
DR   TreeFam; TF335679; -.
DR   Reactome; R-CFA-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-CFA-388841; Costimulation by the CD28 family.
DR   Reactome; R-CFA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Proteomes; UP000002254; Chromosome 37.
DR   Bgee; ENSCAFG00000012880; Expressed in blood and 33 other tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0031295; P:T cell costimulation; IBA:GO_Central.
DR   GO; GO:0002517; P:T cell tolerance induction; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR039943; ICOS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013106; Ig_V-set.
DR   PANTHER; PTHR20904; PTHR20904; 1.
DR   Pfam; PF15910; V-set_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..208
FT                   /note="Inducible T-cell costimulator"
FT                   /id="PRO_0000014805"
FT   TOPO_DOM        20..140
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..132
FT                   /note="Ig-like V-type"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..108
FT                   /evidence="ECO:0000250"
FT   DISULFID        63..82
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   208 AA;  23587 MW;  8BAB95D1A07FAC7E CRC64;
     MKSDLWYFLL FCFQVEALTG EINDSTKSEM FTFHDGGVQI LCKFNAIVSQ YKMELLKGTE
     VLCDLTTTKE NGNTVSKNPK FCQSQSSSDG VSFFLYNLDS SHASYYACQL SIFDPPPFQR
     KNISREYLNV YESQTCCQLK FWLPIGCAAF VVVYIFGCIF LCWLTKKKYR SSVHDPNSEY
     MFMAAVNTAK KPGLTGVTHN LELCGTQA