ICOSL_MOUSE
ID ICOSL_MOUSE Reviewed; 322 AA.
AC Q9JHJ8;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=ICOS ligand;
DE AltName: Full=B7 homolog 2;
DE Short=B7-H2;
DE AltName: Full=B7-like protein Gl50;
DE AltName: Full=B7-related protein 1;
DE Short=B7RP-1;
DE AltName: Full=LICOS;
DE AltName: CD_antigen=CD275;
DE Flags: Precursor;
GN Name=Icoslg; Synonyms=B7h2, B7rp1, Icosl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Lymphocyte;
RX PubMed=10617205; DOI=10.1038/45582;
RA Yoshinaga S.K., Whoriskey J.S., Khare S.D., Sarmiento U., Guo J., Horan T.,
RA Shih G., Zhang M., Coccia M.A., Kohno T., Tafuri-Bladt A., Brankow D.,
RA Campbell P., Chang D., Chiu L., Dai T., Duncan G., Elliott G.S., Hui A.,
RA McCabe S.M., Scully S., Shahinian A., Shaklee C.L., Van G., Mak T.W.,
RA Senaldi G.;
RT "T-cell co-stimulation through B7RP-1 and ICOS.";
RL Nature 402:827-832(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=10549624; DOI=10.1016/s1074-7613(00)80117-x;
RA Swallow M.M., Wallin J.J., Sha W.C.;
RT "B7h, a novel costimulatory homolog of B7.1 and B7.2, is induced by
RT TNFalpha.";
RL Immunity 11:423-432(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=C3H/HeJ; TISSUE=Fetal thymus;
RX PubMed=10657606; DOI=10.4049/jimmunol.164.4.1653;
RA Ling V., Wu P.W., Finnerty H.F., Bean K.M., Spaulding V., Fouser L.A.,
RA Leonard J.P., Hunter S.E., Zollner R., Thomas J.L., Miyashiro J.S.,
RA Jacobs K.A., Collins M.;
RT "Identification of GL50, a novel B7-like protein that functionally binds to
RT ICOS receptor.";
RL J. Immunol. 164:1653-1657(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC TISSUE=Peripheral blood lymphocyte;
RX PubMed=11390480; DOI=10.4049/jimmunol.166.12.7300;
RA Ling V., Wu P.W., Miyashiro J.S., Marusic S., Finnerty H.F., Collins M.;
RT "Differential expression of inducible costimulator-ligand splice variants:
RT lymphoid regulation of mouse gl50-b and human gl50 molecules.";
RL J. Immunol. 166:7300-7308(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RA Ling V., Dunussi-Joannopolulos K.;
RT "Gl50 molecules and uses therefor.";
RL Patent number WO0121796, 29-MAR-2001.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Ligand for the T-cell-specific cell surface receptor ICOS.
CC Acts as a costimulatory signal for T-cell proliferation and cytokine
CC secretion; induces also B-cell proliferation and differentiation into
CC plasma cells. Could play an important role in mediating local tissue
CC responses to inflammatory conditions, as well as in modulating the
CC secondary immune response by co-stimulating memory T-cell function.
CC During pregnancy, may function to skew the cytokine of maternal T-cells
CC toward immunoprotective Th2 phenotype.
CC -!- SUBUNIT: Interacts with CTLA4 (in vitro).
CC {ECO:0000250|UniProtKB:O75144}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75144};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9JHJ8-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9JHJ8-2; Sequence=VSP_002521;
CC -!- TISSUE SPECIFICITY: Isoform 1 highest expression in lymphoid tissues,
CC such as spleen (mostly in the marginal zone), lymph nodes (particularly
CC in the cortex and in both primary and secondary follicles), thymus
CC (predominantly in the medulla) and Peyer patches (mostly in the
CC follicles), lower levels in many non-lymphoid tissues, such as brain,
CC heart, kidney, liver, lung, skeletal muscle and testis. Present on
CC freshly isolated splenic B-cells, T-cells, dendritic cells and
CC macrophages. The expression of isoform 2 is restricted to heart, spleen
CC and kidney.
CC -!- DEVELOPMENTAL STAGE: Detected early in hemopoiesis: in the yolk sac at
CC 11.5 and 12.5 dpc and, to a lesser extent, in the liver at 14.5 dpc.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
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DR EMBL; AF216747; AAF45149.1; -; mRNA.
DR EMBL; AF199027; AAF34738.1; -; mRNA.
DR EMBL; AX100591; CAC36463.1; -; Unassigned_DNA.
DR EMBL; AX100593; CAC36464.1; -; Unassigned_DNA.
DR EMBL; AF394451; AAK77544.1; -; mRNA.
DR EMBL; BC029227; AAH29227.1; -; mRNA.
DR CCDS; CCDS35956.1; -. [Q9JHJ8-1]
DR RefSeq; NP_056605.1; NM_015790.3. [Q9JHJ8-1]
DR AlphaFoldDB; Q9JHJ8; -.
DR SMR; Q9JHJ8; -.
DR STRING; 10090.ENSMUSP00000101032; -.
DR GlyGen; Q9JHJ8; 7 sites.
DR PhosphoSitePlus; Q9JHJ8; -.
DR MaxQB; Q9JHJ8; -.
DR PaxDb; Q9JHJ8; -.
DR PRIDE; Q9JHJ8; -.
DR ProteomicsDB; 273086; -. [Q9JHJ8-1]
DR ProteomicsDB; 273087; -. [Q9JHJ8-2]
DR DNASU; 50723; -.
DR Ensembl; ENSMUST00000105393; ENSMUSP00000101032; ENSMUSG00000000732. [Q9JHJ8-1]
DR GeneID; 50723; -.
DR KEGG; mmu:50723; -.
DR UCSC; uc007fxi.1; mouse. [Q9JHJ8-1]
DR CTD; 50723; -.
DR MGI; MGI:1354701; Icosl.
DR VEuPathDB; HostDB:ENSMUSG00000000732; -.
DR eggNOG; ENOG502SQ2A; Eukaryota.
DR GeneTree; ENSGT00940000161590; -.
DR HOGENOM; CLU_013137_8_2_1; -.
DR InParanoid; Q9JHJ8; -.
DR OMA; VYWQIAD; -.
DR PhylomeDB; Q9JHJ8; -.
DR TreeFam; TF331083; -.
DR Reactome; R-MMU-388841; Costimulation by the CD28 family.
DR BioGRID-ORCS; 50723; 5 hits in 113 CRISPR screens.
DR ChiTaRS; Icosl; mouse.
DR PRO; PR:Q9JHJ8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9JHJ8; protein.
DR Bgee; ENSMUSG00000000732; Expressed in peripheral lymph node and 138 other tissues.
DR ExpressionAtlas; Q9JHJ8; baseline and differential.
DR Genevisible; Q9JHJ8; MM.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0045190; P:isotype switching; NAS:UniProtKB.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; TAS:UniProtKB.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IMP:UniProtKB.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; B-cell activation; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..46
FT /evidence="ECO:0000250"
FT CHAIN 47..322
FT /note="ICOS ligand"
FT /id="PRO_0000014804"
FT TOPO_DOM 47..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..149
FT /note="Ig-like V-type"
FT DOMAIN 167..263
FT /note="Ig-like C2-type"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 185..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 321..322
FT /note="HA -> TWAPVPYQDYLIPRYLMSPCLKTRGLP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002521"
FT CONFLICT 237
FT /note="R -> H (in Ref. 4; AAK77544 and 5; CAC36464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35960 MW; 55CCBA4AD12E47E6 CRC64;
MQLKCPCFVS LGTRQPVWKK LHVSSGFFSG LGLFLLLLSS LCAASAETEV GAMVGSNVVL
SCIDPHRRHF NLSGLYVYWQ IENPEVSVTY YLPYKSPGIN VDSSYKNRGH LSLDSMKQGN
FSLYLKNVTP QDTQEFTCRV FMNTATELVK ILEEVVRLRV AANFSTPVIS TSDSSNPGQE
RTYTCMSKNG YPEPNLYWIN TTDNSLIDTA LQNNTVYLNK LGLYDVISTL RLPWTSRGDV
LCCVENVALH QNITSISQAE SFTGNNTKNP QETHNNELKV LVPVLAVLAA AAFVSFIIYR
RTRPHRSYTG PKTVQLELTD HA
