CD80_MOUSE
ID CD80_MOUSE Reviewed; 306 AA.
AC Q00609; Q61332;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=T-lymphocyte activation antigen CD80;
DE AltName: Full=Activation B7-1 antigen;
DE Short=B7;
DE AltName: CD_antigen=CD80;
DE Flags: Precursor;
GN Name=Cd80; Synonyms=B7;
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 [MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=1714935; DOI=10.1084/jem.174.3.625;
RA Freeman G.J., Gray G.S., Gimmi C.D., Lombard D.B., Zhou L.-J., White M.,
RA Fingeroth J.D., Gribben J.G., Nadler L.M.;
RT "Structure, expression, and T cell costimulatory activity of the murine
RT homologue of the human B lymphocyte activation antigen B7.";
RL J. Exp. Med. 174:625-631(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=B-cell;
RX PubMed=7686531; DOI=10.1007/bf00188807;
RA Selvakumar A., White P.C., Dupont B.;
RT "Genomic organization of the mouse B-lymphocyte activation antigen B7.";
RL Immunogenetics 38:292-295(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=7513163; DOI=10.1006/bbrc.1994.1469;
RA Inobe M., Linsley P.S., Ledbetter J.A., Nagai Y., Tamakoshi M., Uede T.;
RT "Identification of an alternatively spliced form of the murine homologue of
RT B7.";
RL Biochem. Biophys. Res. Commun. 200:443-449(1994).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-149; ASN-189; ASN-210 AND
RP ASN-214.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
CC -!- FUNCTION: Involved in the costimulatory signal essential for T
CC lymphocytes activation. T-cell proliferation and cytokine production is
CC induced by the binding of CD28 or CTLA-4 to this receptor.
CC -!- INTERACTION:
CC Q00609; Q9EP73: Cd274; NbExp=7; IntAct=EBI-5258929, EBI-5258879;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q00609-1; Sequence=Displayed;
CC Name=2; Synonyms=MB7-2;
CC IsoId=Q00609-2; Sequence=VSP_012552;
CC -!- TISSUE SPECIFICITY: Expressed on activated B-cells, gamma interferon
CC stimulated monocytes and non-circulating B-cell malignancies.
CC -!- DEVELOPMENTAL STAGE: Expressed between 4 and 12 hours post-activation.
CC Protein was detected at cell surface at 24 hours and it's expression
CC was maximal from 48 to 72 hours post-activation.
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DR EMBL; X60958; CAA43291.1; -; mRNA.
DR EMBL; L12589; AAA37240.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L12585; AAA37240.1; JOINED; Genomic_DNA.
DR EMBL; L12586; AAA37240.1; JOINED; Genomic_DNA.
DR EMBL; L12587; AAA37240.1; JOINED; Genomic_DNA.
DR EMBL; L12588; AAA37240.1; JOINED; Genomic_DNA.
DR EMBL; D16220; BAA03748.1; -; mRNA.
DR CCDS; CCDS28168.1; -. [Q00609-1]
DR PIR; I49503; I49503.
DR RefSeq; NP_033985.3; NM_009855.2. [Q00609-1]
DR PDB; 4RWH; X-ray; 1.80 A; A=40-144.
DR PDBsum; 4RWH; -.
DR AlphaFoldDB; Q00609; -.
DR SMR; Q00609; -.
DR IntAct; Q00609; 1.
DR STRING; 10090.ENSMUSP00000097404; -.
DR GlyGen; Q00609; 6 sites.
DR iPTMnet; Q00609; -.
DR PhosphoSitePlus; Q00609; -.
DR SwissPalm; Q00609; -.
DR EPD; Q00609; -.
DR PaxDb; Q00609; -.
DR PRIDE; Q00609; -.
DR ProteomicsDB; 265628; -. [Q00609-1]
DR ProteomicsDB; 265629; -. [Q00609-2]
DR Antibodypedia; 16574; 2279 antibodies from 52 providers.
DR DNASU; 12519; -.
DR Ensembl; ENSMUST00000099816; ENSMUSP00000097404; ENSMUSG00000075122. [Q00609-1]
DR Ensembl; ENSMUST00000231716; ENSMUSP00000156031; ENSMUSG00000075122. [Q00609-1]
DR Ensembl; ENSMUST00000232409; ENSMUSP00000156252; ENSMUSG00000075122. [Q00609-2]
DR GeneID; 12519; -.
DR KEGG; mmu:12519; -.
DR UCSC; uc007zez.2; mouse. [Q00609-1]
DR UCSC; uc012afo.1; mouse. [Q00609-2]
DR CTD; 941; -.
DR MGI; MGI:101775; Cd80.
DR VEuPathDB; HostDB:ENSMUSG00000075122; -.
DR eggNOG; ENOG502S5B5; Eukaryota.
DR GeneTree; ENSGT00940000162632; -.
DR HOGENOM; CLU_071073_2_0_1; -.
DR InParanoid; Q00609; -.
DR OMA; YLPRHVC; -.
DR OrthoDB; 1083437at2759; -.
DR PhylomeDB; Q00609; -.
DR TreeFam; TF351094; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-389356; CD28 co-stimulation.
DR Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR BioGRID-ORCS; 12519; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Cd80; mouse.
DR PRO; PR:Q00609; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q00609; protein.
DR Bgee; ENSMUSG00000075122; Expressed in granulocyte and 68 other tissues.
DR ExpressionAtlas; Q00609; baseline and differential.
DR Genevisible; Q00609; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; ISO:MGI.
DR GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central.
DR GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IDA:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IGI:MGI.
DR GO; GO:0031295; P:T cell costimulation; IDA:MGI.
DR CDD; cd16083; IgC_CD80; 1.
DR CDD; cd16086; IgV_CD80; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR037676; CD80_IgC.
DR InterPro; IPR042711; CD80_IgV.
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 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..37
FT CHAIN 38..306
FT /note="T-lymphocyte activation antigen CD80"
FT /id="PRO_0000014548"
FT TOPO_DOM 38..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..135
FT /note="Ig-like V-type"
FT DOMAIN 148..229
FT /note="Ig-like C2-type"
FT REGION 227..246
FT /note="Ig-hinge-like"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT DISULFID 54..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 165..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 144..237
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7513163"
FT /id="VSP_012552"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4RWH"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4RWH"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:4RWH"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:4RWH"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:4RWH"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4RWH"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4RWH"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4RWH"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4RWH"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:4RWH"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:4RWH"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4RWH"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:4RWH"
FT STRAND 129..142
FT /evidence="ECO:0007829|PDB:4RWH"
SQ SEQUENCE 306 AA; 34590 MW; 1DBADE0931B84C62 CRC64;
MACNCQLMQD TPLLKFPCPR LILLFVLLIR LSQVSSDVDE QLSKSVKDKV LLPCRYNSPH
EDESEDRIYW QKHDKVVLSV IAGKLKVWPE YKNRTLYDNT TYSLIILGLV LSDRGTYSCV
VQKKERGTYE VKHLALVKLS IKADFSTPNI TESGNPSADT KRITCFASGG FPKPRFSWLE
NGRELPGINT TISQDPESEL YTISSQLDFN TTRNHTIKCL IKYGDAHVSE DFTWEKPPED
PPDSKNTLVL FGAGFGAVIT VVVIVVIIKC FCKHRSCFRR NEASRETNNS LTFGPEEALA
EQTVFL
