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   27-MAR-2024, entry version 183.
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.ENSMUSP00000156031; -.
DR   GlyCosmos; Q00609; 6 sites, No reported glycans.
DR   GlyGen; Q00609; 6 sites.
DR   iPTMnet; Q00609; -.
DR   PhosphoSitePlus; Q00609; -.
DR   SwissPalm; Q00609; -.
DR   EPD; Q00609; -.
DR   PaxDb; 10090-ENSMUSP00000097404; -.
DR   ProteomicsDB; 265628; -. [Q00609-1]
DR   ProteomicsDB; 265629; -. [Q00609-2]
DR   Antibodypedia; 16574; 2602 antibodies from 53 providers.
DR   DNASU; 12519; -.
DR   Ensembl; ENSMUST00000099816.3; ENSMUSP00000097404.3; ENSMUSG00000075122.6. [Q00609-1]
DR   Ensembl; ENSMUST00000231716.2; ENSMUSP00000156031.2; ENSMUSG00000075122.6. [Q00609-1]
DR   Ensembl; ENSMUST00000232409.2; ENSMUSP00000156252.2; ENSMUSG00000075122.6. [Q00609-2]
DR   GeneID; 12519; -.
DR   KEGG; mmu:12519; -.
DR   UCSC; uc007zez.2; mouse. [Q00609-1]
DR   UCSC; uc012afo.1; mouse. [Q00609-2]
DR   AGR; MGI:101775; -.
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; HMTSVML; -.
DR   OrthoDB; 5401666at2759; -.
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 81 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 69 other cell types or tissues.
DR   ExpressionAtlas; Q00609; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
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:0048018; F:receptor ligand activity; ISO:MGI.
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:0002710; P:negative regulation of T cell mediated immunity; ISO:MGI.
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:0042110; P:T cell activation; ISO:MGI.
DR   GO; GO:0031295; P:T cell costimulation; IDA:MGI.
DR   CDD; cd16083; IgC1_CD80; 1.
DR   CDD; cd16086; IgV_CD80; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR25466; T-LYMPHOCYTE ACTIVATION ANTIGEN; 1.
DR   PANTHER; PTHR25466:SF4; T-LYMPHOCYTE ACTIVATION ANTIGEN CD80; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   Genevisible; Q00609; MM.
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
//