ID CD28_MOUSE Reviewed; 218 AA. AC P31041; Q6GSH7; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 27-MAR-2024, entry version 178. DE RecName: Full=T-cell-specific surface glycoprotein CD28; DE AltName: CD_antigen=CD28; DE Flags: Precursor; GN Name=Cd28; 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]. RX PubMed=2157764; RA Gross J.A., St John T., Allison J.P.; RT "The murine homologue of the T lymphocyte antigen CD28. Molecular cloning RT and cell surface expression."; RL J. Immunol. 144:3201-3210(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Thymus; 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). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 156-218. RX PubMed=1713603; RA Harper K., Balzano C., Rouvier E., Mattei M.-G., Luciani M.-F., RA Golstein P.; RT "CTLA-4 and CD28 activated lymphocyte molecules are closely related in both RT mouse and human as to sequence, message expression, gene structure, and RT chromosomal location."; RL J. Immunol. 147:1037-1044(1991). CC -!- FUNCTION: Involved in T-cell activation, the induction of cell CC proliferation and cytokine production and promotion of T-cell survival. CC Enhances the production of IL4 and IL10 in T-cells in conjunction with CC TCR/CD3 ligation and CD40L costimulation. CC {ECO:0000250|UniProtKB:P10747}. CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with DUSP14. Binds to CC CD80/B7-1 and CD86/B7-2/B70. Interacts with GRB2 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. 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; M34563; AAA37395.1; -; mRNA. DR EMBL; AL646054; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL672024; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936842; CAM13249.1; -; Genomic_DNA. DR EMBL; CH466548; EDL00156.1; -; Genomic_DNA. DR EMBL; BC064058; AAH64058.1; -; mRNA. DR EMBL; M74361; AAA37396.1; -; mRNA. DR CCDS; CCDS14992.1; -. DR PIR; A43523; A43523. DR PIR; I49584; I49584. DR RefSeq; NP_031668.3; NM_007642.4. DR PDB; 2NAE; NMR; -; A=177-218. DR PDBsum; 2NAE; -. DR AlphaFoldDB; P31041; -. DR SMR; P31041; -. DR DIP; DIP-60858N; -. DR IntAct; P31041; 3. DR STRING; 10090.ENSMUSP00000027165; -. DR GlyCosmos; P31041; 4 sites, No reported glycans. DR GlyGen; P31041; 4 sites. DR iPTMnet; P31041; -. DR PhosphoSitePlus; P31041; -. DR SwissPalm; P31041; -. DR EPD; P31041; -. DR PaxDb; 10090-ENSMUSP00000027165; -. DR PeptideAtlas; P31041; -. DR ProteomicsDB; 280017; -. DR Antibodypedia; 19958; 3331 antibodies from 49 providers. DR DNASU; 12487; -. DR Ensembl; ENSMUST00000027165.3; ENSMUSP00000027165.3; ENSMUSG00000026012.3. DR GeneID; 12487; -. DR KEGG; mmu:12487; -. DR UCSC; uc007bev.2; mouse. DR AGR; MGI:88327; -. DR CTD; 940; -. DR MGI; MGI:88327; Cd28. DR VEuPathDB; HostDB:ENSMUSG00000026012; -. DR eggNOG; ENOG502SAVP; Eukaryota. DR GeneTree; ENSGT00530000063873; -. DR HOGENOM; CLU_085095_1_0_1; -. DR InParanoid; P31041; -. DR OMA; YSHQLQF; -. DR OrthoDB; 4108912at2759; -. DR PhylomeDB; P31041; -. DR TreeFam; TF335679; -. 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-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR BioGRID-ORCS; 12487; 2 hits in 117 CRISPR screens. DR PRO; PR:P31041; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; P31041; Protein. DR Bgee; ENSMUSG00000026012; Expressed in thymus and 56 other cell types or tissues. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0001772; C:immunological synapse; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0098636; C:protein complex involved in cell adhesion; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0002020; F:protease binding; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; IPI:MGI. DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI. DR GO; GO:0035739; P:CD4-positive, alpha-beta T cell proliferation; IDA:MGI. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI. DR GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:MGI. DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IDA:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:0002863; P:positive regulation of inflammatory response to antigenic stimulus; IMP:MGI. DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISS:UniProtKB. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:MGI. DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB. DR GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IMP:MGI. DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISS:UniProtKB. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:MGI. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0045589; P:regulation of regulatory T cell differentiation; IGI:MGI. DR GO; GO:0045066; P:regulatory T cell differentiation; ISO:MGI. DR GO; GO:0042110; P:T cell activation; ISO:MGI. DR GO; GO:0031295; P:T cell costimulation; IDA:MGI. DR GO; GO:0042098; P:T cell proliferation; IDA:MGI. DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR008093; CD28. DR InterPro; IPR040216; CTLA4/CD28. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013106; Ig_V-set. DR PANTHER; PTHR11494; CYTOTOXIC T-LYMPHOCYTE PROTEIN; 1. DR PANTHER; PTHR11494:SF7; T-CELL-SPECIFIC SURFACE GLYCOPROTEIN CD28; 1. DR Pfam; PF07686; V-set; 1. DR PRINTS; PR01717; CD28ANTIGEN. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR Genevisible; P31041; MM. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Glycoprotein; Immunoglobulin domain; KW Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000250" FT CHAIN 20..218 FT /note="T-cell-specific surface glycoprotein CD28" FT /id="PRO_0000014653" FT TOPO_DOM 20..150 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 151..177 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 178..218 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 29..138 FT /note="Ig-like V-type" FT MOD_RES 187 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P10747" FT MOD_RES 189 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P10747" FT MOD_RES 207 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P10747" FT CARBOHYD 72 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 93 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 106 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 130 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 41..113 FT /evidence="ECO:0000250" FT DISULFID 67..87 FT /evidence="ECO:0000250" FT CONFLICT 187..189 FT /note="SDY -> VTT (in Ref. 1; AAA37395)" FT /evidence="ECO:0000305" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:2NAE" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:2NAE" SQ SEQUENCE 218 AA; 25243 MW; C8E1339DD7E53CA6 CRC64; MTLRLLFLAL NFFSVQVTEN KILVKQSPLL VVDSNEVSLS CRYSYNLLAK EFRASLYKGV NSDVEVCVGN GNFTYQPQFR SNAEFNCDGD FDNETVTFRL WNLHVNHTDI YFCKIEFMYP PPYLDNERSN GTIIHIKEKH LCHTQSSPKL FWALVVVAGV LFCYGLLVTV ALCVIWTNSR RNRLLQSDYM NMTPRRPGLT RKPYQPYAPA RDFAAYRP //