ID CD28_RAT Reviewed; 218 AA.
AC P31042;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 24-JAN-2024, entry version 150.
DE RecName: Full=T-cell-specific surface glycoprotein CD28;
DE AltName: CD_antigen=CD28;
DE Flags: Precursor;
GN Name=Cd28;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DA; TISSUE=Lymphoid tissue;
RX PubMed=1309509; DOI=10.1007/bf00216628;
RA Clark G.J., Dallman M.J.;
RT "Identification of a cDNA encoding the rat CD28 homologue.";
RL Immunogenetics 35:54-57(1992).
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.
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DR EMBL; X55288; CAA39003.1; -; mRNA.
DR PIR; S24413; S24413.
DR RefSeq; NP_037253.1; NM_013121.1.
DR AlphaFoldDB; P31042; -.
DR SMR; P31042; -.
DR STRING; 10116.ENSRNOP00000013701; -.
DR GlyCosmos; P31042; 4 sites, No reported glycans.
DR GlyGen; P31042; 4 sites.
DR PhosphoSitePlus; P31042; -.
DR PaxDb; 10116-ENSRNOP00000013701; -.
DR GeneID; 25660; -.
DR KEGG; rno:25660; -.
DR UCSC; RGD:2299; rat.
DR AGR; RGD:2299; -.
DR CTD; 940; -.
DR RGD; 2299; Cd28.
DR eggNOG; ENOG502SAVP; Eukaryota.
DR InParanoid; P31042; -.
DR OrthoDB; 4108912at2759; -.
DR PhylomeDB; P31042; -.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-389356; CD28 co-stimulation.
DR Reactome; R-RNO-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-RNO-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR PRO; PR:P31042; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; ISO:RGD.
DR GO; GO:0015026; F:coreceptor activity; NAS:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0035739; P:CD4-positive, alpha-beta T cell proliferation; ISO:RGD.
DR GO; GO:0006955; P:immune response; TAS:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0045060; P:negative thymic T cell selection; ISO:RGD.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:RGD.
DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0002863; P:positive regulation of inflammatory response to antigenic stimulus; ISO:RGD.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISS:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISS:UniProtKB.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045589; P:regulation of regulatory T cell differentiation; ISO:RGD.
DR GO; GO:0045066; P:regulatory T cell differentiation; ISO:RGD.
DR GO; GO:0042110; P:T cell activation; ISO:RGD.
DR GO; GO:0031295; P:T cell costimulation; IMP:RGD.
DR GO; GO:0042098; P:T cell proliferation; ISO:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD.
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; PF15910; V-set_2; 1.
DR PRINTS; PR01717; CD28ANTIGEN.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW 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_0000014654"
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"
SQ SEQUENCE 218 AA; 25170 MW; 2E151C8F324C0B6E CRC64;
MTLRLLFLAL SFFSVQVTEN KILVKQSPLL VVDNNEVSLS CRYSYNLLAK EFRASLYKGV
NSDVEVCVGN GNFTYQPQFR PNVGFNCDGN FDNETVTFRL WNLDVNHTDI YFCKIEVMYP
PPYLDNEKSN GTIIHIKEKH LCHAQTSPKL FWPLVVVAGV LLCYGLLVTV TLCIIWTNSR
RNRLLQSDYM NMTPRRLGPT RKHYQPYAPA RDFAAYRP
//
