ID   CD28_FELCA              Reviewed;         221 AA.
AC   O02757;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=T-cell-specific surface glycoprotein CD28;
DE   AltName: CD_antigen=CD28;
DE   Flags: Precursor;
GN   Name=CD28;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10973685; DOI=10.1016/s0165-2427(00)00192-6;
RA   Choi I.S., Hash S.M., Collisson E.W.;
RT   "Molecular cloning and expression of feline CD28 and CTLA-4 cDNA.";
RL   Vet. Immunol. Immunopathol. 76:45-59(2000).
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; U57754; AAB53574.1; -; mRNA.
DR   AlphaFoldDB; O02757; -.
DR   SMR; O02757; -.
DR   STRING; 9685.ENSFCAP00000013242; -.
DR   eggNOG; ENOG502SAVP; Eukaryota.
DR   InParanoid; O02757; -.
DR   Proteomes; UP000011712; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
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:0045840; P:positive regulation of mitotic nuclear division; ISS:UniProtKB.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR   GO; GO:0042110; P:T cell activation; IBA:GO_Central.
DR   GO; GO:0031295; P:T cell costimulation; IBA:GO_Central.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 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; PTHR11494; 1.
DR   Pfam; PF15910; V-set_2; 1.
DR   PRINTS; PR01717; CD28ANTIGEN.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; SSF48726; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..221
FT                   /note="T-cell-specific surface glycoprotein CD28"
FT                   /id="PRO_0000226723"
FT   TOPO_DOM        21..153
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        175..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..138
FT                   /note="Ig-like V-type"
FT   MOD_RES         190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10747"
FT   MOD_RES         192
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P10747"
FT   MOD_RES         210
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P10747"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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   221 AA;  25317 MW;  5B71717E461AE5E3 CRC64;
     MILRLLLALN FFPSIQVTEN KILVKQLPRL VVYNNEVNLS CKYTHNFFSK EFRASLYKGV
     DSAVEVCVVN GNYSHQPQFY SSTGFDCDGK LGNETVTFYL RNLFVNQTDI YFCKIEVMYP
     PPYIDNEKSN GTIIHVKEKH LCPAQLSPES SKPFWALVVV GGILGFYSLL ATVALGACWM
     KTKRSRILQS DYMNMTPRRP GPTRRHYQPY APARDFAAYR S