CD8B_FELCA
ID CD8B_FELCA Reviewed; 210 AA.
AC P79336;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=T-cell surface glycoprotein CD8 beta chain;
DE AltName: CD_antigen=CD8b;
DE Flags: Precursor;
GN Name=CD8B; Synonyms=CD8B1;
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].
RC TISSUE=Thymus;
RX PubMed=8911144; DOI=10.1046/j.1365-2567.1996.d01-710.x;
RA Pecoraro M.R., Shimojima M., Maeda K., Inoshima Y., Kawaguchi Y., Kai C.,
RA Mikami T.;
RT "Molecular cloning of the feline CD8 beta-chain.";
RL Immunology 89:84-88(1996).
CC -!- FUNCTION: Integral membrane glycoprotein that plays an essential role
CC in the immune response and serves multiple functions in responses
CC against both external and internal offenses. In T-cells, functions
CC primarily as a coreceptor for MHC class I molecule:peptide complex. The
CC antigens presented by class I peptides are derived from cytosolic
CC proteins while class II derived from extracellular proteins. Interacts
CC simultaneously with the T-cell receptor (TCR) and the MHC class I
CC proteins presented by antigen presenting cells (APCs). In turn,
CC recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. A
CC palmitoylation site in the cytoplasmic tail of CD8B chain contributes
CC to partitioning of CD8 into the plasma membrane lipid rafts where
CC signaling proteins are enriched. Once LCK recruited, it initiates
CC different intracellular signaling pathways by phosphorylating various
CC substrates ultimately leading to lymphokine production, motility,
CC adhesion and activation of cytotoxic T-lymphocytes (CTLs).
CC Additionally, plays a critical role in thymic selection of CD8+ T-
CC cells. {ECO:0000250|UniProtKB:P10300, ECO:0000250|UniProtKB:P10966}.
CC -!- SUBUNIT: Forms disulfide-linked heterodimers with CD8A at the cell
CC surface. Interacts with CD3D; this interaction couples TCR-CD3 with
CC CD8. Interacts with LCK. {ECO:0000250|UniProtKB:P10300,
CC ECO:0000250|UniProtKB:P10966}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P10966};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P10966}.
CC Note=Requires the partner CD8A for efficient cell surface expression.
CC The heterodimer CD8A/CD8B localizes to lipid rafts due to CD8B
CC cytoplasmic tail palmitoylation. {ECO:0000250|UniProtKB:P10966}.
CC -!- PTM: Phosphorylated as a consequence of T-cell activation.
CC {ECO:0000250|UniProtKB:P10966}.
CC -!- PTM: Palmitoylated at the cytoplasmic tail and thereby targets the
CC heterodimer CD8A/CD8B to lipid rafts unlike CD8A homodimers.
CC {ECO:0000250|UniProtKB:P10966}.
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DR EMBL; AB000484; BAA19125.1; -; mRNA.
DR RefSeq; NP_001009867.1; NM_001009867.1.
DR AlphaFoldDB; P79336; -.
DR SMR; P79336; -.
DR STRING; 9685.ENSFCAP00000025660; -.
DR GeneID; 493948; -.
DR KEGG; fca:493948; -.
DR CTD; 926; -.
DR eggNOG; ENOG502SANQ; Eukaryota.
DR InParanoid; P79336; -.
DR OrthoDB; 1377095at2759; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
DR GO; GO:0042288; F:MHC class I protein binding; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR042414; CD8B.
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; PTHR11292; PTHR11292; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..210
FT /note="T-cell surface glycoprotein CD8 beta chain"
FT /id="PRO_0000014642"
FT TOPO_DOM 22..170
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..132
FT /note="Ig-like V-type"
FT REGION 139..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 210 AA; 23105 MW; 9E00A4AEAC8C6293 CRC64;
MQPGLWLLLA TQLAALRGSS VLQQAPGSVM VQTNGMVIMS CEAKTSPTST RIYWLRHRQA
PSPDSHYECL AYWDPIKGIV YGQEVEPEKL TVFPDATRSI LNLTSVKPAD SGIYFCMTVG
SPELTFGKGT RLSVVDVLPT NSQPTKKPTP RKKMCRPPSP VTQKGPSCGL LTLGLLVAGV
LVLLVSLGVA IHLYRLKRRA RLRLLKQFYK
