ID CD4_MACFU Reviewed; 458 AA. AC P79184; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 27-SEP-2017, entry version 85. DE RecName: Full=T-cell surface glycoprotein CD4; DE AltName: Full=T-cell surface antigen T4/Leu-3; DE AltName: CD_antigen=CD4; DE Flags: Precursor; GN Name=CD4; OS Macaca fuscata fuscata (Japanese macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9543; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Hashimoto O., Tatsumi M.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Integral membrane glycoprotein that plays an essential CC role in the immune response and serves multiple functions in CC responses against both external and internal offenses. In T-cells, CC functions primarily as a coreceptor for MHC class II CC molecule:peptide complex. The antigens presented by class II CC peptides are derived from extracellular proteins while class I CC peptides are derived from cytosolic proteins. Interacts CC simultaneously with the T-cell receptor (TCR) and the MHC class II CC presented by antigen presenting cells (APCs). In turn, recruits CC the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK CC then initiates different intracellular signaling pathways by CC phosphorylating various substrates ultimately leading to CC lymphokine production, motility, adhesion and activation of T- CC helper cells. In other cells such as macrophages or NK cells, CC plays a role in differentiation/activation, cytokine expression CC and cell migration in a TCR/LCK-independent pathway. Participates CC in the development of T-helper cells in the thymus and triggers CC the differentiation of monocytes into functional mature CC macrophages. {ECO:0000250|UniProtKB:P01730}. CC -!- SUBUNIT: Forms disulfide-linked homo-dimers at the cell surface. CC Interacts with LCK. Interacts with PTK2/FAK1. Binds to P4HB/PDI. CC Interacts with IL16; this interaction induces a CD4-dependent CC signaling in lymphocytes. {ECO:0000250|UniProtKB:P01730}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000250|UniProtKB:P01730}; Single-pass type I membrane CC protein {ECO:0000250|UniProtKB:P01730}. Note=Localizes to lipid CC rafts. {ECO:0000250|UniProtKB:P01730}. CC -!- PTM: Palmitoylation and association with LCK contribute to the CC enrichment of CD4 in lipid rafts. {ECO:0000250|UniProtKB:P01730}. CC -!- PTM: Phosphorylated by PKC; phosphorylation plays an important CC role for CD4 internalization. {ECO:0000250|UniProtKB:P01730}. 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; D63348; BAA09672.1; -; mRNA. DR ProteinModelPortal; P79184; -. DR SMR; P79184; -. DR HOVERGEN; HBG005281; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0015026; F:coreceptor activity; IEA:InterPro. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB. DR GO; GO:0045058; P:T cell selection; ISS:UniProtKB. DR Gene3D; 2.60.40.10; -; 3. DR InterPro; IPR000973; CD4. DR InterPro; IPR015274; CD4-extracel. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR008424; Ig_C2-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR013151; Immunoglobulin. DR InterPro; IPR021963; Tcell_CD4_Cterm. DR PANTHER; PTHR11422:SF3; PTHR11422:SF3; 1. DR Pfam; PF05790; C2-set; 2. DR Pfam; PF09191; CD4-extracel; 1. DR Pfam; PF00047; ig; 1. DR Pfam; PF12104; Tcell_CD4_C; 1. DR PRINTS; PR00692; CD4TCANTIGEN. DR SMART; SM00409; IG; 3. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; SSF48726; 4. DR PROSITE; PS50835; IG_LIKE; 1. PE 2: Evidence at transcript level; KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; KW Immunity; Immunoglobulin domain; Lipoprotein; Membrane; Palmitate; KW Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 25 {ECO:0000250}. FT CHAIN 26 458 T-cell surface glycoprotein CD4. FT /FTId=PRO_0000014623. FT TOPO_DOM 26 396 Extracellular. {ECO:0000255}. FT TRANSMEM 397 418 Helical. {ECO:0000255}. FT TOPO_DOM 419 458 Cytoplasmic. {ECO:0000255}. FT DOMAIN 26 125 Ig-like V-type. FT DOMAIN 126 203 Ig-like C2-type 1. FT DOMAIN 204 317 Ig-like C2-type 2. FT DOMAIN 318 374 Ig-like C2-type 3. FT LIPID 419 419 S-palmitoyl cysteine. {ECO:0000250}. FT LIPID 422 422 S-palmitoyl cysteine. {ECO:0000250}. FT CARBOHYD 42 42 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 296 296 N-linked (GlcNAc...) asparagine. FT {ECO:0000250}. FT CARBOHYD 325 325 N-linked (GlcNAc...) asparagine. FT {ECO:0000250}. FT DISULFID 41 109 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 155 184 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 328 370 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 458 AA; 50828 MW; 76B3E7EF08185535 CRC64; MNRGIPFRHL LLVLQLALLP AVTQGKKVVL GKKGDTVELT CNASQKKNTQ FHWKNSNQIK ILGIQGSFLT KGPSKLSDRA DSRKSLWDQG CFSMIIKNLK IEDSDTYICE VENKKEEVEL LVFGLTANSD THLLEGQSLT LTLESPPGSS PSVKCRSPGG KNIQGGRTIS VPQLERQDSG TWTCTVSQDQ KTVEFKIDIV VLAFQKASST VYKKEGEQVE FSFPLAFTLE KLTGSGELWW QAERASSSKS WITFDLKNKE VSVKRVTQDP KLQMGKKLPL HLTLPQALPQ YAGSGNLTLA LEAKTGKLHQ EVNLVVMRAA QFQENLTCEV WGPTSPKLTL SLKLENKGAT VSKQAKAVWV LNPEAGMWQC LLSDSGQVLL ESNIKVVPTW PTPVQPMALI VLGGVAGLLL FTGLGIFFCV RCRHRRRQAE RMSQIKRLLS EKKTCQCPHR FQKTCSPI //