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T-cell surface glycoprotein CD4 (T-cell surface antigen T4/Leu-3) (CD antigen CD4)

 CD4_DELLE               Reviewed;         455 AA.
Q9XS78;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 73.
RecName: Full=T-cell surface glycoprotein CD4;
AltName: Full=T-cell surface antigen T4/Leu-3;
AltName: CD_antigen=CD4;
Flags: Precursor;
Name=CD4;
Delphinapterus leucas (Beluga whale).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Cetacea;
Odontoceti; Monodontidae; Delphinapterus.
NCBI_TaxID=9749;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Thymus;
PubMed=10199913; DOI=10.1007/s002510050510;
Romano T.A., Ridgway S.H., Felten D.L., Quaranta V.;
"Molecular cloning and characterization of CD4 in an aquatic mammal,
the white whale Delphinapterus leucas.";
Immunogenetics 49:376-383(1999).
-!- FUNCTION: Integral membrane glycoprotein that plays an essential
role in the immune response and serves multiple functions in
responses against both external and internal offenses. In T-cells,
functions primarily as a coreceptor for MHC class II
molecule:peptide complex. The antigens presented by class II
peptides are derived from extracellular proteins while class I
peptides are derived from cytosolic proteins. Interacts
simultaneously with the T-cell receptor (TCR) and the MHC class II
presented by antigen presenting cells (APCs). In turn, recruits
the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK
then initiates different intracellular signaling pathways by
phosphorylating various substrates ultimately leading to
lymphokine production, motility, adhesion and activation of T-
helper cells. In other cells such as macrophages or NK cells,
plays a role in differentiation/activation, cytokine expression
and cell migration in a TCR/LCK-independent pathway. Participates
in the development of T-helper cells in the thymus and triggers
the differentiation of monocytes into functional mature
macrophages. {ECO:0000250|UniProtKB:P01730}.
-!- SUBUNIT: Forms disulfide-linked homo-dimers at the cell surface.
Interacts with LCK. Interacts with PTK2/FAK1. Binds to P4HB/PDI.
Interacts with IL16; this interaction induces a CD4-dependent
signaling in lymphocytes. {ECO:0000250|UniProtKB:P01730}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P01730}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P01730}. Note=Localizes to lipid
rafts. {ECO:0000250|UniProtKB:P01730}.
-!- PTM: Palmitoylation and association with LCK contribute to the
enrichment of CD4 in lipid rafts. {ECO:0000250|UniProtKB:P01730}.
-!- PTM: Phosphorylated by PKC; phosphorylation plays an important
role for CD4 internalization. {ECO:0000250|UniProtKB:P01730}.
-----------------------------------------------------------------------
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EMBL; AF071799; AAD23738.1; -; mRNA.
ProteinModelPortal; Q9XS78; -.
SMR; Q9XS78; -.
PRIDE; Q9XS78; -.
HOVERGEN; HBG005281; -.
Proteomes; UP000248483; Genome assembly.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR000973; CD4.
InterPro; IPR015274; CD4-extracel.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR008424; Ig_C2-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR021963; Tcell_CD4_Cterm.
PANTHER; PTHR11422:SF0; PTHR11422:SF0; 1.
Pfam; PF05790; C2-set; 2.
Pfam; PF09191; CD4-extracel; 1.
Pfam; PF00047; ig; 1.
Pfam; PF12104; Tcell_CD4_C; 1.
PRINTS; PR00692; CD4TCANTIGEN.
SMART; SM00409; IG; 3.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 2.
2: Evidence at transcript level;
Adaptive immunity; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 455 T-cell surface glycoprotein CD4.
/FTId=PRO_0000045165.
TOPO_DOM 26 394 Extracellular. {ECO:0000255}.
TRANSMEM 395 415 Helical. {ECO:0000255}.
TOPO_DOM 416 455 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 125 Ig-like V-type.
DOMAIN 126 203 Ig-like C2-type 1.
DOMAIN 204 314 Ig-like C2-type 2.
DOMAIN 315 371 Ig-like C2-type 3.
MOD_RES 430 430 Phosphoserine.
{ECO:0000250|UniProtKB:P01730}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000250|UniProtKB:P01730}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000250|UniProtKB:P01730}.
LIPID 419 419 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 220 220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 343 343 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 109 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 325 367 {ECO:0000255|PROSITE-ProRule:PRU00114}.
SEQUENCE 455 AA; 50499 MW; AA532FD4411AA5D1 CRC64;
MDPRTSLRHL FLVLQLVMLP AGTQGKKVVL GKAGELAELP CKASQNKSLF FSWKNSYQTK
ILGRHGYFWH KGASNLHSRV ESKINLWDQG SFPLVIKDLE VPDSGTYICE VEDKKIEVEL
QVFRLTASSD TRLLLGQSLT LTLEGPSGSN PSVQWKGPGN KRKNEAKSLS LPQVGLQDSG
TWTCTVSQAQ QTLVFNKHIL VLAFQEVSST VYAKEGEQMN FSFPLTFGDE NLSGELSWLQ
AKGNSSPESW ITFKLNNGKV TVGKARKDLK LRMSKALPLH LTLPQALPQY AGSGNLTLNL
TKGKLYQEVN LVVMRVTKSP NSLTCEVLGP TSPRLILSLK KENQSMRVSD QQKLVTVLGP
EAGMWQCLLS DKGKVLLESK VKILPPVLAH AWPKLLAVVL GGITSLLLLA GFCIFSAKCW
HRRRRAERTS QIKRLLSEKK TCHCSHRLQK TCSLT


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