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T-cell surface glycoprotein CD4 (T-cell differentiation antigen L3T4) (T-cell surface antigen T4/Leu-3) (CD antigen CD4)

 CD4_MOUSE               Reviewed;         457 AA.
P06332;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
22-NOV-2017, entry version 175.
RecName: Full=T-cell surface glycoprotein CD4;
AltName: Full=T-cell differentiation antigen L3T4;
AltName: Full=T-cell surface antigen T4/Leu-3;
AltName: CD_antigen=CD4;
Flags: Precursor;
Name=Cd4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3094146; DOI=10.1126/science.3094146;
Tourvieille B., Gorman S.D., Field E.H., Hunkapiller T., Parnes J.R.;
"Isolation and sequence of L3T4 complementary DNA clones: expression
in T cells and brain.";
Science 234:610-614(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3027575; DOI=10.1038/325453a0;
Littman D.R., Gettner S.N.;
"Unusual intron in the immunoglobulin domain of the newly isolated
murine CD4 (L3T4) gene.";
Nature 325:453-455(1987).
[3]
NUCLEOTIDE SEQUENCE.
TISSUE=Brain;
PubMed=3326818; DOI=10.1111/j.1600-065X.1987.tb00529.x;
Parnes J.R., Hunkapiller T.;
"L3T4 and the immunoglobulin gene superfamily: new relationships
between the immune system and the nervous system.";
Immunol. Rev. 100:109-127(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=2823269; DOI=10.1073/pnas.84.21.7644;
Gorman S.D., Tourvieille B., Parnes J.R.;
"Structure of the mouse gene encoding CD4 and an unusual transcript in
brain.";
Proc. Natl. Acad. Sci. U.S.A. 84:7644-7648(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9445485;
Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M.,
Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W.,
Gibbs R.A.;
"Comparative sequence analysis of a gene-rich cluster at human
chromosome 12p13 and its syntenic region in mouse chromosome 6.";
Genome Res. 8:29-40(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 27-43.
PubMed=3082751; DOI=10.1007/BF00377974;
Classon B.J., Tsagaratos J., Kirszbaum L., Maddox J., McKay C.R.,
Brandon M., McKenzie I.F.C., Walker I.D.;
"The L3T4 antigen in mouse and the sheep equivalent are
immunoglobulin-like.";
Immunogenetics 23:129-132(1986).
[8]
DISULFIDE BONDS.
PubMed=3086886; DOI=10.1073/pnas.83.12.4499;
Classon B.J., Tsagaratos J., McKenzie I.F.C., Walker I.D.;
"Partial primary structure of the T4 antigens of mouse and sheep:
assignment of intrachain disulfide bonds.";
Proc. Natl. Acad. Sci. U.S.A. 83:4499-4503(1986).
[9]
FUNCTION, INTERACTION WITH LCK, AND SUBCELLULAR LOCATION.
PubMed=3262426;
Veillette A., Bookman M.A., Horak E.M., Bolen J.B.;
"The CD4 and CD8 T cell surface antigens are associated with the
internal membrane tyrosine-protein kinase p56lck.";
Cell 55:301-308(1988).
[10]
FUNCTION.
PubMed=2784195; DOI=10.1038/338257a0;
Veillette A., Bookman M.A., Horak E.M., Samelson L.E., Bolen J.B.;
"Signal transduction through the CD4 receptor involves the activation
of the internal membrane tyrosine-protein kinase p56lck.";
Nature 338:257-259(1989).
[11]
PHOSPHORYLATION.
PubMed=2512251;
DiSanto J.P., Klein J.S., Flomenberg N.;
"Phosphorylation and down-regulation of CD4 and CD8 in human CTLs and
mouse L cells.";
Immunogenetics 30:494-501(1989).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=1832488; DOI=10.1038/353180a0;
Rahemtulla A., Fung-Leung W.P., Schilham M.W., Kuendig T.M.,
Sambhara S.R., Narendran A., Arabian A., Wakeham A., Paige C.J.,
Zinkernagel R.M.;
"Normal development and function of CD8+ cells but markedly decreased
helper cell activity in mice lacking CD4.";
Nature 353:180-184(1991).
[13]
TISSUE SPECIFICITY.
PubMed=10706685;
Vremec D., Pooley J., Hochrein H., Wu L., Shortman K.;
"CD4 and CD8 expression by dendritic cell subtypes in mouse thymus and
spleen.";
J. Immunol. 164:2978-2986(2000).
[14]
FUNCTION, AND SUBUNIT.
PubMed=16709847;
Maekawa A., Schmidt B., Fazekas de St Groth B., Sanejouand Y.H.,
Hogg P.J.;
"Evidence for a domain-swapped CD4 dimer as the coreceptor for binding
to class II MHC.";
J. Immunol. 176:6873-6878(2006).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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,
ECO:0000269|PubMed:16709847, ECO:0000269|PubMed:1832488,
ECO:0000269|PubMed:2784195, ECO:0000269|PubMed:3262426}.
-!- 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}.
-!- INTERACTION:
P06240:Lck; NbExp=3; IntAct=EBI-1404, EBI-1401;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P01730}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P01730}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P06332-1; Sequence=Displayed;
Name=2; Synonyms=Brain-specific;
IsoId=P06332-2; Sequence=VSP_002489;
-!- TISSUE SPECIFICITY: Highly expressed in T-helper cells. The
presence of CD4 is a hallmark of T-helper cells which are
specialized in the activation and growth of cytotoxic T-cells,
regulation of B cells, or activation of phagocytes. CD4 is also
present in other immune cells such as macrophages, dendritic cells
or NK cells. {ECO:0000250|UniProtKB:P01730,
ECO:0000269|PubMed:10706685}.
-!- 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:0000269|PubMed:2512251}.
-!- DISRUPTION PHENOTYPE: Mice lacking Cd4 display markedly decreased
T-helper cell activity. {ECO:0000269|PubMed:1832488}.
-----------------------------------------------------------------------
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EMBL; M36850; AAA39401.1; -; mRNA.
EMBL; M13816; AAA37267.1; -; mRNA.
EMBL; X04836; CAA28539.1; -; mRNA.
EMBL; M36851; AAA39402.1; -; Genomic_DNA.
EMBL; M17080; AAA37403.1; -; Genomic_DNA.
EMBL; M17078; AAA37403.1; JOINED; Genomic_DNA.
EMBL; M17079; AAA37403.1; JOINED; Genomic_DNA.
EMBL; AC002397; AAC36010.1; -; Genomic_DNA.
EMBL; BC039137; AAH39137.1; -; mRNA.
CCDS; CCDS20535.1; -. [P06332-1]
PIR; A02110; RWMST4.
RefSeq; NP_038516.1; NM_013488.2. [P06332-1]
UniGene; Mm.2209; -.
ProteinModelPortal; P06332; -.
SMR; P06332; -.
BioGrid; 198599; 1.
IntAct; P06332; 5.
MINT; MINT-5024918; -.
STRING; 10090.ENSMUSP00000024044; -.
iPTMnet; P06332; -.
PhosphoSitePlus; P06332; -.
PaxDb; P06332; -.
PRIDE; P06332; -.
Ensembl; ENSMUST00000024044; ENSMUSP00000024044; ENSMUSG00000023274. [P06332-1]
GeneID; 12504; -.
KEGG; mmu:12504; -.
UCSC; uc009dsi.1; mouse. [P06332-1]
UCSC; uc012esr.1; mouse. [P06332-2]
CTD; 920; -.
MGI; MGI:88335; Cd4.
eggNOG; ENOG410IK9F; Eukaryota.
eggNOG; ENOG410YWI4; LUCA.
GeneTree; ENSGT00390000001745; -.
HOGENOM; HOG000008696; -.
HOVERGEN; HBG005281; -.
InParanoid; P06332; -.
KO; K06454; -.
OMA; PEAGMWQ; -.
OrthoDB; EOG091G0AZL; -.
PhylomeDB; P06332; -.
TreeFam; TF335974; -.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-MMU-202433; Generation of second messenger molecules.
Reactome; R-MMU-389948; PD-1 signaling.
Reactome; R-MMU-449836; Other interleukin signaling.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
PRO; PR:P06332; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000023274; -.
CleanEx; MM_CD4; -.
ExpressionAtlas; P06332; baseline and differential.
Genevisible; P06332; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0019865; F:immunoglobulin binding; IEA:Ensembl.
GO; GO:0042011; F:interleukin-16 binding; ISO:MGI.
GO; GO:0042012; F:interleukin-16 receptor activity; ISO:MGI.
GO; GO:0042289; F:MHC class II protein binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISO:MGI.
GO; GO:0001816; P:cytokine production; IMP:MGI.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:MGI.
GO; GO:0035397; P:helper T cell enhancement of adaptive immune response; IMP:UniProtKB.
GO; GO:0006948; P:induction by virus of host cell-cell fusion; ISO:MGI.
GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISO:MGI.
GO; GO:0032507; P:maintenance of protein location in cell; ISO:MGI.
GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IEA:Ensembl.
GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0033674; P:positive regulation of kinase activity; ISO:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
GO; GO:0045657; P:positive regulation of monocyte differentiation; ISO:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0050870; P:positive regulation of T cell activation; IDA:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0046598; P:positive regulation of viral entry into host cell; ISO:MGI.
GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
GO; GO:0050863; P:regulation of T cell activation; ISO:MGI.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
GO; GO:0045058; P:T cell selection; ISS:UniProtKB.
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; 3.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Lipoprotein; Membrane;
Palmitate; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 26 {ECO:0000269|PubMed:3082751}.
CHAIN 27 457 T-cell surface glycoprotein CD4.
/FTId=PRO_0000014627.
TOPO_DOM 27 394 Extracellular. {ECO:0000255}.
TRANSMEM 395 417 Helical. {ECO:0000255}.
TOPO_DOM 418 457 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 128 Ig-like V-type.
DOMAIN 129 207 Ig-like C2-type 1.
DOMAIN 208 317 Ig-like C2-type 2.
DOMAIN 318 374 Ig-like C2-type 3.
LIPID 418 418 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 421 421 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 298 298 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 42 112 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:3086886}.
DISULFID 159 188 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:3086886}.
DISULFID 328 370 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:3086886}.
VAR_SEQ 1 240 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_002489.
SEQUENCE 457 AA; 51297 MW; 1B1DA7527CB00F33 CRC64;
MCRAISLRRL LLLLLQLSQL LAVTQGKTLV LGKEGESAEL PCESSQKKIT VFTWKFSDQR
KILGQHGKGV LIRGGSPSQF DRFDSKKGAW EKGSFPLIIN KLKMEDSQTY ICELENRKEE
VELWVFKVTF SPGTSLLQGQ SLTLTLDSNS KVSNPLTECK HKKGKVVSGS KVLSMSNLRV
QDSDFWNCTV TLDQKKNWFG MTLSVLGFQS TAITAYKSEG ESAEFSFPLN FAEENGWGEL
MWKAEKDSFF QPWISFSIKN KEVSVQKSTK DLKLQLKETL PLTLKIPQVS LQFAGSGNLT
LTLDKGTLHQ EVNLVVMKVA QLNNTLTCEV MGPTSPKMRL TLKQENQEAR VSEEQKVVQV
VAPETGLWQC LLSEGDKVKM DSRIQVLSRG VNQTVFLACV LGGSFGFLGF LGLCILCCVR
CRHQQRQAAR MSQIKRLLSE KKTCQCPHRM QKSHNLI


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