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

 CD4_CANLF               Reviewed;         463 AA.
P33705;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
25-OCT-2017, entry version 119.
RecName: Full=T-cell surface glycoprotein CD4;
AltName: Full=T-cell surface antigen T4/Leu-3;
AltName: CD_antigen=CD4;
Flags: Precursor;
Name=CD4;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Beagle; TISSUE=Thymus;
PubMed=8091416; DOI=10.1111/j.1399-0039.1994.tb02320.x;
Gorman S.D., Frewin M.R., Cobbold S.P., Waldmann H.;
"Isolation and expression of cDNA encoding the canine CD4 and CD8
alpha antigens.";
Tissue Antigens 43:184-188(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 13-463.
STRAIN=Beagle; TISSUE=Thymus;
PubMed=7916632; DOI=10.1016/0167-4781(93)90220-8;
Milde K.F., Conner G.E., Minz D.H., Alejandro R.;
"Primary structure of the canine CD4 antigen.";
Biochim. Biophys. Acta 1172:315-318(1993).
-!- 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}.
-!- TISSUE SPECIFICITY: Expressed in macrophages and a subset of T
lymphocytes. {ECO:0000269|PubMed:8091416}.
-!- 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; X68565; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; L06130; AAB02295.1; -; mRNA.
RefSeq; NP_001003252.1; NM_001003252.1.
UniGene; Cfa.3673; -.
ProteinModelPortal; P33705; -.
SMR; P33705; -.
GeneID; 403931; -.
KEGG; cfa:403931; -.
CTD; 920; -.
HOGENOM; HOG000008696; -.
HOVERGEN; HBG005281; -.
InParanoid; P33705; -.
KO; K06454; -.
Proteomes; UP000002254; Unplaced.
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.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
GO; GO:0045058; P:T cell selection; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 3.
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; 1.
2: Evidence at transcript level;
Adaptive immunity; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Lipoprotein; Membrane;
Palmitate; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 463 T-cell surface glycoprotein CD4.
/FTId=PRO_0000014619.
TOPO_DOM 25 401 Extracellular. {ECO:0000255}.
TRANSMEM 402 423 Helical. {ECO:0000255}.
TOPO_DOM 424 463 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 124 Ig-like V-type.
DOMAIN 125 211 Ig-like C2-type 1.
DOMAIN 212 321 Ig-like C2-type 2.
DOMAIN 322 378 Ig-like C2-type 3.
LIPID 424 424 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 427 427 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 109 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 332 374 {ECO:0000255|PROSITE-ProRule:PRU00114}.
SEQUENCE 463 AA; 51640 MW; 95805170CB44A833 CRC64;
MNQEAAFRHL LLMLQLVMLP AVTPVREVVL GKAGDAVELP CQTSQKKNIH FNWRDSSMVQ
ILGNQGSFWT VGSSRLKHRV ESKKNLWDQG SFPLVIKDLE VADSGIYFCD TDKRQEVELL
VFNLTAKWDS GSSSGSSNIR LLQGQQLTLT LENPSGSSPS VQWKGPGNKS KHGGQNLSLS
WPELQDGGTW TCIISQSQKT VEFNINVLVL AFQKVSNTFY AREGDQVEFS FPLSFEDENL
VGELRWQAQG ASSSLLWISF TLENRKLSMK EAHAPLKLQM KESLPLRFTL PQVLSRYAGS
GILTLNLAKG TLYQEVNLVV MRANSSQNNL TCEVLGPTSP ELTLSLNLKE QAAKVSKQQK
LVWVVDPEGG TWQCLLSDKD KVLLASSLNV SSPVVIKSWP KFLAITLGGI LGLLLLIGLC
VFCCVKCWRR RRQAERMSQI KRLLSEKKTC QCSHRIQKTC SLI


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