Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01443
Entry Name
UniProt Accession
Theoretical PI
9.6
Molecular Weight
51110.54
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
T-cell surface glycoprotein CD4
Protein Synonyms/Alias
T-cell surface antigen T4/Leu-3; CD4;
Gene Name
CD4
Gene Synonyms/Alias
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
419
Canonical
IGLGIFFCVRCRHRR
[1][2][3]
S-Palmitoylation
422
Canonical
GIFFCVRCRHRRRQA
[1][2][3]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Fragoso R, Ren D, Zhang X, Su MW, Burakoff SJ, Jin YJ. Lipid raft distributionof CD4 depends on its palmitoylation and association with Lck, and evidence forCD4-induced lipid raft aggregation as an additional mechanism to enhance CD3signaling. J Immunol. 2003 Jan 15;170(2):913-21.[PMID:12517957]
[2] Popik W, Alce TM. CD4 receptor localized to non-raft membrane microdomainssupports HIV-1 entry. Identification of a novel raft localization marker in CD4. J Biol Chem. 2004 Jan 2;279(1):704-12. Epub 2003 Oct 21.[PMID:14570906]
[3] Sol-Foulon N, Esnault C, Percherancier Y, Porrot F, Metais-Cunha P, BachelerieF, Schwartz O. The effects of HIV-1 Nef on CD4 surface expression and viralinfectivity in lymphoid cells are independent of rafts. J Biol Chem. 2004 Jul23;279(30):31398-408. Epub 2004 May 7.[PMID:15133044]
Functional Description
Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation. Induces the aggregation of lipid rafts.
Sequence Annotation
Topological domain: 26 396 Extracellular.
Transmembrane: 397 418 Helical.
Topological domain: 419 458 Cytoplasmic.
Domain: 26 125 Ig-like V-type.
Domain: 126 203 Ig-like C2-type 1.
Domain: 204 317 Ig-like C2-type 2.
Domain: 318 374 Ig-like C2-type 3.
Region: 427 455 HIV-1 Vpu-susceptibility domain.
Protein Length
458 AA.
Protein Sequence
(Canonical)
MNRGVPFRHL LLVLQLALLP AATQGKKVVL GKKGDTVELT CTASQKKSIQ FHWKNSNQIK  60
ILGNQGSFLT KGPSKLNDRA DSRRSLWDQG NFPLIIKNLK IEDSDTYICE VEDQKEEVQL  120
LVFGLTANSD THLLQGQSLT LTLESPPGSS PSVQCRSPRG KNIQGGKTLS VSQLELQDSG  180
TWTCTVLQNQ KKVEFKIDIV VLAFQKASSI VYKKEGEQVE FSFPLAFTVE KLTGSGELWW  240
QAERASSSKS WITFDLKNKE VSVKRVTQDP KLQMGKKLPL HLTLPQALPQ YAGSGNLTLA  300
LEAKTGKLHQ EVNLVVMRAT QLQKNLTCEV WGPTSPKLML SLKLENKEAK VSKREKAVWV  360
LNPEAGMWQC LLSDSGQVLL ESNIKVLPTW STPVQPMALI VLGGVAGLLL FIGLGIFFCV  420
RCRHRRRQAE RMSQIKRLLS EKKTCQCPHR FQKTCSPI                          458
FASTA
(Canonical)
>LipidDB-9606-01443|P01730
MNRGVPFRHLLLVLQLALLPAATQGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIK
ILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQL
LVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSG
TWTCTVLQNQKKVEFKIDIVVLAFQKASSIVYKKEGEQVEFSFPLAFTVEKLTGSGELWW
QAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLA
LEAKTGKLHQEVNLVVMRATQLQKNLTCEVWGPTSPKLMLSLKLENKEAKVSKREKAVWV
LNPEAGMWQCLLSDSGQVLLESNIKVLPTWSTPVQPMALIVLGGVAGLLLFIGLGIFFCV
RCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI
Gene Ontology
GO:0005769; C:early endosome; TAS:Reactome
GO:0005788; C:endoplasmic reticulum lumen; IEA:Ensembl
GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome
GO:0009897; C:external side of plasma membrane; IDA:MGI
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0045121; C:membrane raft; IEA:Ensembl
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0042101; C:T cell receptor complex; NAS:UniProtKB
GO:0015026; F:coreceptor activity; NAS:UniProtKB
GO:0019899; F:enzyme binding; IPI:UniProtKB
GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB
GO:0001948; F:glycoprotein binding; IPI:UniProtKB
GO:0042289; F:MHC class II protein binding; NAS:UniProtKB
GO:0042803; F:protein homodimerization activity; IDA:UniProtKB
GO:0019901; F:protein kinase binding; IPI:UniProtKB
GO:0004872; F:receptor activity; TAS:ProtInc
GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc
GO:0008270; F:zinc ion binding; IDA:UniProtKB
GO:0007155; P:cell adhesion; IEA:InterPro
GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc
GO:0001816; P:cytokine production; IEA:Ensembl
GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl
GO:0030260; P:entry into host cell; TAS:Reactome
GO:0007167; P:enzyme linked receptor protein signaling pathway; TAS:ProtInc
GO:0006955; P:immune response; NAS:UniProtKB
GO:0006948; P:induction by virus of host cell-cell fusion; IDA:UniProtKB
GO:0045087; P:innate immune response; TAS:Reactome
GO:0032507; P:maintenance of protein location in cell; IDA:MGI
GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl
GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; NAS:UniProtKB
GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl
GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB
GO:0045234; P:protein palmitoleylation; IDA:MGI
GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome
GO:0050863; P:regulation of T cell activation; IDA:UniProtKB
GO:0007165; P:signal transduction; TAS:ProtInc
GO:0031295; P:T cell costimulation; TAS:Reactome
GO:0030217; P:T cell differentiation; IDA:UniProtKB
GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome
GO:0045058; P:T cell selection; IDA:UniProtKB
GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; NAS:UniProtKB
GO:0016032; P:viral process; TAS:Reactome
Interpro
InterPro; IPR000973; CD4
InterPro; IPR015274; CD4-extracel
InterPro; IPR007110; Ig-like_dom
InterPro; IPR013783; Ig-like_fold
InterPro; IPR008424; Ig_C2-set
InterPro; IPR003599; Ig_sub
InterPro; IPR013106; Ig_V-set
InterPro; IPR003596; Ig_V-set_subgr
InterPro; IPR021963; Tcell_CD4_Cterm
Pfam
Pfam; PF05790; C2-set;
Pfam; PF09191; CD4-extracel;
Pfam; PF12104; Tcell_CD4_Cterm;
Pfam; PF07686; V-set;
SMART
SMART; SM00409; IG;
SMART; SM00406; IGv;
PROSITE
PROSITE; PS50835; IG_LIKE;
PRINTS
PRINTS; PR00692; CD4TCANTIGEN;