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P05540 (CD4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-cell surface glycoprotein CD4
Alternative name(s):
T-cell surface antigen T4/Leu-3
W3/25 antigen
CD_antigen=CD4
Gene names
Name:Cd4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation.

Subunit structure

Associates with p56-LCK. Interacts with SPG21 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
   Cellular componentMembrane
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell activation

Inferred from mutant phenotype PubMed 10458478. Source: RGD

T cell differentiation

Inferred from sequence or structural similarity PubMed 1533274. Source: UniProtKB

T cell selection

Inferred from sequence or structural similarity PubMed 9551897. Source: UniProtKB

cell adhesion

Inferred from electronic annotation. Source: InterPro

cell surface receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

cytokine production

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-negative bacterium

Inferred from electronic annotation. Source: Ensembl

immune response

Inferred from electronic annotation. Source: InterPro

induction by virus of host cell-cell fusion

Inferred from electronic annotation. Source: Ensembl

maintenance of protein location in cell

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell activation

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

protein palmitoleylation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane raft

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein kinase binding

Inferred from physical interaction PubMed 1372996. Source: RGD

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 457430T-cell surface glycoprotein CD4
PRO_0000014629

Regions

Topological domain28 – 394367Extracellular Potential
Transmembrane395 – 41723Helical; Potential
Topological domain418 – 45740Cytoplasmic Potential
Domain28 – 127100Ig-like V-type
Domain128 – 20679Ig-like C2-type 1
Domain207 – 316110Ig-like C2-type 2
Domain317 – 37458Ig-like C2-type 3

Amino acid modifications

Lipidation4181S-palmitoyl cysteine By similarity
Lipidation4211S-palmitoyl cysteine By similarity
Glycosylation1861N-linked (GlcNAc...) Ref.2
Glycosylation2971N-linked (GlcNAc...) Ref.2
Glycosylation3921N-linked (GlcNAc...) Potential
Disulfide bond43 ↔ 111 Ref.2
Disulfide bond158 ↔ 187 Ref.2
Disulfide bond328 ↔ 370 Ref.2

Experimental info

Mutagenesis1861N → T: No change in secretion; when associated with S-297. Ref.2
Mutagenesis2971N → S: No change in secretion; when associated with T-186. Ref.2

Secondary structure

............................. 457
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05540 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 477BE157D30954C1

FASTA45751,438
        10         20         30         40         50         60 
MCRGFSFRHL LPLLLLQLSK LLVVTQGKTV VLGKEGGSAE LPCESTSRRS ASFAWKSSDQ 

        70         80         90        100        110        120 
KTILGYKNKL LIKGSLELYS RFDSRKNAWE RGSFPLIINK LRMEDSQTYV CELENKKEEV 

       130        140        150        160        170        180 
ELWVFRVTFN PGTRLLQGQS LTLILDSNPK VSDPPIECKH KSSNIVKDSK AFSTHSLRIQ 

       190        200        210        220        230        240 
DSGIWNCTVT LNQKKHSFDM KLSVLGFAST SITAYKSEGE SAEFSFPLNL GEESLQGELR 

       250        260        270        280        290        300 
WKAEKAPSSQ SWITFSLKNQ KVSVQKSTSN PKFQLSETLP LTLQIPQVSL QFAGSGNLTL 

       310        320        330        340        350        360 
TLDRGILYQE VNLVVMKVTQ PDSNTLTCEV MGPTSPKMRL ILKQENQEAR VSRQEKVIQV 

       370        380        390        400        410        420 
QAPEAGVWQC LLSEGEEVKM DSKIQVLSKG LNQTMFLAVV LGSAFSFLVF TGLCILFCVR 

       430        440        450 
CRHQQRQAAR MSQIKRLLSE KKTCQCSHRM QKSHNLI 

« Hide

References

[1]"Peptide and nucleotide sequences of rat CD4 (W3/25) antigen: evidence for derivation from a structure with four immunoglobulin-related domains."
Clark S.J., Jefferies W.A., Barclay A.N., Gagnon J., Williams A.F.
Proc. Natl. Acad. Sci. U.S.A. 84:1649-1653(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"High level expression in Chinese hamster ovary cells of soluble forms of CD4 T lymphocyte glycoprotein including glycosylation variants."
Davis S.J., Ward H.A., Puklavec M.J., Willis A.C., Williams A.F., Barclay A.N.
J. Biol. Chem. 265:10410-10418(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 42-51; 83-88; 95-101; 109-112; 146-164; 178-192; 256-273; 292-300; 327-329 AND 368-371, DISULFIDE BONDS, GLYCOSYLATION AT ASN-186 AND ASN-297, MUTAGENESIS OF ASN-186 AND ASN-297.
[3]"Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains."
Brady R.L., Dodson E.J., Dodson G.G., Lange G., Davis S.J., Williams A.F., Barclay A.N.
Science 260:979-983(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 210-393.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15768 mRNA. Translation: AAA40901.1.
PIRA27449.
RefSeqNP_036837.1. NM_012705.1.
XP_006237393.1. XM_006237331.1.
UniGeneRn.10748.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CIDX-ray2.80A210-386[»]
ProteinModelPortalP05540.
SMRP05540. Positions 210-386, 420-453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247037. 1 interaction.
MINTMINT-4996350.
STRING10116.ENSRNOP00000021915.

PTM databases

UniCarbKBP05540.

Proteomic databases

PRIDEP05540.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000021915; ENSRNOP00000021915; ENSRNOG00000016294.
GeneID24932.
KEGGrno:24932.
UCSCRGD:2306. rat.

Organism-specific databases

CTD920.
RGD2306. Cd4.

Phylogenomic databases

eggNOGNOG47205.
GeneTreeENSGT00390000001745.
HOGENOMHOG000008696.
HOVERGENHBG005281.
InParanoidP05540.
KOK06454.
OMAWQCLLSD.
OrthoDBEOG7HXCQS.
PhylomeDBP05540.
TreeFamTF335974.

Gene expression databases

GenevestigatorP05540.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR000973. Ag_CD4.
IPR015274. CD4-extracel.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR021963. Tcell_CD4_Cterm.
[Graphical view]
PfamPF05790. C2-set. 2 hits.
PF09191. CD4-extracel. 1 hit.
PF12104. Tcell_CD4_Cterm. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSPR00692. CD4TCANTIGEN.
SMARTSM00409. IG. 2 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05540.
NextBio604903.
PROP05540.

Entry information

Entry nameCD4_RAT
AccessionPrimary (citable) accession number: P05540
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: April 16, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references