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Protein

T-cell surface glycoprotein CD4

Gene

Cd4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • coreceptor activity Source: InterPro
  • protein kinase binding Source: RGD
  • zinc ion binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiREACT_274291. Generation of second messenger molecules.
REACT_281751. Translocation of ZAP-70 to Immunological synapse.
REACT_316530. Phosphorylation of CD3 and TCR zeta chains.
REACT_329159. Alpha-defensins.
REACT_342970. Downstream TCR signaling.
REACT_352796. PD-1 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
T-cell surface glycoprotein CD4
Alternative name(s):
T-cell surface antigen T4/Leu-3
W3/25 antigen
CD_antigen: CD4
Gene namesi
Name:Cd4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi2306. Cd4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 394367ExtracellularSequence AnalysisAdd
BLAST
Transmembranei395 – 41723HelicalSequence AnalysisAdd
BLAST
Topological domaini418 – 45740CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi186 – 1861N → T: No change in secretion; when associated with S-297. 1 Publication
Mutagenesisi297 – 2971N → S: No change in secretion; when associated with T-186. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Add
BLAST
Chaini28 – 457430T-cell surface glycoprotein CD4PRO_0000014629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 111PROSITE-ProRule annotation1 Publication
Disulfide bondi158 ↔ 187PROSITE-ProRule annotation1 Publication
Glycosylationi186 – 1861N-linked (GlcNAc...)1 Publication
Glycosylationi297 – 2971N-linked (GlcNAc...)1 Publication
Disulfide bondi328 ↔ 370PROSITE-ProRule annotation1 Publication
Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence Analysis
Lipidationi418 – 4181S-palmitoyl cysteineBy similarity
Lipidationi421 – 4211S-palmitoyl cysteineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PRIDEiP05540.

PTM databases

UniCarbKBiP05540.

Expressioni

Gene expression databases

GenevisibleiP05540. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi247037. 1 interaction.
MINTiMINT-4996350.
STRINGi10116.ENSRNOP00000021915.

Structurei

Secondary structure

1
457
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi213 – 2175Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi235 – 24511Combined sources
Beta strandi252 – 2587Combined sources
Beta strandi261 – 2666Combined sources
Beta strandi282 – 2854Combined sources
Helixi290 – 2923Combined sources
Beta strandi294 – 3018Combined sources
Beta strandi303 – 31917Combined sources
Beta strandi321 – 33212Combined sources
Beta strandi336 – 3449Combined sources
Beta strandi349 – 36214Combined sources
Beta strandi365 – 37410Combined sources
Beta strandi377 – 3859Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CIDX-ray2.80A210-386[»]
ProteinModelPortaliP05540.
SMRiP05540. Positions 210-386, 420-453.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05540.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 127100Ig-like V-typeAdd
BLAST
Domaini128 – 20679Ig-like C2-type 1Add
BLAST
Domaini207 – 316110Ig-like C2-type 2Add
BLAST
Domaini317 – 37458Ig-like C2-type 3Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47205.
GeneTreeiENSGT00390000001745.
HOGENOMiHOG000008696.
HOVERGENiHBG005281.
InParanoidiP05540.
KOiK06454.
OMAiPEAGMWQ.
OrthoDBiEOG7HXCQS.
PhylomeDBiP05540.
TreeFamiTF335974.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR000973. 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]
PfamiPF05790. C2-set. 2 hits.
PF09191. CD4-extracel. 1 hit.
PF12104. Tcell_CD4_Cterm. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR00692. CD4TCANTIGEN.
SMARTiSM00409. IG. 2 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05540-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCRGFSFRHL LPLLLLQLSK LLVVTQGKTV VLGKEGGSAE LPCESTSRRS
60 70 80 90 100
ASFAWKSSDQ KTILGYKNKL LIKGSLELYS RFDSRKNAWE RGSFPLIINK
110 120 130 140 150
LRMEDSQTYV CELENKKEEV ELWVFRVTFN PGTRLLQGQS LTLILDSNPK
160 170 180 190 200
VSDPPIECKH KSSNIVKDSK AFSTHSLRIQ DSGIWNCTVT LNQKKHSFDM
210 220 230 240 250
KLSVLGFAST SITAYKSEGE SAEFSFPLNL GEESLQGELR WKAEKAPSSQ
260 270 280 290 300
SWITFSLKNQ KVSVQKSTSN PKFQLSETLP LTLQIPQVSL QFAGSGNLTL
310 320 330 340 350
TLDRGILYQE VNLVVMKVTQ PDSNTLTCEV MGPTSPKMRL ILKQENQEAR
360 370 380 390 400
VSRQEKVIQV QAPEAGVWQC LLSEGEEVKM DSKIQVLSKG LNQTMFLAVV
410 420 430 440 450
LGSAFSFLVF TGLCILFCVR CRHQQRQAAR MSQIKRLLSE KKTCQCSHRM

QKSHNLI
Length:457
Mass (Da):51,438
Last modified:November 1, 1988 - v1
Checksum:i477BE157D30954C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15768 mRNA. Translation: AAA40901.1.
PIRiA27449.
RefSeqiNP_036837.1. NM_012705.1.
XP_006237393.1. XM_006237331.2.
XP_008761502.1. XM_008763280.1.
UniGeneiRn.10748.

Genome annotation databases

EnsembliENSRNOT00000021915; ENSRNOP00000021915; ENSRNOG00000016294.
GeneIDi24932.
KEGGirno:24932.
UCSCiRGD:2306. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15768 mRNA. Translation: AAA40901.1.
PIRiA27449.
RefSeqiNP_036837.1. NM_012705.1.
XP_006237393.1. XM_006237331.2.
XP_008761502.1. XM_008763280.1.
UniGeneiRn.10748.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CIDX-ray2.80A210-386[»]
ProteinModelPortaliP05540.
SMRiP05540. Positions 210-386, 420-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247037. 1 interaction.
MINTiMINT-4996350.
STRINGi10116.ENSRNOP00000021915.

PTM databases

UniCarbKBiP05540.

Proteomic databases

PRIDEiP05540.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021915; ENSRNOP00000021915; ENSRNOG00000016294.
GeneIDi24932.
KEGGirno:24932.
UCSCiRGD:2306. rat.

Organism-specific databases

CTDi920.
RGDi2306. Cd4.

Phylogenomic databases

eggNOGiNOG47205.
GeneTreeiENSGT00390000001745.
HOGENOMiHOG000008696.
HOVERGENiHBG005281.
InParanoidiP05540.
KOiK06454.
OMAiPEAGMWQ.
OrthoDBiEOG7HXCQS.
PhylomeDBiP05540.
TreeFamiTF335974.

Enzyme and pathway databases

ReactomeiREACT_274291. Generation of second messenger molecules.
REACT_281751. Translocation of ZAP-70 to Immunological synapse.
REACT_316530. Phosphorylation of CD3 and TCR zeta chains.
REACT_329159. Alpha-defensins.
REACT_342970. Downstream TCR signaling.
REACT_352796. PD-1 signaling.

Miscellaneous databases

EvolutionaryTraceiP05540.
NextBioi604903.
PROiP05540.

Gene expression databases

GenevisibleiP05540. RN.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR000973. 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]
PfamiPF05790. C2-set. 2 hits.
PF09191. CD4-extracel. 1 hit.
PF12104. Tcell_CD4_Cterm. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR00692. CD4TCANTIGEN.
SMARTiSM00409. IG. 2 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCD4_RAT
AccessioniPrimary (citable) accession number: P05540
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: June 24, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.