T-cell surface glycoprotein CD4 precursor

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P05540 (CD4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Adaptive immunity Immunity
Cellular component	Membrane
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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: Compara cytokine production Inferred from electronic annotation. Source: Compara defense response to Gram-negative bacterium Inferred from electronic annotation. Source: Compara immune response Inferred from electronic annotation. Source: InterPro induction by virus of host cell-cell fusion Inferred from electronic annotation. Source: Compara maintenance of protein location in cell Inferred from electronic annotation. Source: Compara positive regulation of T cell activation Inferred from electronic annotation. Source: Compara positive regulation of calcium-mediated signaling Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of protein kinase activity Inferred from electronic annotation. Source: Compara protein palmitoleylation Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: Compara endoplasmic reticulum membrane Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane raft Inferred from electronic annotation. Source: Compara
Molecular_function	zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

Chain

28 – 457

430

T-cell surface glycoprotein CD4

PRO_0000014629

Regions

Topological domain

28 – 394

367

Extracellular Potential

Transmembrane

395 – 417

Helical; Potential

Topological domain

418 – 457

Cytoplasmic Potential

Domain

28 – 127

100

Ig-like V-type

Domain

128 – 206

Ig-like C2-type 1

Domain

207 – 316

110

Ig-like C2-type 2

Domain

317 – 374

Ig-like C2-type 3

Amino acid modifications

Lipidation

418

S-palmitoyl cysteine By similarity

Lipidation

421

S-palmitoyl cysteine By similarity

Glycosylation

186

N-linked (GlcNAc...) Ref.2

Glycosylation

297

N-linked (GlcNAc...) Ref.2

Glycosylation

392

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Experimental info

Mutagenesis

186

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

Mutagenesis

297

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

Secondary structure

457

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P05540 [UniParc].

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

FASTA

457

51,438

        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.

IPI

IPI00200583.

PIR

A27449.

RefSeq

NP_036837.1. NM_012705.1.

UniGene

Rn.10748.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CID	X-ray	2.80	A	210-386	[»]

ProteinModelPortal

P05540.

SMR

P05540. Positions 210-386, 420-453.

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000021915.

PTM databases

GlycoSuiteDB

P05540.

Proteomic databases

PRIDE

P05540.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000021915; ENSRNOP00000021915; ENSRNOG00000016294.

GeneID

24932.

KEGG

rno:24932.

UCSC

RGD:2306. rat.

Organism-specific databases

CTD

920.

RGD

2306. Cd4.

Phylogenomic databases

eggNOG

NOG47205.

GeneTree

ENSGT00390000001745.

HOGENOM

HOG000008696.

HOVERGEN

HBG005281.

InParanoid

P05540.

K06454.

OMA

CEVWGPT.

OrthoDB

EOG4NVZM4.

Gene expression databases

Genevestigator

P05540.

GermOnline

ENSRNOG00000016294. Rattus norvegicus.

Family and domain databases

Gene3D

2.60.40.10. 4 hits.

InterPro

IPR000973. 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]

Pfam

PF05790. C2-set. 2 hits.
PF09191. CD4-extracel. 1 hit.
PF12104. Tcell_CD4_Cterm. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]

PRINTS

PR00692. CD4TCANTIGEN.

SMART

SM00409. IG. 2 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P05540.

NextBio

604903.

Entry information

Entry name

CD4_RAT

Accession

Primary (citable) accession number: P05540

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	April 3, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents