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P07725 (CD8A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
T-cell surface glycoprotein CD8 alpha chain
Alternative name(s):
CD8 antigen 32 kDa chain
OX-8 membrane antigen
CD_antigen=CD8a
Gene names
Name:Cd8a
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Identifies cytotoxic/suppressor T-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of T-cell mediated killing. CD8 alpha chains binds to class I MHC molecules alpha-3 domains.

Subunit structure

In general heterodimer of an alpha and a beta chain linked by two disulfide bonds. Can also form homodimers.

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 236210T-cell surface glycoprotein CD8 alpha chain
PRO_0000014641

Regions

Topological domain27 – 189163Extracellular Potential
Transmembrane190 – 21021Helical; Potential
Topological domain211 – 23626Cytoplasmic Potential
Domain27 – 130104Ig-like V-type

Amino acid modifications

Glycosylation631N-linked (GlcNAc...) Probable
Glycosylation1441O-linked (GalNAc...); partial Ref.3
Glycosylation1481O-linked (GalNAc...) Ref.3
Glycosylation1521O-linked (GalNAc...) Ref.3
Glycosylation1581O-linked (GalNAc...) Ref.3
Glycosylation1601O-linked (GalNAc...) Ref.3
Disulfide bond47 ↔ 119 Potential

Sequences

Sequence LengthMass (Da)Tools
P07725 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: ADFAC54E4C99C1BE

FASTA23626,196
        10         20         30         40         50         60 
MASRVICFLS LNLLLLDVIT RLQVSGQLQL SPKKVDAEIG QEVKLTCEVL RDTSQGCSWL 

        70         80         90        100        110        120 
FRNSSSELLQ PTFIIYVSSS RSKLNDILDP NLFSARKENN KYILTLSKFS TKNQGYYFCS 

       130        140        150        160        170        180 
ITSNSVMYFS PLVPVFQKVN SIITKPVTRA PTPVPPPTGT PRPLRPEACR PGASGSVEGM 

       190        200        210        220        230 
GLGFACDIYI WAPLAGICAV LLLSLVITLI CCHRNRRRVC KCPRPLVKPR PSEKFV 

« Hide

References

« Hide 'large scale' references
[1]"Purification, chain separation and sequence of the MRC OX-8 antigen, a marker of rat cytotoxic T lymphocytes."
Johnson P., Gagnon J., Barclay A.N., Williams A.F.
EMBO J. 4:2539-2545(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
[3]"Glycosylation sites identified by detection of glycosylated amino acids released from Edman degradation: the identification of Xaa-Pro-Xaa-Xaa as a motif for Thr-O-glycosylation."
Gooley A.A., Classon B.J., Marschalek R., Williams K.L.
Biochem. Biophys. Res. Commun. 178:1194-1200(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-63; THR-144; THR-148; THR-152; THR-158 AND THR-160.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03015 mRNA. Translation: CAA26798.1.
BC088126 mRNA. Translation: AAH88126.1.
IPIIPI00210541.
PIRA24637.
RefSeqNP_113726.1. NM_031538.2.
UniGeneRn.10306.

3D structure databases

ProteinModelPortalP07725.
SMRP07725. Positions 27-140.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000009516.

PTM databases

PhosphoSiteP07725.

Proteomic databases

PRIDEP07725.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000009515; ENSRNOP00000009516; ENSRNOG00000007178.
GeneID24930.
KEGGrno:24930.
UCSCRGD:2316. rat.

Organism-specific databases

CTD925.
RGD2316. Cd8a.

Phylogenomic databases

eggNOGNOG46810.
GeneTreeENSGT00510000048935.
HOGENOMHOG000004794.
HOVERGENHBG008488.
InParanoidP07725.
KOK06458.
OrthoDBEOG4JDH84.

Gene expression databases

GenevestigatorP07725.
GermOnlineENSRNOG00000007178. Rattus norvegicus.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR015468. CD8_asu.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
[Graphical view]
PANTHERPTHR10441. PTHR10441. 1 hit.
PfamPF00047. ig. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604895.

Entry information

Entry nameCD8A_RAT
AccessionPrimary (citable) accession number: P07725
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 3, 2013
This is version 114 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