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Protein

T-cell surface antigen CD2

Gene

Cd2

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

Functioni

CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.

GO - Molecular functioni

  • antigen binding Source: RGD
  • glycoprotein binding Source: RGD
  • protein homodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • protein self-association Source: RGD
  • receptor tyrosine kinase binding Source: RGD

GO - Biological processi

  • single organismal cell-cell adhesion Source: RGD
  • T cell activation Source: RGD
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
T-cell surface antigen CD2
Alternative name(s):
LFA-2
LFA-3 receptor
OX-34 antigen
T-cell surface antigen T11/Leu-5
CD_antigen: CD2
Gene namesi
Name:Cd2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2297. Cd2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 202180ExtracellularSequence analysisAdd
BLAST
Transmembranei203 – 22826HelicalSequence analysisAdd
BLAST
Topological domaini229 – 344116CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • membrane raft Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Chaini23 – 344322T-cell surface antigen CD2PRO_0000014603Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence analysis
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence analysis
Disulfide bondi132 ↔ 196Combined sources1 Publication
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence analysis
Disulfide bondi139 ↔ 179Combined sources1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP08921.
PRIDEiP08921.

PTM databases

iPTMnetiP08921.
PhosphoSiteiP08921.

Interactioni

Subunit structurei

Interacts with CD2AP and PSTPIP1.By similarity

GO - Molecular functioni

  • glycoprotein binding Source: RGD
  • protein homodimerization activity Source: RGD
  • protein kinase binding Source: RGD
  • protein self-association Source: RGD
  • receptor tyrosine kinase binding Source: RGD

Protein-protein interaction databases

MINTiMINT-1514111.
STRINGi10116.ENSRNOP00000021268.

Structurei

Secondary structure

1
344
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 315Combined sources
Beta strandi36 – 383Combined sources
Beta strandi49 – 568Combined sources
Beta strandi59 – 668Combined sources
Beta strandi71 – 744Combined sources
Beta strandi77 – 793Combined sources
Beta strandi85 – 895Combined sources
Helixi92 – 943Combined sources
Beta strandi96 – 1049Combined sources
Beta strandi109 – 12012Combined sources
Beta strandi127 – 1315Combined sources
Turni132 – 1354Combined sources
Beta strandi136 – 1405Combined sources
Beta strandi148 – 1536Combined sources
Beta strandi156 – 16914Combined sources
Beta strandi177 – 1837Combined sources
Beta strandi186 – 1927Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A64X-ray2.00A/B23-121[»]
1A6PX-ray2.08A/B26-121[»]
1A7BX-ray3.10A/B/C/D23-121[»]
1CDCX-ray2.00A/B23-121[»]
1HNGX-ray2.80A/B23-198[»]
1T6WNMR-A23-121[»]
ProteinModelPortaliP08921.
SMRiP08921. Positions 24-198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08921.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 12199Ig-like V-typeAdd
BLAST
Domaini122 – 20281Ig-like C2-typeAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi277 – 34367Pro-richSequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IW98. Eukaryota.
ENOG410Y7BE. LUCA.
HOGENOMiHOG000276890.
HOVERGENiHBG000262.
InParanoidiP08921.
KOiK06449.
PhylomeDBiP08921.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR015632. CD2.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF05790. C2-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01870. CD2ANTIGEN.
SUPFAMiSSF48726. SSF48726. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P08921-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRCKFLGSFF LLFSLSSKGA DCRDSGTVWG ALGHGINLNI PNFQMTDDID
60 70 80 90 100
EVRWERGSTL VAEFKRKMKP FLKSGAFEIL ANGDLKIKNL TRDDSGTYNV
110 120 130 140 150
TVYSTNGTRI LDKALDLRIL EMVSKPMIYW ECSNATLTCE VLEGTDVELK
160 170 180 190 200
LYQGKEHLRS LRQKTMSYQW TNLRAPFKCK AVNRVSQESE MEVVNCPEKG
210 220 230 240 250
LPLYLIVGVS AGGLLLVFFG ALFIFCICKR KKRNRRRKGE ELEIKASRMS
260 270 280 290 300
TVERGPKPHS TQASAPASQN PVASQAPPPP GHHLQTPGHR PLPPSHRNRE
310 320 330 340
HQPKKRPPPS GTQVHQQKGP PLPRPRVQPK PPCGSGDVSL PPPN
Length:344
Mass (Da):38,414
Last modified:November 1, 1988 - v1
Checksum:i41BAED392CE16356
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05111 mRNA. Translation: CAA28757.1.
PIRiA33071. RWRTC2.
RefSeqiNP_036962.1. NM_012830.1.
UniGeneiRn.10328.

Genome annotation databases

GeneIDi497761.
KEGGirno:497761.
UCSCiRGD:2297. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05111 mRNA. Translation: CAA28757.1.
PIRiA33071. RWRTC2.
RefSeqiNP_036962.1. NM_012830.1.
UniGeneiRn.10328.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A64X-ray2.00A/B23-121[»]
1A6PX-ray2.08A/B26-121[»]
1A7BX-ray3.10A/B/C/D23-121[»]
1CDCX-ray2.00A/B23-121[»]
1HNGX-ray2.80A/B23-198[»]
1T6WNMR-A23-121[»]
ProteinModelPortaliP08921.
SMRiP08921. Positions 24-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1514111.
STRINGi10116.ENSRNOP00000021268.

PTM databases

iPTMnetiP08921.
PhosphoSiteiP08921.

Proteomic databases

PaxDbiP08921.
PRIDEiP08921.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi497761.
KEGGirno:497761.
UCSCiRGD:2297. rat.

Organism-specific databases

CTDi914.
RGDi2297. Cd2.

Phylogenomic databases

eggNOGiENOG410IW98. Eukaryota.
ENOG410Y7BE. LUCA.
HOGENOMiHOG000276890.
HOVERGENiHBG000262.
InParanoidiP08921.
KOiK06449.
PhylomeDBiP08921.

Miscellaneous databases

EvolutionaryTraceiP08921.
PROiP08921.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR015632. CD2.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR013106. Ig_V-set.
[Graphical view]
PfamiPF05790. C2-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01870. CD2ANTIGEN.
SUPFAMiSSF48726. SSF48726. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Similarities in sequences and cellular expression between rat CD2 and CD4 antigens."
    Williams A.F., Barclay A.N., Clark S.J., Paterson D.J., Willis A.C.
    J. Exp. Med. 165:368-380(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-344, PARTIAL PROTEIN SEQUENCE.
    Strain: AO.
  2. Barclay A.N., Williams A.F.
    Submitted (MAY-1987) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: AO.
  3. "A role in transmembrane signaling for the cytoplasmic domain of the CD2 T lymphocyte surface antigen."
    He Q., Beyers A.D., Barclay A.N., Williams A.F.
    Cell 54:979-984(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: IMPORTANCE OF C-TERMINAL IN SIGNALING.
  4. "Crystal structure at 2.8-A resolution of a soluble form of the cell adhesion molecule CD2."
    Jones E.Y., Davis S.J., Williams A.F., Harlos K., Stuart D.I.
    Nature 360:232-239(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-198, DISULFIDE BONDS.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-121.
  6. "Engineering an intertwined form of CD2 for stability and assembly."
    Murray A.J., Head J.G., Barker J.J., Brady R.L.
    Nat. Struct. Biol. 5:778-782(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-121.
  7. "Structure of domain 1 of rat T lymphocyte CD2 antigen."
    Driscoll P.C., Cyster J.G., Campbell I.D., Williams A.F.
    Nature 353:762-765(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 23-121.

Entry informationi

Entry nameiCD2_RAT
AccessioniPrimary (citable) accession number: P08921
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: June 8, 2016
This is version 145 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

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 one 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.