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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)DescriptionActionsGraphical viewLength
Topological domaini23 – 202ExtracellularSequence analysisAdd BLAST180
Transmembranei203 – 228HelicalSequence analysisAdd BLAST26
Topological domaini229 – 344CytoplasmicSequence analysisAdd BLAST116

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Add BLAST22
ChainiPRO_000001460323 – 344T-cell surface antigen CD2Add BLAST322

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi99N-linked (GlcNAc...)Sequence analysis1
Glycosylationi106N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi132 ↔ 196Combined sources1 Publication
Glycosylationi134N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi139 ↔ 179Combined sources1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP08921.
PRIDEiP08921.

PTM databases

iPTMnetiP08921.
PhosphoSitePlusiP08921.

Interactioni

Subunit structurei

Interacts with CD2AP and PSTPIP1.By similarity

GO - Molecular functioni

  • 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

1344
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 31Combined sources5
Beta strandi36 – 38Combined sources3
Beta strandi49 – 56Combined sources8
Beta strandi59 – 66Combined sources8
Beta strandi71 – 74Combined sources4
Beta strandi77 – 79Combined sources3
Beta strandi85 – 89Combined sources5
Helixi92 – 94Combined sources3
Beta strandi96 – 104Combined sources9
Beta strandi109 – 120Combined sources12
Beta strandi127 – 131Combined sources5
Turni132 – 135Combined sources4
Beta strandi136 – 140Combined sources5
Beta strandi148 – 153Combined sources6
Beta strandi156 – 169Combined sources14
Beta strandi177 – 183Combined sources7
Beta strandi186 – 192Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08921.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 121Ig-like V-typeAdd BLAST99
Domaini122 – 202Ig-like C2-typeAdd BLAST81

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi277 – 343Pro-richSequence analysisAdd BLAST67

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1514111.
STRINGi10116.ENSRNOP00000021268.

PTM databases

iPTMnetiP08921.
PhosphoSitePlusiP08921.

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...

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: November 2, 2016
This is version 147 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.