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T-cell surface antigen CD2 (LFA-2) (LFA-3 receptor) (OX-34 antigen) (T-cell surface antigen T11/Leu-5) (CD antigen CD2)

 CD2_RAT                 Reviewed;         344 AA.
P08921;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
25-OCT-2017, entry version 151.
RecName: Full=T-cell surface antigen CD2;
AltName: Full=LFA-2;
AltName: Full=LFA-3 receptor;
AltName: Full=OX-34 antigen;
AltName: Full=T-cell surface antigen T11/Leu-5;
AltName: CD_antigen=CD2;
Flags: Precursor;
Name=Cd2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 42-344, AND PARTIAL PROTEIN SEQUENCE.
STRAIN=AO;
PubMed=3102667; DOI=10.1084/jem.165.2.368;
Williams A.F., Barclay A.N., Clark S.J., Paterson D.J., Willis A.C.;
"Similarities in sequences and cellular expression between rat CD2 and
CD4 antigens.";
J. Exp. Med. 165:368-380(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=AO;
Barclay A.N., Williams A.F.;
Submitted (MAY-1987) to the EMBL/GenBank/DDBJ databases.
[3]
IMPORTANCE OF C-TERMINAL IN SIGNALING.
PubMed=2901293; DOI=10.1016/0092-8674(88)90112-2;
He Q., Beyers A.D., Barclay A.N., Williams A.F.;
"A role in transmembrane signaling for the cytoplasmic domain of the
CD2 T lymphocyte surface antigen.";
Cell 54:979-984(1988).
[4]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-198, AND DISULFIDE BONDS.
PubMed=1279440; DOI=10.1038/360232a0;
Jones E.Y., Davis S.J., Williams A.F., Harlos K., Stuart D.I.;
"Crystal structure at 2.8-A resolution of a soluble form of the cell
adhesion molecule CD2.";
Nature 360:232-239(1992).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-121.
PubMed=7638192; DOI=10.1073/pnas.92.16.7337;
Murray A.J., Lewis S.J., Barclay A.N., Brady R.L.;
"One sequence, two folds: a metastable structure of CD2.";
Proc. Natl. Acad. Sci. U.S.A. 92:7337-7341(1995).
[6]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-121.
PubMed=9731771; DOI=10.1038/1816;
Murray A.J., Head J.G., Barker J.J., Brady R.L.;
"Engineering an intertwined form of CD2 for stability and assembly.";
Nat. Struct. Biol. 5:778-782(1998).
[7]
STRUCTURE BY NMR OF 23-121.
PubMed=1682812; DOI=10.1038/353762a0;
Driscoll P.C., Cyster J.G., Campbell I.D., Williams A.F.;
"Structure of domain 1 of rat T lymphocyte CD2 antigen.";
Nature 353:762-765(1991).
-!- FUNCTION: 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.
-!- SUBUNIT: Interacts with CD2AP and PSTPIP1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-----------------------------------------------------------------------
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EMBL; X05111; CAA28757.1; -; mRNA.
PIR; A33071; RWRTC2.
RefSeq; NP_036962.1; NM_012830.1.
UniGene; Rn.10328; -.
PDB; 1A64; X-ray; 2.00 A; A/B=23-121.
PDB; 1A6P; X-ray; 2.08 A; A/B=26-121.
PDB; 1A7B; X-ray; 3.10 A; A/B/C/D=23-121.
PDB; 1CDC; X-ray; 2.00 A; A/B=23-121.
PDB; 1HNG; X-ray; 2.80 A; A/B=23-198.
PDB; 1T6W; NMR; -; A=23-121.
PDBsum; 1A64; -.
PDBsum; 1A6P; -.
PDBsum; 1A7B; -.
PDBsum; 1CDC; -.
PDBsum; 1HNG; -.
PDBsum; 1T6W; -.
ProteinModelPortal; P08921; -.
SMR; P08921; -.
MINT; MINT-1514111; -.
STRING; 10116.ENSRNOP00000021268; -.
iPTMnet; P08921; -.
PhosphoSitePlus; P08921; -.
PaxDb; P08921; -.
PRIDE; P08921; -.
GeneID; 497761; -.
KEGG; rno:497761; -.
UCSC; RGD:2297; rat.
CTD; 914; -.
RGD; 2297; Cd2.
eggNOG; ENOG410IW98; Eukaryota.
eggNOG; ENOG410Y7BE; LUCA.
HOGENOM; HOG000276890; -.
HOVERGEN; HBG000262; -.
InParanoid; P08921; -.
KO; K06449; -.
PhylomeDB; P08921; -.
EvolutionaryTrace; P08921; -.
PRO; PR:P08921; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0003823; F:antigen binding; IMP:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0043621; F:protein self-association; IDA:RGD.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD.
GO; GO:0098609; P:cell-cell adhesion; IMP:RGD.
GO; GO:0042110; P:T cell activation; IMP:RGD.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR015632; CD2.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR008424; Ig_C2-set.
InterPro; IPR013106; Ig_V-set.
Pfam; PF05790; C2-set; 1.
Pfam; PF07686; V-set; 1.
PRINTS; PR01870; CD2ANTIGEN.
SUPFAM; SSF48726; SSF48726; 2.
1: Evidence at protein level;
3D-structure; Cell adhesion; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 22
CHAIN 23 344 T-cell surface antigen CD2.
/FTId=PRO_0000014603.
TOPO_DOM 23 202 Extracellular. {ECO:0000255}.
TRANSMEM 203 228 Helical. {ECO:0000255}.
TOPO_DOM 229 344 Cytoplasmic. {ECO:0000255}.
DOMAIN 23 121 Ig-like V-type.
DOMAIN 122 202 Ig-like C2-type.
COMPBIAS 277 343 Pro-rich. {ECO:0000255}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 132 196 {ECO:0000244|PDB:1HNG,
ECO:0000269|PubMed:1279440}.
DISULFID 139 179 {ECO:0000244|PDB:1HNG,
ECO:0000269|PubMed:1279440}.
STRAND 27 31 {ECO:0000244|PDB:1A64}.
STRAND 36 38 {ECO:0000244|PDB:1A64}.
STRAND 49 56 {ECO:0000244|PDB:1A64}.
STRAND 59 66 {ECO:0000244|PDB:1A64}.
STRAND 71 74 {ECO:0000244|PDB:1A64}.
STRAND 77 79 {ECO:0000244|PDB:1A64}.
STRAND 85 89 {ECO:0000244|PDB:1A64}.
HELIX 92 94 {ECO:0000244|PDB:1A64}.
STRAND 96 104 {ECO:0000244|PDB:1A64}.
STRAND 109 120 {ECO:0000244|PDB:1A64}.
STRAND 127 131 {ECO:0000244|PDB:1HNG}.
TURN 132 135 {ECO:0000244|PDB:1HNG}.
STRAND 136 140 {ECO:0000244|PDB:1HNG}.
STRAND 148 153 {ECO:0000244|PDB:1HNG}.
STRAND 156 169 {ECO:0000244|PDB:1HNG}.
STRAND 177 183 {ECO:0000244|PDB:1HNG}.
STRAND 186 192 {ECO:0000244|PDB:1HNG}.
SEQUENCE 344 AA; 38414 MW; 41BAED392CE16356 CRC64;
MRCKFLGSFF LLFSLSSKGA DCRDSGTVWG ALGHGINLNI PNFQMTDDID EVRWERGSTL
VAEFKRKMKP FLKSGAFEIL ANGDLKIKNL TRDDSGTYNV TVYSTNGTRI LDKALDLRIL
EMVSKPMIYW ECSNATLTCE VLEGTDVELK LYQGKEHLRS LRQKTMSYQW TNLRAPFKCK
AVNRVSQESE MEVVNCPEKG LPLYLIVGVS AGGLLLVFFG ALFIFCICKR KKRNRRRKGE
ELEIKASRMS TVERGPKPHS TQASAPASQN PVASQAPPPP GHHLQTPGHR PLPPSHRNRE
HQPKKRPPPS GTQVHQQKGP PLPRPRVQPK PPCGSGDVSL PPPN


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