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

 CD2_HUMAN               Reviewed;         351 AA.
P06729; Q96TE5;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 2.
25-OCT-2017, entry version 197.
RecName: Full=T-cell surface antigen CD2;
AltName: Full=Erythrocyte receptor;
AltName: Full=LFA-2;
AltName: Full=LFA-3 receptor;
AltName: Full=Rosette receptor;
AltName: Full=T-cell surface antigen T11/Leu-5;
AltName: CD_antigen=CD2;
Flags: Precursor;
Name=CD2; Synonyms=SRBC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2894031; DOI=10.1073/pnas.85.5.1615;
Diamond D.J., Clayton L.K., Sayre P.H., Reinherz E.L.;
"Exon-intron organization and sequence comparison of human and murine
T11 (CD2) genes.";
Proc. Natl. Acad. Sci. U.S.A. 85:1615-1619(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-266.
PubMed=2437578; DOI=10.1073/pnas.84.10.3365;
Seed B., Aruffo A.;
"Molecular cloning of the CD2 antigen, the T-cell erythrocyte
receptor, by a rapid immunoselection procedure.";
Proc. Natl. Acad. Sci. U.S.A. 84:3365-3369(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3490670; DOI=10.1073/pnas.83.22.8718;
Sewell W.A., Brown M.H., Dunne J., Owen M.J., Crumpton M.J.;
"Molecular cloning of the human T-lymphocyte surface CD2 (T11)
antigen.";
Proc. Natl. Acad. Sci. U.S.A. 83:8718-8722(1986).
[4]
ERRATUM, AND SEQUENCE REVISION.
Sewell W.A., Brown M.H., Dunne J., Owen M.J., Crumpton M.J.;
Proc. Natl. Acad. Sci. U.S.A. 84:7256-7256(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2883656; DOI=10.1073/pnas.84.9.2941;
Sayre P.H., Chang H.-C., Hussey R.E., Brown N.R., Richardson N.E.,
Spagnoli G., Clayton L.K., Reinherz E.L.;
"Molecular cloning and expression of T11 cDNAs reveal a receptor-like
structure on human T lymphocytes.";
Proc. Natl. Acad. Sci. U.S.A. 84:2941-2945(1987).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-266.
PubMed=2901953;
Lang G., Wotton D., Owen M.J., Sewell W.A., Brown M.H., Mason D.Y.,
Crumpton M.J., Kioussis D.;
"The structure of the human CD2 gene and its expression in transgenic
mice.";
EMBO J. 7:1675-1682(1988).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-266.
TISSUE=Pancreas, and Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
MUTAGENESIS.
PubMed=2444890; DOI=10.1038/329842a0;
Peterson A., Seed B.;
"Monoclonal antibody and ligand binding sites of the T cell
erythrocyte receptor (CD2).";
Nature 329:842-846(1987).
[10]
CD59-BINDING DATA.
PubMed=1377404; DOI=10.1126/science.1377404;
Hahn W.C., Menu E., Bothwell A.L.M., Sims P.J., Bierer B.E.;
"Overlapping but nonidentical binding sites on CD2 for CD58 and a
second ligand CD59.";
Science 256:1805-1807(1992).
[11]
INTERACTION WITH PSTPIP1.
PubMed=9857189; DOI=10.1093/emboj/17.24.7320;
Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R.,
Sunder-Plassmann R., Reinherz E.L.;
"A cdc15-like adaptor protein (CD2BP1) interacts with the CD2
cytoplasmic domain and regulates CD2-triggered adhesion.";
EMBO J. 17:7320-7336(1998).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-206, AND DISULFIDE BONDS.
PubMed=7994575; DOI=10.1016/S0969-2126(94)00076-X;
Bodian D.L., Jones E.Y., Harlos K., Stuart D.I., Davis S.J.;
"Crystal structure of the extracellular region of the human cell
adhesion molecule CD2 at 2.5-A resolution.";
Structure 2:755-766(1994).
[13]
STRUCTURE BY NMR OF 25-129.
PubMed=7915183; DOI=10.1016/0969-2126(93)90009-6;
Withka J.M., Wyss D.F., Wagner G., Arulanandam A.R.N., Reinherz E.L.,
Recny M.A.;
"Structure of the glycosylated adhesion domain of human T lymphocyte
glycoprotein CD2.";
Structure 1:69-81(1993).
[14]
STRUCTURE BY NMR OF 25-129.
PubMed=7544493; DOI=10.1126/science.7544493;
Wyss D.F., Choi J.S., Li J., Knoppers M.H., Willis K.J.,
Arulanandam A.R., Smolyar A., Reinherz E.L., Wagner G.;
"Conformation and function of the N-linked glycan in the adhesion
domain of human CD2.";
Science 269:1273-1278(1995).
[15]
VARIANT [LARGE SCALE ANALYSIS] TYR-217.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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 (By similarity). Interacts with
PSTPIP1. {ECO:0000250, ECO:0000269|PubMed:9857189}.
-!- INTERACTION:
Q9Y5K6:CD2AP; NbExp=4; IntAct=EBI-3912464, EBI-298152;
O95400:CD2BP2; NbExp=3; IntAct=EBI-3912464, EBI-768015;
Q96B97:SH3KBP1; NbExp=3; IntAct=EBI-3912464, EBI-346595;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- WEB RESOURCE: Name=Wikipedia; Note=CD2 entry;
URL="https://en.wikipedia.org/wiki/CD2";
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EMBL; M19806; AAA53095.1; -; Genomic_DNA.
EMBL; M19798; AAA53095.1; JOINED; Genomic_DNA.
EMBL; M19800; AAA53095.1; JOINED; Genomic_DNA.
EMBL; M19802; AAA53095.1; JOINED; Genomic_DNA.
EMBL; M19804; AAA53095.1; JOINED; Genomic_DNA.
EMBL; M16445; AAA51738.1; -; mRNA.
EMBL; M14362; AAA35571.1; -; mRNA.
EMBL; M16336; AAA51946.1; -; mRNA.
EMBL; X07871; CAA30721.1; -; Genomic_DNA.
EMBL; X07872; CAA30721.1; JOINED; Genomic_DNA.
EMBL; X07873; CAA30721.1; JOINED; Genomic_DNA.
EMBL; X07874; CAA30721.1; JOINED; Genomic_DNA.
EMBL; AL135798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC033583; AAH33583.1; -; mRNA.
CCDS; CCDS889.1; -.
PIR; A28967; RWHUC2.
RefSeq; NP_001315538.1; NM_001328609.1.
RefSeq; NP_001758.2; NM_001767.4.
UniGene; Hs.523500; -.
PDB; 1CDB; NMR; -; A=25-129.
PDB; 1GYA; NMR; -; A=25-129.
PDB; 1HNF; X-ray; 2.50 A; A=25-206.
PDB; 1L2Z; NMR; -; B=294-304.
PDB; 1QA9; X-ray; 3.20 A; A/C=28-129.
PDB; 2J6O; X-ray; 2.22 A; C=324-333.
PDB; 2J7I; X-ray; 2.90 A; C/D=324-333.
PDBsum; 1CDB; -.
PDBsum; 1GYA; -.
PDBsum; 1HNF; -.
PDBsum; 1L2Z; -.
PDBsum; 1QA9; -.
PDBsum; 2J6O; -.
PDBsum; 2J7I; -.
ProteinModelPortal; P06729; -.
SMR; P06729; -.
BioGrid; 107352; 16.
ELM; P06729; -.
IntAct; P06729; 8.
MINT; MINT-99488; -.
STRING; 9606.ENSP00000358490; -.
BindingDB; P06729; -.
ChEMBL; CHEMBL2040; -.
DrugBank; DB00092; Alefacept.
iPTMnet; P06729; -.
PhosphoSitePlus; P06729; -.
UniCarbKB; P06729; -.
BioMuta; CD2; -.
DMDM; 160370002; -.
PaxDb; P06729; -.
PeptideAtlas; P06729; -.
PRIDE; P06729; -.
DNASU; 914; -.
Ensembl; ENST00000369478; ENSP00000358490; ENSG00000116824.
GeneID; 914; -.
KEGG; hsa:914; -.
CTD; 914; -.
DisGeNET; 914; -.
EuPathDB; HostDB:ENSG00000116824.4; -.
GeneCards; CD2; -.
H-InvDB; HIX0000931; -.
HGNC; HGNC:1639; CD2.
HPA; CAB002430; -.
HPA; HPA003883; -.
MIM; 186990; gene.
neXtProt; NX_P06729; -.
OpenTargets; ENSG00000116824; -.
PharmGKB; PA26198; -.
eggNOG; ENOG410IW98; Eukaryota.
eggNOG; ENOG410Y7BE; LUCA.
GeneTree; ENSGT00390000009232; -.
HOGENOM; HOG000276890; -.
HOVERGEN; HBG000262; -.
InParanoid; P06729; -.
KO; K06449; -.
OMA; GTQVHQQ; -.
OrthoDB; EOG091G0M7A; -.
PhylomeDB; P06729; -.
TreeFam; TF335971; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
SignaLink; P06729; -.
EvolutionaryTrace; P06729; -.
GeneWiki; CD2; -.
GenomeRNAi; 914; -.
PRO; PR:P06729; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116824; -.
CleanEx; HS_CD2; -.
ExpressionAtlas; P06729; baseline and differential.
Genevisible; P06729; HS.
GO; GO:0046658; C:anchored component of plasma membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005576; C:extracellular region; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0004872; F:receptor activity; NAS:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:UniProtKB.
GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
GO; GO:0034113; P:heterotypic cell-cell adhesion; IDA:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0001766; P:membrane raft polarization; TAS:UniProtKB.
GO; GO:0030101; P:natural killer cell activation; NAS:UniProtKB.
GO; GO:1902715; P:positive regulation of interferon-gamma secretion; IDA:UniProtKB.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IMP:UniProtKB.
GO; GO:0030887; P:positive regulation of myeloid dendritic cell activation; NAS:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
GO; GO:0045580; P:regulation of T cell differentiation; NAS:UniProtKB.
GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR015632; CD2.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
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; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 24
CHAIN 25 351 T-cell surface antigen CD2.
/FTId=PRO_0000014600.
TOPO_DOM 25 209 Extracellular. {ECO:0000255}.
TRANSMEM 210 235 Helical. {ECO:0000255}.
TOPO_DOM 236 351 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 128 Ig-like V-type.
DOMAIN 129 209 Ig-like C2-type.
REGION 61 75 LFA-3 (CD58) binding region 1.
REGION 106 120 LFA-3 (CD58) binding region 2.
COMPBIAS 282 338 Pro-rich.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 139 203 {ECO:0000269|PubMed:7994575}.
DISULFID 146 186 {ECO:0000269|PubMed:7994575}.
VARIANT 217 217 C -> Y (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035504.
VARIANT 266 266 H -> Q (in dbSNP:rs699738).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2437578,
ECO:0000269|PubMed:2901953}.
/FTId=VAR_017104.
VARIANT 339 339 H -> N (in dbSNP:rs35880225).
/FTId=VAR_033608.
MUTAGEN 67 67 K->R: Loss of LFA-3 binding.
{ECO:0000269|PubMed:2444890}.
MUTAGEN 70 70 Q->K: Loss of LFA-3 binding.
{ECO:0000269|PubMed:2444890}.
MUTAGEN 110 110 Y->D: Loss of LFA-3 and CD59 binding.
{ECO:0000269|PubMed:2444890}.
MUTAGEN 111 111 D->H: Loss of LFA-3 and CD59 binding.
{ECO:0000269|PubMed:2444890}.
CONFLICT 287 287 G -> A (in Ref. 3). {ECO:0000305}.
CONFLICT 339 351 HGAAENSLSPSSN -> MGQQKTHCPLPLIKKDRNCLFQ
(in Ref. 3; AAA51946). {ECO:0000305}.
STRAND 31 36 {ECO:0000244|PDB:1HNF}.
STRAND 41 43 {ECO:0000244|PDB:1HNF}.
STRAND 52 61 {ECO:0000244|PDB:1HNF}.
HELIX 62 64 {ECO:0000244|PDB:1HNF}.
STRAND 67 71 {ECO:0000244|PDB:1HNF}.
HELIX 73 75 {ECO:0000244|PDB:1HNF}.
STRAND 77 80 {ECO:0000244|PDB:1HNF}.
STRAND 84 86 {ECO:0000244|PDB:1HNF}.
TURN 88 90 {ECO:0000244|PDB:1QA9}.
STRAND 92 94 {ECO:0000244|PDB:1HNF}.
HELIX 99 101 {ECO:0000244|PDB:1HNF}.
STRAND 103 111 {ECO:0000244|PDB:1HNF}.
STRAND 116 127 {ECO:0000244|PDB:1HNF}.
STRAND 134 138 {ECO:0000244|PDB:1HNF}.
TURN 139 142 {ECO:0000244|PDB:1HNF}.
STRAND 143 147 {ECO:0000244|PDB:1HNF}.
STRAND 155 162 {ECO:0000244|PDB:1HNF}.
STRAND 164 170 {ECO:0000244|PDB:1HNF}.
STRAND 172 175 {ECO:0000244|PDB:1HNF}.
STRAND 180 189 {ECO:0000244|PDB:1HNF}.
STRAND 194 203 {ECO:0000244|PDB:1HNF}.
SEQUENCE 351 AA; 39448 MW; A03D853C3B618917 CRC64;
MSFPCKFVAS FLLIFNVSSK GAVSKEITNA LETWGALGQD INLDIPSFQM SDDIDDIKWE
KTSDKKKIAQ FRKEKETFKE KDTYKLFKNG TLKIKHLKTD DQDIYKVSIY DTKGKNVLEK
IFDLKIQERV SKPKISWTCI NTTLTCEVMN GTDPELNLYQ DGKHLKLSQR VITHKWTTSL
SAKFKCTAGN KVSKESSVEP VSCPEKGLDI YLIIGICGGG SLLMVFVALL VFYITKRKKQ
RSRRNDEELE TRAHRVATEE RGRKPHQIPA STPQNPATSQ HPPPPPGHRS QAPSHRPPPP
GHRVQHQPQK RPPAPSGTQV HQQKGPPLPR PRVQPKPPHG AAENSLSPSS N


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U1784h CLIA CD7,GP40,Homo sapiens,Human,T-cell antigen CD7,T-cell leukemia antigen,T-cell surface antigen Leu-9,TP41 96T
E1784h ELISA kit CD7,GP40,Homo sapiens,Human,T-cell antigen CD7,T-cell leukemia antigen,T-cell surface antigen Leu-9,TP41 96T
E1784h ELISA CD7,GP40,Homo sapiens,Human,T-cell antigen CD7,T-cell leukemia antigen,T-cell surface antigen Leu-9,TP41 96T
EIAAB25059 CD200 cell surface glycoprotein receptor,Cd200r1,Cell surface glycoprotein CD200 receptor 1,Cell surface glycoprotein OX2 receptor 1,Mouse,Mox2r,Mus musculus,Ox2r


 

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