P06729 (CD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
T-cell surface antigen CD2

Alternative name(s):
Erythrocyte receptor
LFA-2
LFA-3 receptor
Rosette receptor
T-cell surface antigen T11/Leu-5
CD_antigen=CD2

Gene names

Name:	CD2
Synonyms:	SRBC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	Interacts with CD2AP By similarity. Interacts with PSTPIP1. Ref.11
Subcellular location	Membrane; Single-pass type I membrane protein.
Sequence similarities	Contains 1 Ig-like C2-type (immunoglobulin-like) domain. Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell activation Traceable author statement PubMed 2471997. Source: UniProtKB blood coagulation Traceable author statement. Source: Reactome cell surface receptor signaling pathway Traceable author statement PubMed 10575274. Source: UniProtKB cell-cell adhesion Non-traceable author statement Ref.14. Source: UniProtKB induction of apoptosis Traceable author statement PubMed 10575274PubMed 9270771. Source: UniProtKB leukocyte migration Traceable author statement. Source: Reactome membrane raft polarization Traceable author statement PubMed 11376005PubMed 11591762. Source: UniProtKB natural killer cell activation Non-traceable author statement PubMed 12714509. Source: UniProtKB positive regulation of myeloid dendritic cell activation Non-traceable author statement PubMed 12714509. Source: UniProtKB regulation of T cell differentiation Non-traceable author statement PubMed 11544295. Source: UniProtKB
Cellular_component	anchored to plasma membrane Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from direct assay PubMed 21460847. Source: MGI extracellular region Inferred from electronic annotation. Source: Compara integral to plasma membrane Non-traceable author statement Ref.14. Source: UniProtKB internal side of plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	eukaryotic cell surface binding Inferred from electronic annotation. Source: Compara receptor activity Non-traceable author statement Ref.14. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Chain

25 – 351

327

T-cell surface antigen CD2

PRO_0000014600

Regions

Topological domain

25 – 209

185

Extracellular Potential

Transmembrane

210 – 235

26

Helical; Potential

Topological domain

236 – 351

116

Cytoplasmic Potential

Domain

25 – 128

104

Ig-like V-type

Domain

129 – 209

81

Ig-like C2-type

Region

61 – 75

15

LFA-3 (CD58) binding region 1

Region

106 – 120

15

LFA-3 (CD58) binding region 2

Compositional bias

282 – 338

57

Pro-rich

Amino acid modifications

Glycosylation

89

1

N-linked (GlcNAc...)

Glycosylation

141

1

N-linked (GlcNAc...) Potential

Glycosylation

150

1

N-linked (GlcNAc...) Potential

Disulfide bond

139 ↔ 203

Ref.12

Disulfide bond

146 ↔ 186

Ref.12

Natural variations

Natural variant

217

1

C → Y in a breast cancer sample; somatic mutation. Ref.15

VAR_035504

Natural variant

266

1

H → Q. Ref.2 Ref.6 Ref.8
Corresponds to variant rs699738 [ dbSNP | Ensembl ].

VAR_017104

Natural variant

339

1

H → N.
Corresponds to variant rs35880225 [ dbSNP | Ensembl ].

VAR_033608

Experimental info

Mutagenesis

67

1

K → R: Loss of LFA-3 binding.

Mutagenesis

70

1

Q → K: Loss of LFA-3 binding.

Mutagenesis

110

1

Y → D: Loss of LFA-3 and CD59 binding.

Mutagenesis

111

1

D → H: Loss of LFA-3 and CD59 binding.

Sequence conflict

287

1

G → A Ref.3

Sequence conflict

339 – 351

13

HGAAE…SPSSN → MGQQKTHCPLPLIKKDRNCL FQ in AAA51946. Ref.3

Secondary structure

1

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351

Helix Strand Turn

Details...

Beta strand

31 – 36

6

Beta strand

41 – 43

3

Beta strand

52 – 61

10

Helix

62 – 64

3

Beta strand

67 – 71

5

Helix

73 – 75

3

Beta strand

77 – 80

4

Beta strand

84 – 86

3

Turn

88 – 90

3

Beta strand

92 – 94

3

Helix

99 – 101

3

Beta strand

103 – 111

9

Beta strand

116 – 127

12

Beta strand

134 – 138

5

Turn

139 – 142

4

Beta strand

143 – 147

5

Beta strand

155 – 162

8

Beta strand

164 – 170

7

Beta strand

172 – 175

4

Beta strand

180 – 189

10

Beta strand

194 – 203

10

Sequences

	Sequence		Length	Mass (Da)
	P06729 [UniParc]. Last modified October 23, 2007. Version 2. Checksum: A03D853C3B618917	FASTA	351	39,448
	10 20 30 40 50 60 MSFPCKFVAS FLLIFNVSSK GAVSKEITNA LETWGALGQD INLDIPSFQM SDDIDDIKWE 70 80 90 100 110 120 KTSDKKKIAQ FRKEKETFKE KDTYKLFKNG TLKIKHLKTD DQDIYKVSIY DTKGKNVLEK 130 140 150 160 170 180 IFDLKIQERV SKPKISWTCI NTTLTCEVMN GTDPELNLYQ DGKHLKLSQR VITHKWTTSL 190 200 210 220 230 240 SAKFKCTAGN KVSKESSVEP VSCPEKGLDI YLIIGICGGG SLLMVFVALL VFYITKRKKQ 250 260 270 280 290 300 RSRRNDEELE TRAHRVATEE RGRKPHQIPA STPQNPATSQ HPPPPPGHRS QAPSHRPPPP 310 320 330 340 350 GHRVQHQPQK RPPAPSGTQV HQQKGPPLPR PRVQPKPPHG AAENSLSPSS N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Exon-intron organization and sequence comparison of human and murine T11 (CD2) genes." Diamond D.J., Clayton L.K., Sayre P.H., Reinherz E.L. Proc. Natl. Acad. Sci. U.S.A. 85:1615-1619(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure." Seed B., Aruffo A. Proc. Natl. Acad. Sci. U.S.A. 84:3365-3369(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-266.
[3]	"Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen." Sewell W.A., Brown M.H., Dunne J., Owen M.J., Crumpton M.J. Proc. Natl. Acad. Sci. U.S.A. 83:8718-8722(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	Erratum 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) Cited for: SEQUENCE REVISION.
[5]	"Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes." Sayre P.H., Chang H.-C., Hussey R.E., Brown N.R., Richardson N.E., Spagnoli G., Clayton L.K., Reinherz E.L. Proc. Natl. Acad. Sci. U.S.A. 84:2941-2945(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"The structure of the human CD2 gene and its expression in transgenic mice." Lang G., Wotton D., Owen M.J., Sewell W.A., Brown M.H., Mason D.Y., Crumpton M.J., Kioussis D. EMBO J. 7:1675-1682(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-266.
[7]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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], VARIANT GLN-266. Tissue: Pancreas and Spleen.
[9]	"Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2)." Peterson A., Seed B. Nature 329:842-846(1987) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[10]	"Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59." Hahn W.C., Menu E., Bothwell A.L.M., Sims P.J., Bierer B.E. Science 256:1805-1807(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CD59-BINDING DATA.
[11]	"A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion." Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R., Sunder-Plassmann R., Reinherz E.L. EMBO J. 17:7320-7336(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSTPIP1.
[12]	"Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5-A resolution." Bodian D.L., Jones E.Y., Harlos K., Stuart D.I., Davis S.J. Structure 2:755-766(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-206, DISULFIDE BONDS.
[13]	"Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2." Withka J.M., Wyss D.F., Wagner G., Arulanandam A.R.N., Reinherz E.L., Recny M.A. Structure 1:69-81(1993) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 25-129.
[14]	"Conformation and function of the N-linked glycan in the adhesion domain of human CD2." Wyss D.F., Choi J.S., Li J., Knoppers M.H., Willis K.J., Arulanandam A.R., Smolyar A., Reinherz E.L., Wagner G. Science 269:1273-1278(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 25-129.
[15]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-217.
+	Additional computationally mapped references.

Web resources

Wikipedia

CD2 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19806 , M19798, M19800, M19802, M19804 Genomic DNA. Translation: AAA53095.1.
M16445 mRNA. Translation: AAA51738.1.
M14362 mRNA. Translation: AAA35571.1.
M16336 mRNA. Translation: AAA51946.1.
X07871 , X07872, X07873, X07874 Genomic DNA. Translation: CAA30721.1.
AL135798 Genomic DNA. Translation: CAC14840.1.
BC033583 mRNA. Translation: AAH33583.1.

IPI

IPI00027484.

PIR

RWHUC2. A28967.

RefSeq

NP_001758.2. NM_001767.3.

UniGene

Hs.523500.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CDB	NMR	-	A	25-129	[»]
1GYA	NMR	-	A	25-129	[»]
1HNF	X-ray	2.50	A	25-206	[»]
1L2Z	NMR	-	B	294-304	[»]
1QA9	X-ray	3.20	A/C	28-129	[»]
2J6O	X-ray	2.22	C	324-333	[»]
2J7I	X-ray	2.90	C/D	324-333	[»]

ProteinModelPortal

P06729.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06729. 3 interactions.

MINT

MINT-99488.

STRING

9606.ENSP00000358490.

PTM databases

GlycoSuiteDB

P06729.

PhosphoSite

P06729.

Polymorphism databases

DMDM

160370002.

Proteomic databases

PaxDb

P06729.

PRIDE

P06729.

Protocols and materials databases

DNASU

914.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369478; ENSP00000358490; ENSG00000116824.

GeneID

914.

KEGG

hsa:914.

UCSC

uc001egu.4. human.

Organism-specific databases

CTD

914.

GeneCards

GC01P117297.

H-InvDB

HIX0000931.

HGNC

HGNC:1639. CD2.

HPA

CAB002430.
HPA003883.

MIM

186990. gene.

neXtProt

NX_P06729.

PharmGKB

PA26198.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG47564.

HOGENOM

HOG000276890.

HOVERGEN

HBG000262.

InParanoid

P06729.

KO

K06449.

OMA

GTQVHQQ.

OrthoDB

EOG4H9XMK.

PhylomeDB

P06729.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

SignaLink

P06729.

Gene expression databases

ArrayExpress

P06729.

Bgee

P06729.

CleanEx

HS_CD2.

Genevestigator

P06729.

GermOnline

ENSG00000116824. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR013106. Ig_V-set.
IPR015631. SLAM_fam_rcpts.
IPR015632. T-cell_sdhesion_molc_CD2.
[Graphical view]

PANTHER

PTHR12080. PTHR12080. 1 hit.
PTHR12080:SF10. PTHR12080:SF10. 1 hit.

Pfam

PF05790. C2-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]

PRINTS

PR01870. CD2ANTIGEN.

PROSITE

PS50835. IG_LIKE. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2040.

DrugBank

DB00092. Alefacept.

EvolutionaryTrace

P06729.

GenomeRNAi

914.

NextBio

3780.

SOURCE

Search...

Entry information

Entry name

CD2_HUMAN

Accession

Primary (citable) accession number: P06729
Secondary accession number(s): Q96TE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	October 23, 2007
Last modified:	May 29, 2013
This is version 157 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.