T-cell surface antigen CD2 precursor - Rattus norvegicus (Rat)

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P08921 (CD2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 125. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

Cd2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	344 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 and PSTPIP1 By similarity.
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
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell activation Inferred from mutant phenotype PubMed 10458478. Source: RGD cell-cell adhesion Inferred from mutant phenotype PubMed 8938183. Source: RGD
Cellular_component	cell surface Inferred from direct assay PubMed 11981840 PubMed 8938183. Source: RGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane raft Inferred from direct assay PubMed 18178839. Source: RGD protein complex Inferred from direct assay PubMed 9576909. Source: RGD
Molecular_function	antigen binding Inferred from mutant phenotype PubMed 9576909. Source: RGD protein homodimerization activity Inferred from direct assay PubMed 10526406. Source: RGD protein self-association Inferred from direct assay PubMed 10841761. Source: RGD receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Chain

23 – 344

322

T-cell surface antigen CD2

PRO_0000014603

Regions

Topological domain

23 – 202

180

Extracellular Potential

Transmembrane

203 – 228

Helical; Potential

Topological domain

229 – 344

116

Cytoplasmic Potential

Domain

23 – 121

Ig-like V-type

Domain

122 – 202

Ig-like C2-type

Compositional bias

277 – 343

Pro-rich

Amino acid modifications

Glycosylation

N-linked (GlcNAc...)

Glycosylation

106

N-linked (GlcNAc...)

Glycosylation

134

N-linked (GlcNAc...)

Disulfide bond

132 ↔ 196

Disulfide bond

139 ↔ 179

Secondary structure

344

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P08921 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 41BAED392CE16356
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FASTA

344

38,414

        10         20         30         40         50         60 
MRCKFLGSFF LLFSLSSKGA DCRDSGTVWG ALGHGINLNI PNFQMTDDID EVRWERGSTL 

        70         80         90        100        110        120 
VAEFKRKMKP FLKSGAFEIL ANGDLKIKNL TRDDSGTYNV TVYSTNGTRI LDKALDLRIL 

       130        140        150        160        170        180 
EMVSKPMIYW ECSNATLTCE VLEGTDVELK LYQGKEHLRS LRQKTMSYQW TNLRAPFKCK 

       190        200        210        220        230        240 
AVNRVSQESE MEVVNCPEKG LPLYLIVGVS AGGLLLVFFG ALFIFCICKR KKRNRRRKGE 

       250        260        270        280        290        300 
ELEIKASRMS TVERGPKPHS TQASAPASQN PVASQAPPPP GHHLQTPGHR PLPPSHRNRE 

       310        320        330        340 
HQPKKRPPPS GTQVHQQKGP PLPRPRVQPK PPCGSGDVSL PPPN

« Hide

References

[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.
[5]	"One sequence, two folds: a metastable structure of CD2." Murray A.J., Lewis S.J., Barclay A.N., Brady R.L. Proc. Natl. Acad. Sci. U.S.A. 92:7337-7341(1995) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05111 mRNA. Translation: CAA28757.1.

IPI

IPI00566418.

PIR

RWRTC2. A33071.

RefSeq

NP_036962.1. NM_012830.1.

UniGene

Rn.10328.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A64	X-ray	2.00	A/B	23-121	[»]
1A6P	X-ray	2.08	A/B	26-121	[»]
1A7B	X-ray	3.10	A/B/C/D	23-121	[»]
1CDC	X-ray	2.00	A/B	23-121	[»]
1HNG	X-ray	2.80	A/B	23-198	[»]
1T6W	NMR	-	A	23-121	[»]

ProteinModelPortal

P08921.

SMR

P08921. Positions 24-198.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1514111.

STRING

10116.ENSRNOP00000046134.

PTM databases

PhosphoSite

P08921.

Proteomic databases

PRIDE

P08921.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

497761.

KEGG

rno:497761.

UCSC

RGD:2297. rat.

Organism-specific databases

CTD

914.

RGD

2297. Cd2.

Phylogenomic databases

eggNOG

NOG47564.

HOGENOM

HOG000276890.

HOVERGEN

HBG000262.

K06449.

Gene expression databases

ArrayExpress

P08921.

Genevestigator

P08921.

GermOnline

ENSRNOG00000015821. Rattus norvegicus.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR003599. Ig_sub.
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.

SMART

SM00409. IG. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P08921.

NextBio

697752.

Entry information

Entry name

CD2_RAT

Accession

Primary (citable) accession number: P08921

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	April 3, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents