Q07108 (CD69_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Early activation antigen CD69

Alternative name(s):
Activation inducer molecule
Short name=AIM
BL-AC/P26
C-type lectin domain family 2 member C
EA1
Early T-cell activation antigen p60
GP32/28
Leukocyte surface antigen Leu-23
MLR-3
CD_antigen=CD69

Gene names

Name:	CD69
Synonyms:	CLEC2C

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	199 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in lymphocyte proliferation and functions as a signal transmitting receptor in lymphocytes, natural killer (NK) cells, and platelets.
Subunit structure	Homodimer; disulfide-linked. Ref.6 Ref.7 Ref.8
Subcellular location	Membrane; Single-pass type II membrane protein.
Tissue specificity	Expressed on the surface of activated T-cells, B-cells, natural killer cells, neutrophils, eosinophils, epidermal Langerhans cells and platelets.
Developmental stage	Earliest inducible cell surface glycoprotein acquired during lymphoid activation.
Induction	By antigens, mitogens or activators of PKC on the surface of T and B-lymphocytes. By interaction of IL-2 with the p75 IL-2R on the surface of NK cells.
Post-translational modification	Constitutive Ser/Thr phosphorylation in both mature thymocytes and activated T-lymphocytes.
Sequence similarities	Contains 1 C-type lectin domain.

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Lectin
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to drug Inferred from electronic annotation. Source: Compara
Cellular_component	external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro transmembrane signaling receptor activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 199

199

Early activation antigen CD69

PRO_0000046583

Regions

Topological domain

1 – 40

40

Cytoplasmic Potential

Transmembrane

41 – 61

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

62 – 199

138

Extracellular Potential

Domain

92 – 195

104

C-type lectin

Amino acid modifications

Glycosylation

166

1

N-linked (GlcNAc...) Potential

Disulfide bond

68

Interchain Probable

Disulfide bond

85 ↔ 96

Ref.6 Ref.7 Ref.8

Disulfide bond

113 ↔ 194

Ref.6 Ref.7 Ref.8

Disulfide bond

173 ↔ 186

Ref.6 Ref.7 Ref.8

Secondary structure

1

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199

Helix Strand Turn

Details...

Beta strand

90 – 92

3

Beta strand

95 – 99

5

Helix

106 – 114

9

Turn

115 – 117

3

Helix

126 – 136

11

Beta strand

141 – 147

7

Beta strand

153 – 155

3

Beta strand

168 – 170

3

Beta strand

172 – 177

6

Beta strand

180 – 184

5

Beta strand

190 – 197

8

Sequences

	Sequence		Length	Mass (Da)
	Q07108 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 172E2699D2FB8DFB	FASTA	199	22,559
	10 20 30 40 50 60 MSSENCFVAE NSSLHPESGQ ENDATSPHFS TRHEGSFQVP VLCAVMNVVF ITILIIALIA 70 80 90 100 110 120 LSVGQYNCPG QYTFSMPSDS HVSSCSEDWV GYQRKCYFIS TVKRSWTSAQ NACSEHGATL 130 140 150 160 170 180 AVIDSEKDMN FLKRYAGREE HWVGLKKEPG HPWKWSNGKE FNNWFNVTGS DKCVFLKNTE 190 VSSMECEKNL YWICNKPYK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression cloning of the early activation antigen CD69, a type II integral membrane protein with a C-type lectin domain." Hamann J., Fiebig H., Strauss M. J. Immunol. 150:4920-4927(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Blood.
[2]	"Molecular cloning, expression, and chromosomal localization of the human earliest lymphocyte activation antigen AIM/CD69, a new member of the C-type animal lectin superfamily of signal-transmitting receptors." Lopez-Cabrera M., Santis A.G., Fernandez-Ruiz E., Blacher R., Esch F., Sanchez-Mateos P., Sanchez-Madrid F. J. Exp. Med. 178:537-547(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 96-103; 128-146 AND 189-199. Tissue: Blood.
[3]	"Molecular characterization of the early activation antigen CD69: a type II membrane glycoprotein related to a family of natural killer cell activation antigens." Ziegler S.F., Ramsdell F., Hjerrild K.A., Armitage R.J., Grabstein K.H., Hennen K.B., Farrah T., Fanslow W.C., Shevach E.M., Alderson M.R. Eur. J. Immunol. 23:1643-1648(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Structure of the gene coding for the human early lymphocyte activation antigen CD69: a C-type lectin receptor evolutionarily related with the gene families of natural killer cell-specific receptors." Santis A., Lopez-Cabrera M., Hamann J., Strauss M., Sanchez-Madrid F. Eur. J. Immunol. 24:1692-1697(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[5]	"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]. Tissue: Pancreas.
[6]	"Crystal structure of human CD69: a C-type lectin-like activation marker of hematopoietic cells." Natarajan K., Sawicki M.W., Margulies D.H., Mariuzza R.A. Biochemistry 39:14779-14786(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS), SUBUNIT, DISULFIDE BONDS.
[7]	"Crystal structure of the C-type lectin-like domain from the human hematopoietic cell receptor CD69." Llera A.S., Viedma F., Sanchez-Madrid F., Tormo J. J. Biol. Chem. 276:7312-7319(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 82-199, SUBUNIT, DISULFIDE BONDS.
[8]	"Soluble recombinant CD69 receptors optimized to have an exceptional physical and chemical stability display prolonged circulation and remain intact in the blood of mice." Vanek O., Nalezkova M., Kavan D., Borovickova I., Pompach P., Novak P., Kumar V., Vannucci L., Hudecek J., Hofbauerova K., Kopecky V. Jr., Brynda J., Kolenko P., Dohnalek J., Kaderavek P., Chmelik J., Gorcik L., Zidek L., Sklenar V., Bezouska K. FEBS J. 275:5589-5606(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 82-199, SUBUNIT, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

CD69

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L07555 mRNA. Translation: AAB46359.1.
Z22576 mRNA. Translation: CAA80298.1.
Z30426 , Z30430, Z30427, Z30429, Z30428 Genomic DNA. Translation: CAA83017.1.
BC007037 mRNA. Translation: AAH07037.1.

IPI

IPI00014854.

PIR

JH0822.

RefSeq

NP_001772.1. NM_001781.2.

UniGene

Hs.208854.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E87	X-ray	1.50	A	82-199	[»]
1E8I	X-ray	1.95	A/B	82-199	[»]
1FM5	X-ray	2.27	A	1-199	[»]
3CCK	X-ray	1.80	A/B	82-199	[»]
3HUP	X-ray	1.37	A/B	70-199	[»]

DisProt

DP00306.

ProteinModelPortal

Q07108.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q07108. 1 interaction.

STRING

9606.ENSP00000228434.

PTM databases

PhosphoSite

Q07108.

Polymorphism databases

DMDM

584906.

Proteomic databases

PaxDb

Q07108.

PRIDE

Q07108.

Protocols and materials databases

DNASU

969.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000228434; ENSP00000228434; ENSG00000110848.

GeneID

969.

KEGG

hsa:969.

UCSC

uc001qwk.3. human.

Organism-specific databases

CTD

969.

GeneCards

GC12M009908.

HGNC

HGNC:1694. CD69.

HPA

CAB002503.

MIM

107273. gene.

neXtProt

NX_Q07108.

PharmGKB

PA26233.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG276386.

HOGENOM

HOG000111491.

HOVERGEN

HBG005288.

InParanoid

Q07108.

KO

K06502.

OMA

VGQYNCP.

OrthoDB

EOG495ZT7.

PhylomeDB

Q07108.

Gene expression databases

ArrayExpress

Q07108.

Bgee

Q07108.

CleanEx

HS_CD69.

Genevestigator

Q07108.

GermOnline

ENSG00000110848. Homo sapiens.

Family and domain databases

Gene3D

3.10.100.10. 1 hit.

InterPro

IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
[Graphical view]

Pfam

PF00059. Lectin_C. 1 hit.
[Graphical view]

SMART

SM00034. CLECT. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.

PROSITE

PS00615. C_TYPE_LECTIN_1. False negative.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q07108.

GenomeRNAi

969.

NextBio

4056.

SOURCE

Search...

Entry information

Entry name

CD69_HUMAN

Accession

Primary (citable) accession number: Q07108

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 127 of the entry and version 1 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.