CD2_MOUSE
ID CD2_MOUSE Reviewed; 344 AA.
AC P08920; Q61394;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=T-cell surface antigen CD2;
DE AltName: Full=LFA-2;
DE AltName: Full=LFA-3 receptor;
DE AltName: Full=Lymphocyte antigen 37;
DE Short=Ly-37;
DE AltName: Full=T-cell surface antigen T11/Leu-5;
DE AltName: CD_antigen=CD2;
DE Flags: Precursor;
GN Name=Cd2; Synonyms=Ly-37;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=B10.A;
RX PubMed=2440689; DOI=10.1002/eji.1830170718;
RA Sewell W.A., Brown M.H., Fink P.J., Kozak C.A., Crumpton M.J.;
RT "The murine homologue of the T lymphocyte CD2 antigen: molecular cloning,
RT chromosome assignment and cell surface expression.";
RL Eur. J. Immunol. 17:1015-1020(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2820751; DOI=10.1002/eji.1830170922;
RA Clayton L.K., Sayre P.H., Novotny J., Reinherz E.L.;
RT "Murine and human T11 (CD2) cDNA sequences suggest a common signal
RT transduction mechanism.";
RL Eur. J. Immunol. 17:1367-1370(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=2894031; DOI=10.1073/pnas.85.5.1615;
RA Diamond D.J., Clayton L.K., Sayre P.H., Reinherz E.L.;
RT "Exon-intron organization and sequence comparison of human and murine T11
RT (CD2) genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1615-1619(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3257775;
RA Yagita H., Okumura K., Nakauchi H.;
RT "Molecular cloning of the murine homologue of CD2. Homology of the molecule
RT to its human counterpart T11.";
RL J. Immunol. 140:1321-1326(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hematopoietic;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH CD2AP.
RX PubMed=9741631; DOI=10.1016/s0092-8674(00)81608-6;
RA Dustin M.L., Olszowy M.W., Holdorf A.D., Li J., Bromley S., Desai N.,
RA Widder P., Rosenberger F., van der Merwe P.A., Allen P.M., Shaw A.S.;
RT "A novel adaptor protein orchestrates receptor patterning and cytoskeletal
RT polarity in T-cell contacts.";
RL Cell 94:667-677(1998).
RN [7]
RP INTERACTION WITH PSTPIP1.
RX PubMed=12530983; DOI=10.1016/s1074-7613(02)00516-2;
RA Badour K., Zhang J., Shi F., McGavin M.K.H., Rampersad V., Hardy L.A.,
RA Field D., Siminovitch K.A.;
RT "The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP
RT and PSTPIP1 adaptors to promote formation of the immunological synapse.";
RL Immunity 18:141-154(2003).
CC -!- FUNCTION: CD2 interacts with lymphocyte function-associated antigen
CC CD58 (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and
CC other cell types. CD2 is implicated in the triggering of T-cells, the
CC cytoplasmic domain is implicated in the signaling function.
CC -!- SUBUNIT: Interacts with CD48 (By similarity). Interacts with CD58 (LFA-
CC 3) (By similarity). Interacts with CD2AP (PubMed:9741631). Interacts
CC with PSTPIP1 (PubMed:12530983). Interacts with FCGR3A; this interaction
CC modulates NK cell activation and cytotoxicity.
CC {ECO:0000250|UniProtKB:P06729, ECO:0000250|UniProtKB:P08921,
CC ECO:0000269|PubMed:12530983, ECO:0000269|PubMed:9741631}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2440689};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in thymus and spleen.
CC {ECO:0000269|PubMed:2440689}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:2440689}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y00023; CAA68258.1; -; mRNA.
DR EMBL; X06143; CAA29500.1; -; mRNA.
DR EMBL; M19807; AAA37393.1; -; Genomic_DNA.
DR EMBL; M19799; AAA37393.1; JOINED; Genomic_DNA.
DR EMBL; M19801; AAA37393.1; JOINED; Genomic_DNA.
DR EMBL; M19803; AAA37393.1; JOINED; Genomic_DNA.
DR EMBL; M19805; AAA37393.1; JOINED; Genomic_DNA.
DR EMBL; M18934; AAA37397.1; -; mRNA.
DR EMBL; BC053731; AAH53731.1; -; mRNA.
DR CCDS; CCDS17681.1; -.
DR PIR; I49585; I49585.
DR RefSeq; NP_038514.1; NM_013486.2.
DR AlphaFoldDB; P08920; -.
DR SMR; P08920; -.
DR IntAct; P08920; 2.
DR MINT; P08920; -.
DR STRING; 10090.ENSMUSP00000029456; -.
DR GlyGen; P08920; 4 sites.
DR PhosphoSitePlus; P08920; -.
DR EPD; P08920; -.
DR PaxDb; P08920; -.
DR PRIDE; P08920; -.
DR ProteomicsDB; 280018; -.
DR ABCD; P08920; 37 sequenced antibodies.
DR Antibodypedia; 1086; 2939 antibodies from 53 providers.
DR DNASU; 12481; -.
DR Ensembl; ENSMUST00000029456; ENSMUSP00000029456; ENSMUSG00000027863.
DR GeneID; 12481; -.
DR KEGG; mmu:12481; -.
DR UCSC; uc008qrf.1; mouse.
DR CTD; 914; -.
DR MGI; MGI:88320; Cd2.
DR VEuPathDB; HostDB:ENSMUSG00000027863; -.
DR eggNOG; ENOG502S5UN; Eukaryota.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_069390_0_0_1; -.
DR InParanoid; P08920; -.
DR OMA; YCIRRKK; -.
DR OrthoDB; 977841at2759; -.
DR PhylomeDB; P08920; -.
DR TreeFam; TF335971; -.
DR BioGRID-ORCS; 12481; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Ccnd2; mouse.
DR PRO; PR:P08920; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P08920; protein.
DR Bgee; ENSMUSG00000027863; Expressed in peripheral lymph node and 55 other tissues.
DR ExpressionAtlas; P08920; baseline and differential.
DR Genevisible; P08920; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0030101; P:natural killer cell activation; ISO:MGI.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0042110; P:T cell activation; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR015632; CD2.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008424; Ig_C2-set.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF05790; C2-set; 1.
DR Pfam; PF07686; V-set; 1.
DR PRINTS; PR01870; CD2ANTIGEN.
DR SUPFAM; SSF48726; SSF48726; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT CHAIN 23..344
FT /note="T-cell surface antigen CD2"
FT /id="PRO_0000014602"
FT TOPO_DOM 23..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..121
FT /note="Ig-like V-type"
FT DOMAIN 122..202
FT /note="Ig-like C2-type"
FT REGION 56..68
FT /note="CD58 binding region 1"
FT /evidence="ECO:0000250|UniProtKB:P06729"
FT REGION 100..114
FT /note="CD58 binding region 2"
FT /evidence="ECO:0000250|UniProtKB:P06729"
FT REGION 238..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..344
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 133..197
FT /evidence="ECO:0000250|UniProtKB:P08921"
FT DISULFID 140..180
FT /evidence="ECO:0000250|UniProtKB:P08921"
FT CONFLICT 99
FT /note="Y -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="M -> V (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="T -> I (in Ref. 4; AAA37397)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="N -> A (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="N -> S (in Ref. 4; AAA37393/AAA37397)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="K -> N (in Ref. 2; CAA29500)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="M -> T (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38415 MW; CFD12FCBD1444450 CRC64;
MKCKFLGSFF LLFSLSGKGA DCRDNETIWG VLGHGITLNI PNFQMTDDID EVRWVRRGTL
VAEFKRKKPP FLISETYEVL ANGSLKIKKP MMRNDSGTYN VMVYGTNGMT RLEKDLDVRI
LERVSKPMIH WECPNTTLTC AVLQGTDFEL KLYQGETLLN SLPQKNMSYQ WTNLNAPFKC
EAINPVSKES KMEVVNCPEK GLSFYVTVGV GAGGLLLVLL VALFIFCICK RRKRNRRRKD
EELEIKASRT STVERGPKPH STPAAAAQNS VALQAPPPPG HHLQTPGHRP LPPGHRTREH
QQKKRPPPSG TQIHQQKGPP LPRPRVQPKP PCGSGDGVSL PPPN
