ID   CD2_MACFA               Reviewed;         351 AA.
AC   Q6SZ61;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=T-cell surface antigen CD2;
DE   AltName: CD_antigen=CD2;
DE   Flags: Precursor;
GN   Name=CD2;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15302161; DOI=10.1016/j.molimm.2004.05.004;
RA   Damschroder M.M., Kozhich A.A., Woods R.M., Cheng L., Mullikin B.A.,
RA   Wilson S.D., Ulbrandt N.D., Bachy C.M., Wu H., Suzich J.A., Kiener P.A.,
RA   Dall'Acqua W.F., White W.I.;
RT   "Analysis of human and primate CD2 molecules by protein sequence and
RT   epitope mapping with anti-human CD2 antibodies.";
RL   Mol. Immunol. 41:985-1000(2004).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CD48 (By similarity). Interacts with CD58 (LFA-
CC       3) (By similarity). Interacts with CD2AP (By similarity). Interacts
CC       with PSTPIP1 (By similarity). Interacts with FCGR3A; this interaction
CC       modulates NK cell activation and cytotoxicity.
CC       {ECO:0000250|UniProtKB:P06729, ECO:0000250|UniProtKB:P08920,
CC       ECO:0000250|UniProtKB:P08921}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P06729};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:P06729}.
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DR   EMBL; AY445036; AAR15883.1; -; mRNA.
DR   RefSeq; NP_001270706.1; NM_001283777.1.
DR   AlphaFoldDB; Q6SZ61; -.
DR   SMR; Q6SZ61; -.
DR   STRING; 9541.XP_005542258.1; -.
DR   ABCD; Q6SZ61; 4 sequenced antibodies.
DR   GeneID; 102120798; -.
DR   CTD; 914; -.
DR   eggNOG; ENOG502S5UN; Eukaryota.
DR   OrthoDB; 977841at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0009986; C:cell surface; IEA:UniProt.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030101; P:natural killer cell activation; ISS:UniProtKB.
DR   GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..351
FT                   /note="T-cell surface antigen CD2"
FT                   /id="PRO_0000014601"
FT   TOPO_DOM        25..209
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..128
FT                   /note="Ig-like V-type"
FT   DOMAIN          129..209
FT                   /note="Ig-like C2-type"
FT   REGION          61..75
FT                   /note="CD58 binding region 1"
FT                   /evidence="ECO:0000250|UniProtKB:P06729"
FT   REGION          106..120
FT                   /note="CD58 binding region 2"
FT                   /evidence="ECO:0000250|UniProtKB:P06729"
FT   REGION          241..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..293
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        139..203
FT                   /evidence="ECO:0000250|UniProtKB:P08921"
FT   DISULFID        146..186
FT                   /evidence="ECO:0000250|UniProtKB:P08921"
SQ   SEQUENCE   351 AA;  39580 MW;  D549EA58D3CD5AE6 CRC64;
     MSFPCKFVAS FLLIFNVSSK GAVSKEIRNA LETWGALGQD IDLDIPSFQM SDDIDDIRWE
     KTSDKKKIAQ FRKEKETFEE KDAYKLFKNG TLKIKHLKIH DQDSYKVSIY DTKGKNVLEK
     TFDLKIQERV SEPKISWTCI NTTLTCEVMN GTDPELNLYQ DGKHVKLSQR VITHKWTTSL
     SAKFKCTAGN KVSKESRMET VSCPEKGLDI YLIIGICGGG SLLMVFVALL VFYITKRKKQ
     RSRRNDEELE IRAHRVATEE RGRKPHQIPA STPQNPAASQ HPPPPPGHRS QAPSHRPLPP
     GHRVQHQPQK RPPAPSGTQV HQQKGPPLPR PRVQPKPPQG AAENSLSPSS N