ID CD2_RAT Reviewed; 344 AA. AC P08921; F1M9W7; Q5I0M6; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 25-APR-2018, sequence version 2. DT 02-SEP-2026, entry version 197. DE RecName: Full=T-cell surface antigen CD2; DE AltName: Full=LFA-2; DE AltName: Full=LFA-3 receptor; DE AltName: Full=OX-34 antigen {ECO:0000303|PubMed:3102667}; DE AltName: Full=T-cell surface antigen T11/Leu-5; DE AltName: CD_antigen=CD2; DE Flags: Precursor; GN Name=Cd2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, RP AND SUBCELLULAR LOCATION. RC STRAIN=AO; RX PubMed=3102667; DOI=10.1084/jem.165.2.368; RA Williams A.F., Barclay A.N., Clark S.J., Paterson D.J., Willis A.C.; RT "Similarities in sequences and cellular expression between rat CD2 and CD4 RT antigens."; RL J. Exp. Med. 165:368-380(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; RX PubMed=15057822; DOI=10.1038/nature02426; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Spleen {ECO:0000312|EMBL:AAH88164.1}; 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 [5] RP IMPORTANCE OF C-TERMINAL IN SIGNALING, AND FUNCTION. RX PubMed=2901293; DOI=10.1016/0092-8674(88)90112-2; RA He Q., Beyers A.D., Barclay A.N., Williams A.F.; RT "A role in transmembrane signaling for the cytoplasmic domain of the CD2 T RT lymphocyte surface antigen."; RL Cell 54:979-984(1988). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-198, AND DISULFIDE BONDS. RX PubMed=1279440; DOI=10.1038/360232a0; RA Jones E.Y., Davis S.J., Williams A.F., Harlos K., Stuart D.I.; RT "Crystal structure at 2.8-A resolution of a soluble form of the cell RT adhesion molecule CD2."; RL Nature 360:232-239(1992). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-121. RX PubMed=7638192; DOI=10.1073/pnas.92.16.7337; RA Murray A.J., Lewis S.J., Barclay A.N., Brady R.L.; RT "One sequence, two folds: a metastable structure of CD2."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7337-7341(1995). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-121. RX PubMed=9731771; DOI=10.1038/1816; RA Murray A.J., Head J.G., Barker J.J., Brady R.L.; RT "Engineering an intertwined form of CD2 for stability and assembly."; RL Nat. Struct. Biol. 5:778-782(1998). RN [9] RP STRUCTURE BY NMR OF 23-121. RX PubMed=1682812; DOI=10.1038/353762a0; RA Driscoll P.C., Cyster J.G., Campbell I.D., Williams A.F.; RT "Structure of domain 1 of rat T lymphocyte CD2 antigen."; RL Nature 353:762-765(1991). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 121-199 IN COMPLEX WITH CD48, RP GLYCOSYLATION AT ASN-134, AND DISULFIDE BOND. RX PubMed=16803907; DOI=10.1074/jbc.m601314200; RA Evans E.J., Castro M.A., O'Brien R., Kearney A., Walsh H., Sparks L.M., RA Tucknott M.G., Davies E.A., Carmo A.M., van der Merwe P.A., Stuart D.I., RA Jones E.Y., Ladbury J.E., Ikemizu S., Davis S.J.; RT "Crystal structure and binding properties of the CD2 and CD244 (2B4)- RT binding protein, CD48."; RL J. Biol. Chem. 281:29309-29320(2006). 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 {ECO:0000269|PubMed:2901293}. CC -!- SUBUNIT: Interacts with CD48 (PubMed:16803907). Interacts with CD58 CC (LFA-3) (By similarity). Interacts with CD2AP (By similarity). CC Interacts with PSTPIP1 (By similarity). Interacts with FCGR3A; this CC interaction modulates NK cell activation and cytotoxicity. CC {ECO:0000250|UniProtKB:P06729, ECO:0000250|UniProtKB:P08920, CC ECO:0000269|PubMed:16803907}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3102667}; CC Single-pass type I membrane protein {ECO:0000305}. 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; X05111; CAA28757.1; -; mRNA. DR EMBL; AABR07012723; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH474015; EDL85525.1; -; Genomic_DNA. DR EMBL; BC088164; AAH88164.1; -; mRNA. DR PIR; A33071; RWRTC2. DR RefSeq; NP_036962.2; NM_012830.2. DR PDB; 1A64; X-ray; 2.00 A; A/B=23-121. DR PDB; 1A6P; X-ray; 2.08 A; A/B=26-121. DR PDB; 1A7B; X-ray; 3.10 A; A/B/C/D=23-121. DR PDB; 1CCZ; X-ray; 1.80 A; A=122-198. DR PDB; 1CDC; X-ray; 2.00 A; A/B=23-121. DR PDB; 1HNG; X-ray; 2.80 A; A/B=23-198. DR PDB; 1T6W; NMR; -; A=23-121. DR PDB; 2DRU; X-ray; 2.60 A; A=121-197. DR AlphaFoldDB; P08921; -. DR BMRB; P08921; -. DR SMR; P08921; -. DR FunCoup; P08921; 277. DR IntAct; P08921; 1. DR MINT; P08921; -. DR STRING; 10116.ENSRNOP00000021268; -. DR GlyCosmos; P08921; 3 sites, No reported glycans. DR GlyGen; P08921; 3 sites. DR iPTMnet; P08921; -. DR PhosphoSitePlus; P08921; -. DR PaxDb; 10116-ENSRNOP00000021268; -. DR ABCD; P08921; 1 sequenced antibody. DR Ensembl; ENSRNOT00000021268.9; ENSRNOP00000021268.6; ENSRNOG00000015821.9. DR Ensembl; ENSRNOT00055033626; ENSRNOP00055027276; ENSRNOG00055019708. DR Ensembl; ENSRNOT00060021542; ENSRNOP00060017024; ENSRNOG00060012683. DR Ensembl; ENSRNOT00065055828; ENSRNOP00065045983; ENSRNOG00065032445. DR GeneID; 497761; -. DR KEGG; rno:497761; -. DR UCSC; RGD:2297; rat. DR AGR; RGD:2297; -. DR CTD; 914; -. DR RGD; 2297; Cd2. DR eggNOG; ENOG502S5UN; Eukaryota. DR GeneTree; ENSGT01030000234540; -. DR HOGENOM; CLU_069390_0_0_1; -. DR InParanoid; P08921; -. DR OMA; DIPNFQM; -. DR OrthoDB; 8439544at2759; -. DR PhylomeDB; P08921; -. DR EvolutionaryTrace; P08921; -. DR PRO; PR:P08921; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000015821; Expressed in thymus and 17 other cell types or tissues. DR GO; GO:0009986; C:cell surface; IDA:RGD. DR GO; GO:0005911; C:cell-cell junction; ISO:RGD. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD. DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD. DR GO; GO:0005576; C:extracellular region; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:RGD. DR GO; GO:0042802; F:identical protein binding; IPI:RGD. DR GO; GO:0019901; F:protein kinase binding; IPI:RGD. DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD. DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD. DR GO; GO:0098609; P:cell-cell adhesion; IMP:RGD. DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0030101; P:natural killer cell activation; ISO:RGD. DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISO:RGD. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD. DR GO; GO:0032729; P:positive regulation of type II interferon production; ISO:RGD. DR CDD; cd05775; IgV_CD2_like_N; 1. DR FunFam; 2.60.40.10:FF:001736; T-cell surface antigen CD2; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR015632; CD2. DR InterPro; IPR015631; CD2/SLAM_rcpt. 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 PANTHER; PTHR12080; SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE; 1. DR PANTHER; PTHR12080:SF54; T-CELL SURFACE ANTIGEN CD2; 1. DR Pfam; PF05790; C2-set; 1. DR Pfam; PF07686; V-set; 1. DR PRINTS; PR01870; CD2ANTIGEN. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PDBsum; 1A64; -. DR PDBsum; 1A6P; -. DR PDBsum; 1A7B; -. DR PDBsum; 1CCZ; -. DR PDBsum; 1CDC; -. DR PDBsum; 1HNG; -. DR PDBsum; 1T6W; -. DR PDBsum; 2DRU; -. PE 1: Evidence at protein level; KW 3D-structure; Cell adhesion; Cell membrane; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..22 FT CHAIN 23..344 FT /note="T-cell surface antigen CD2" FT /id="PRO_0000014603" FT TOPO_DOM 23..202 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 203..228 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 229..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 99..113 FT /note="CD58 binding region 2" FT /evidence="ECO:0000250|UniProtKB:P06729" FT REGION 237..344 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 259..273 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 296..307 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 320..332 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 99 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 106 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 134 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16803907" FT DISULFID 132..196 FT /evidence="ECO:0000269|PubMed:1279440, FT ECO:0000269|PubMed:16803907, ECO:0007744|PDB:1HNG" FT DISULFID 139..179 FT /evidence="ECO:0000269|PubMed:1279440, FT ECO:0000269|PubMed:16803907, ECO:0007744|PDB:1HNG" FT CONFLICT 112 FT /note="N -> D (in Ref. 1; CAA28757)" FT STRAND 27..31 FT /evidence="ECO:0007829|PDB:1A64" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:1A64" FT STRAND 49..56 FT /evidence="ECO:0007829|PDB:1A64" FT STRAND 59..67 FT /evidence="ECO:0007829|PDB:1A64" FT STRAND 71..74 FT /evidence="ECO:0007829|PDB:1A64" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:1A64" FT STRAND 85..89 FT /evidence="ECO:0007829|PDB:1A64" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:1A64" FT STRAND 96..104 FT /evidence="ECO:0007829|PDB:1A64" FT STRAND 109..120 FT /evidence="ECO:0007829|PDB:1A64" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:2DRU" FT STRAND 127..131 FT /evidence="ECO:0007829|PDB:1CCZ" FT TURN 132..135 FT /evidence="ECO:0007829|PDB:1CCZ" FT STRAND 136..140 FT /evidence="ECO:0007829|PDB:1CCZ" FT STRAND 148..153 FT /evidence="ECO:0007829|PDB:1CCZ" FT STRAND 156..169 FT /evidence="ECO:0007829|PDB:1CCZ" FT STRAND 177..183 FT /evidence="ECO:0007829|PDB:1CCZ" FT STRAND 186..192 FT /evidence="ECO:0007829|PDB:1CCZ" SQ SEQUENCE 344 AA; 38413 MW; FE2CB45CBF2E5FA5 CRC64; MRCKFLGSFF LLFSLSSKGA DCRDSGTVWG ALGHGINLNI PNFQMTDDID EVRWERGSTL VAEFKRKMKP FLKSGAFEIL ANGDLKIKNL TRDDSGTYNV TVYSTNGTRI LNKALDLRIL EMVSKPMIYW ECSNATLTCE VLEGTDVELK LYQGKEHLRS LRQKTMSYQW TNLRAPFKCK AVNRVSQESE MEVVNCPEKG LPLYLIVGVS AGGLLLVFFG ALFIFCICKR KKRNRRRKGE ELEIKASRMS TVERGPKPHS TQASAPASQN PVASQAPPPP GHHLQTPGHR PLPPSHRNRE HQPKKRPPPS GTQVHQQKGP PLPRPRVQPK PPCGSGDVSL PPPN //