CD2_RAT
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 03-AUG-2022, entry version 182.
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_036962.1; NM_012830.1.
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=121-199.
DR PDBsum; 1A64; -.
DR PDBsum; 1A6P; -.
DR PDBsum; 1A7B; -.
DR PDBsum; 1CCZ; -.
DR PDBsum; 1CDC; -.
DR PDBsum; 1HNG; -.
DR PDBsum; 1T6W; -.
DR PDBsum; 2DRU; -.
DR AlphaFoldDB; P08921; -.
DR BMRB; P08921; -.
DR SMR; P08921; -.
DR IntAct; P08921; 1.
DR MINT; P08921; -.
DR STRING; 10116.ENSRNOP00000021268; -.
DR GlyGen; P08921; 3 sites.
DR iPTMnet; P08921; -.
DR PhosphoSitePlus; P08921; -.
DR PaxDb; P08921; -.
DR ABCD; P08921; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000021268; ENSRNOP00000021268; ENSRNOG00000015821.
DR GeneID; 497761; -.
DR KEGG; rno:497761; -.
DR UCSC; RGD:2297; rat.
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; YCIRRKK; -.
DR OrthoDB; 977841at2759; -.
DR PhylomeDB; P08921; -.
DR EvolutionaryTrace; P08921; -.
DR PRO; PR:P08921; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Proteomes; UP000234681; Chromosome 2.
DR Bgee; ENSRNOG00000015821; Expressed in thymus and 17 other tissues.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:RGD.
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:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:0043621; F:protein self-association; IDA: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:0030101; P:natural killer cell activation; ISO:RGD.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; 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:0042110; P:T cell activation; IMP:RGD.
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 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 237..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..344
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 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
