(data stored in ACNUC22665 zone)

HOGENOM: RAT2_PE1531

ID   RAT2_PE1531                          STANDARD;      PRT;   344 AA.
AC   RAT2_PE1531; P08921;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=T-cell surface antigen CD2;AltName: Full=LFA-2;AltName:
DE   Full=LFA-3 receptor;AltName: Full=OX-34 antigen;AltName: Full=T-cell
DE   surface antigen T11/Leu-5;AltName: CD_antigen=CD2;Flags: Precursor;
DE   (RAT2.PE1531).
GN   Name=Cd2;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT2.PE1531.
CC       Rattus norvegicus chromosome 2 RGSC3.4  sequence 1..258207540
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:CD2_RAT
CC   -!- FUNCTION: CD2 interacts with lymphocyte function-associated
CC       antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells
CC       and other cell types. CD2 is implicated in the triggering of T-
CC       cells, the cytoplasmic domain is implicated in the signaling
CC       function.
CC   -!- SUBUNIT: Interacts with CD2AP and PSTPIP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -!- GENE_FAMILY: HOG000276890 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000015821;ENSRNOT00000021268;ENSRNOP00000021268.
DR   EMBL; BC088164; - ;
DR   EMBL; CH474015; - ;
DR   EMBL; X05111; - ;
DR   UniProtKB/Swiss-Prot; P08921; -.
DR   EMBL; X05111; CAA28757.1; -; mRNA.
DR   IPI; IPI00566418; -.
DR   PIR; A33071; RWRTC2.
DR   RefSeq; NP_036962.1; NM_012830.1.
DR   UniGene; Rn.10328; -.
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; 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   PDBsum; 1A64; -.
DR   PDBsum; 1A6P; -.
DR   PDBsum; 1A7B; -.
DR   PDBsum; 1CDC; -.
DR   PDBsum; 1HNG; -.
DR   PDBsum; 1T6W; -.
DR   ProteinModelPortal; P08921; -.
DR   SMR; P08921; 24-198.
DR   MINT; MINT-1514111; -.
DR   STRING; P08921; -.
DR   PRIDE; P08921; -.
DR   GeneID; 497761; -.
DR   KEGG; rno:497761; -.
DR   CTD; 914; -.
DR   RGD; 2297; Cd2.
DR   eggNOG; roNOG16173; -.
DR   NextBio; 697752; -.
DR   ArrayExpress; P08921; -.
DR   Genevestigator; P08921; -.
DR   GermOnline; ENSRNOG00000015821; Rattus norvegicus.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; IDA:RGD.
DR   GO; GO:0043234; C:protein complex; IDA:RGD.
DR   GO; GO:0003823; F:antigen binding; IMP:RGD.
DR   GO; GO:0001948; F:glycoprotein binding; IPI:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA: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:0016337; P:cell-cell adhesion; IMP:RGD.
DR   GO; GO:0042110; P:T cell activation; IMP:RGD.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008424; Ig_C2-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR015631; Signal_lymphocyte_activ_molc.
DR   InterPro; IPR015632; T-cell_sdhesion_molc_CD2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   PANTHER; PTHR12080:SF10; CD2_pre; 1.
DR   PANTHER; PTHR12080; SLAM_related; 1.
DR   Pfam; PF05790; C2-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   PRINTS; PR01870; CD2ANTIGEN.
DR   SMART; SM00409; IG; 1.
DR   PROSITE; PS50835; IG_LIKE; FALSE_NEG.
DR   HOGENOMDNA; RAT2.PE1531; -.
KW   ENSRNOG00000015821820036002503210000011;
KW   Cd2; CD2_RAT; Q5I0M6_RAT; BC088164; CH474015; X05111;
KW   3D-structure; Cell adhesion; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   344 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRCKFLGSFF LLFSLSSKGA DCRDSGTVWG ALGHGINLNI PNFQMTDDID EVRWERGSTL
     VAEFKRKMKP FLKSGAFEIL ANGDLKIKNL TRDDSGTYNV TVYSTNGTRI LNKALDLRIL
     EMVSKPMIYW ECSNATLTCE VLEGTDVELK LYQGKEHLRS LRQKTMSYQW TNLRAPFKCK
     AVNRVSQESE MEVVNCPEKG LPLYLIVGVS AGGLLLVFFG ALFIFCICKR KKRNRRRKVI
     EFIIKXSRMS TVERGPKPHS TQASAPASQN PVASQAPPPP GHHLQTPGHR PLPPSHRNRE
     HQPKKRPPPS GTQVHQQKGP PLPRPRVQPK PPCGSGDVSL PPPN
//

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