CD2_HORSE
ID CD2_HORSE Reviewed; 347 AA.
AC P37998;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=T-cell surface antigen CD2;
DE AltName: CD_antigen=CD2;
DE Flags: Precursor;
GN Name=CD2;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP 3D-STRUCTURE MODELING.
RC TISSUE=T-cell;
RX PubMed=7906650; DOI=10.1111/j.1432-1033.1994.tb18579.x;
RA Tavernor A.S., Kydd J.H., Bodian D.L., Jones E.Y., Stuart D.I., Davis S.J.,
RA Butcher G.W.;
RT "Expression cloning of an equine T-lymphocyte glycoprotein CD2 cDNA.
RT Structure-based analysis of conserved sequence elements.";
RL Eur. J. Biochem. 219:969-976(1994).
CC -!- FUNCTION: CD2 interacts with lymphocyte function-associated antigen
CC CD58 (LFA-3) to mediate adhesion between T-cells and other cell types.
CC CD2 is implicated in the triggering of T-cells, the cytoplasmic domain
CC is implicated in the signaling function.
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:0000269|PubMed:7906650};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen and thymus.
CC {ECO:0000269|PubMed:7906650}.
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DR EMBL; X69884; CAA49511.1; -; mRNA.
DR PIR; S41638; S41638.
DR RefSeq; NP_001078903.1; NM_001085434.1.
DR AlphaFoldDB; P37998; -.
DR SMR; P37998; -.
DR ELM; P37998; -.
DR IntAct; P37998; 1.
DR MINT; P37998; -.
DR STRING; 9796.ENSECAP00000017053; -.
DR PaxDb; P37998; -.
DR PRIDE; P37998; -.
DR Ensembl; ENSECAT00000020758; ENSECAP00000017053; ENSECAG00000019437.
DR GeneID; 100034205; -.
DR KEGG; ecb:100034205; -.
DR CTD; 914; -.
DR VGNC; VGNC:16249; CD2.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_069390_0_0_1; -.
DR InParanoid; P37998; -.
DR OMA; YCIRRKK; -.
DR OrthoDB; 977841at2759; -.
DR TreeFam; TF335971; -.
DR Proteomes; UP000002281; Chromosome 5.
DR Bgee; ENSECAG00000019437; Expressed in leukocyte and 18 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IBA:GO_Central.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0042110; P:T cell activation; IBA:GO_Central.
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..347
FT /note="T-cell surface antigen CD2"
FT /id="PRO_0000014599"
FT TOPO_DOM 25..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..123
FT /note="Ig-like V-type"
FT DOMAIN 124..199
FT /note="Ig-like C2-type"
FT REPEAT 283..289
FT /note="1"
FT REPEAT 290..296
FT /note="2"
FT REPEAT 297..303
FT /note="3"
FT REGION 58..70
FT /note="CD58 binding region 1"
FT /evidence="ECO:0000250|UniProtKB:P06729"
FT REGION 101..115
FT /note="CD58 binding region 2"
FT /evidence="ECO:0000250|UniProtKB:P06729"
FT REGION 252..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..303
FT /note="3 X 7 AA tandem repeats of H-R-P-[QL]-[AVP]-P-G"
FT COMPBIAS 271..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 134..199
FT /evidence="ECO:0000250|UniProtKB:P08921"
FT DISULFID 141..182
FT /evidence="ECO:0000250|UniProtKB:P08921"
SQ SEQUENCE 347 AA; 38864 MW; 0529606A2783D5E7 CRC64;
MNLACKLLAS FLLIFFFSSK GAVSKKNITI LGALERDINL DIPAFQMSEH VEDIQWSKGK
TKIAKFKNGS MTFQKDKTYE VLKNGTLKIK HLERIHEGTY KVDAYDSDGK NVLEETFHLS
LLEMVSKPNI SWSCTNTTLT CEVTKGTDFE LKLYLNGRMI QKSPRKVIVY KRASNQIASF
KCTANNTVSE ESSSVVIRCT EKGLDIYLIS GICGGGIILF VFLALLIFYI SKRKKQNSRR
NDEELEIRAH KVISEERGRK PHQIPGSTPL NPAASQPPPP PSHRPQAPGH RPQVPGHRPL
PPGHRVQHQQ QKRPAPTPGT QAHQQKGPPL PRPRVQPKPP RGATENS
