ID CD48_RAT Reviewed; 240 AA.
AC P10252;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 24-JAN-2024, entry version 177.
DE RecName: Full=CD48 antigen;
DE AltName: Full=BCM1 surface antigen;
DE AltName: Full=BLAST-1;
DE AltName: Full=MRC OX-45 surface antigen {ECO:0000303|PubMed:3181129};
DE AltName: Full=SLAM family member 2;
DE Short=SLAMF2;
DE AltName: Full=Signaling lymphocytic activation molecule 2;
DE AltName: CD_antigen=CD48;
DE Flags: Precursor;
GN Name=Cd48; Synonyms=Bcm-1;
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, GLYCOSYLATION AT
RP ASN-186 AND ASN-203, SUBCELLULAR LOCATION, GPI-ANCHOR AT SER-217, AND
RP DISULFIDE BOND.
RX PubMed=3181129; DOI=10.1002/j.1460-2075.1988.tb03174.x;
RA Killeen N., Moessner R., Arvieux J., Willis A., Williams A.F.;
RT "The MRC OX-45 antigen of rat leukocytes and endothelium is in a subset of
RT the immunoglobulin superfamily with CD2, LFA-3 and carcinoembryonic
RT antigens.";
RL EMBO J. 7:3087-3091(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 23-125 IN COMPLEX WITH CD2,
RP INTERACTION WITH CD2 AND CD244, AND GLYCOSYLATION AT ASN-38 AND ASN-97.
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: Glycosylphosphatidylinositol (GPI)-anchored cell surface
CC glycoprotein that interacts via its N-terminal immunoglobulin domain
CC with cell surface receptors including 2B4/CD244 or CD2 to regulate
CC immune cell function and activation. Participates in T-cell signaling
CC transduction by associating with CD2 and efficiently bringing the Src
CC family protein kinase LCK and LAT to the TCR/CD3 complex. In turn,
CC promotes LCK phosphorylation and subsequent activation. Induces the
CC phosphorylation of the cytoplasmic immunoreceptortyrosine switch motifs
CC (ITSMs) of CD244 initiating a series of signaling events that leads to
CC the generation of the immunological synapse and the directed release of
CC cytolytic granules containing perforin and granzymes by T-lymphocytes
CC and NK-cells. {ECO:0000250|UniProtKB:P09326}.
CC -!- SUBUNIT: Interacts with CD2 (PubMed:16803907). Interacts with CD244
CC (PubMed:16803907). Interacts with LCK (By similarity).
CC {ECO:0000250|UniProtKB:P09326, ECO:0000269|PubMed:16803907}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3181129};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:3181129}. Secreted
CC {ECO:0000250|UniProtKB:P09326}.
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DR EMBL; X13016; CAA31438.1; -; mRNA.
DR EMBL; BC060542; AAH60542.1; -; mRNA.
DR PIR; S01299; S01299.
DR RefSeq; NP_620803.1; NM_139103.1.
DR PDB; 2DRU; X-ray; 2.60 A; A=23-125.
DR PDBsum; 2DRU; -.
DR AlphaFoldDB; P10252; -.
DR SMR; P10252; -.
DR STRING; 10116.ENSRNOP00000006306; -.
DR GlyConnect; 371; 18 N-Linked glycans.
DR GlyCosmos; P10252; 5 sites, 34 glycans.
DR GlyGen; P10252; 6 sites, 34 N-linked glycans (1 site).
DR iPTMnet; P10252; -.
DR PhosphoSitePlus; P10252; -.
DR PaxDb; 10116-ENSRNOP00000006306; -.
DR Ensembl; ENSRNOT00055039343; ENSRNOP00055031922; ENSRNOG00055022901.
DR Ensembl; ENSRNOT00060032634; ENSRNOP00060026637; ENSRNOG00060018849.
DR Ensembl; ENSRNOT00065041358; ENSRNOP00065033781; ENSRNOG00065024081.
DR GeneID; 245962; -.
DR KEGG; rno:245962; -.
DR UCSC; RGD:620620; rat.
DR AGR; RGD:620620; -.
DR CTD; 962; -.
DR RGD; 620620; Cd48.
DR VEuPathDB; HostDB:ENSRNOG00000004737; -.
DR eggNOG; ENOG502SB68; Eukaryota.
DR HOGENOM; CLU_099885_0_0_1; -.
DR InParanoid; P10252; -.
DR OrthoDB; 5265418at2759; -.
DR PhylomeDB; P10252; -.
DR TreeFam; TF334964; -.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR EvolutionaryTrace; P10252; -.
DR PRO; PR:P10252; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000004737; Expressed in lung and 20 other cell types or tissues.
DR Genevisible; P10252; RN.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045576; P:mast cell activation; IMP:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0042110; P:T cell activation; ISO:RGD.
DR CDD; cd05775; IgV_CD2_like_N; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR12080:SF105; CD48 ANTIGEN; 1.
DR PANTHER; PTHR12080; SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT CHAIN 23..217
FT /note="CD48 antigen"
FT /id="PRO_0000014885"
FT PROPEP 218..240
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000014886"
FT DOMAIN 29..127
FT /note="Ig-like C2-type 1"
FT DOMAIN 131..207
FT /note="Ig-like C2-type 2"
FT LIPID 217
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000269|PubMed:3181129"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16803907"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16803907"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3181129"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3181129"
FT DISULFID 151..193
FT /evidence="ECO:0000269|PubMed:3181129"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:2DRU"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2DRU"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:2DRU"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2DRU"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2DRU"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2DRU"
FT TURN 79..83
FT /evidence="ECO:0007829|PDB:2DRU"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2DRU"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2DRU"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2DRU"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2DRU"
FT STRAND 104..125
FT /evidence="ECO:0007829|PDB:2DRU"
SQ SEQUENCE 240 AA; 27680 MW; 42CBBF9947A0E437 CRC64;
MYFKKRRWFL ILESLLLSLV TGFQDQSVPN VNAITGSNVT LTILKHPLAS YQRLTWLHTT
NQKILEYFPN GKKTVFESVF KDRVDLDKTN GALRIYNVSK EDRGDYYMRM LHETEDQWKI
TMEVYDLVSK PAIKIEKTKN LTDSCHLRLS CKVEDQGVDY TWYEDSGPFP QRNPGYVLEI
TITPHNKSTF YTCQVSNPVS SENDTLYFIP PCTLARSSGV HWIAAWLVVT LSIIPSILLA
//
