CD48_MOUSE
ID CD48_MOUSE Reviewed; 240 AA.
AC P18181; Q545K2;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=CD48 antigen;
DE AltName: Full=BCM1 surface antigen;
DE AltName: Full=BLAST-1;
DE AltName: Full=HM48-1;
DE AltName: Full=MRC OX-45 surface antigen;
DE AltName: Full=SLAM family member 2;
DE Short=SLAMF2;
DE AltName: Full=Signaling lymphocytic activation molecule 2;
DE AltName: Full=sgp-60;
DE AltName: CD_antigen=CD48;
DE Flags: Precursor;
GN Name=Cd48; Synonyms=Bcm-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GPI-ANCHOR AT SER-217, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=1693656; DOI=10.1084/jem.171.6.2115;
RA Wong Y.W., Williams A.F., Kingsmore S.F., Seldin M.F.;
RT "Structure, expression, and genetic linkage of the mouse BCM1 (OX45 or
RT Blast-1) antigen. Evidence for genetic duplication giving rise to the BCM1
RT region on mouse chromosome 1 and the CD2/LFA3 region on mouse chromosome
RT 3.";
RL J. Exp. Med. 171:2115-2130(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Lung, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 74-80.
RX PubMed=8475091; DOI=10.1073/pnas.90.8.3418;
RA Cabrero J.G., Freeman G.J., Lane W.S., Reiser H.;
RT "Identification, by protein sequencing and gene transfection, of sgp-60 as
RT the murine homologue of CD48.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3418-3422(1993).
RN [4]
RP PROTEIN SEQUENCE OF 23-40, INTERACTION WITH CD2, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=1383383; DOI=10.1084/jem.176.5.1241;
RA Kato K., Koyanagi M., Okada H., Takanahi T., Wong Y.W., Williams A.F.,
RA Okumura K., Yagita H.;
RT "CD48 is a counter-receptor for mouse CD2 and is involved in T cell
RT activation.";
RL J. Exp. Med. 176:1241-1249(1992).
RN [5]
RP FUNCTION, AND INTERACTION WITH LCK.
RX PubMed=9881969; DOI=10.1016/s1074-7613(00)80644-5;
RA Moran M., Miceli M.C.;
RT "Engagement of GPI-linked CD48 contributes to TCR signals and cytoskeletal
RT reorganization: a role for lipid rafts in T cell activation.";
RL Immunity 9:787-796(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21278219; DOI=10.1093/intimm/dxq465;
RA Keszei M., Latchman Y.E., Vanguri V.K., Brown D.R., Detre C., Morra M.,
RA Arancibia-Carcamo C.V., Arancibia C.V., Paul E., Calpe S., Castro W.,
RA Wang N., Terhorst C., Sharpe A.H.;
RT "Auto-antibody production and glomerulonephritis in congenic Slamf1-/- and
RT Slamf2-/- [B6.129] but not in Slamf1-/- and Slamf2-/- [BALB/c.129] mice.";
RL Int. Immunol. 23:149-158(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 27-128 ALONE AND IN COMPLEX WITH
RP CD244.
RX PubMed=17950006; DOI=10.1016/j.immuni.2007.08.019;
RA Velikovsky C.A., Deng L., Chlewicki L.K., Fernandez M.M., Kumar V.,
RA Mariuzza R.A.;
RT "Structure of natural killer receptor 2B4 bound to CD48 reveals basis for
RT heterophilic recognition in signaling lymphocyte activation molecule
RT family.";
RL Immunity 27:572-584(2007).
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 (PubMed:9881969, PubMed:21278219).
CC Participates in T-cell signaling transduction by associating with CD2
CC and efficiently bringing the Src family protein kinase LCK and LAT to
CC the TCR/CD3 complex. In turn, promotes LCK phosphorylation and
CC subsequent activation (PubMed:9881969). Induces the phosphorylation of
CC the cytoplasmic immunoreceptortyrosine switch motifs (ITSMs) of CD244
CC initiating a series of signaling events that leads to the generation of
CC the immunological synapse and the directed release of cytolytic
CC granules containing perforin and granzymes by T-lymphocytes and NK-
CC cells (By similarity) (PubMed:9881969, PubMed:21278219).
CC {ECO:0000250|UniProtKB:P09326, ECO:0000269|PubMed:21278219,
CC ECO:0000269|PubMed:9881969}.
CC -!- SUBUNIT: Interacts with CD2 (PubMed:1383383). Interacts with CD244
CC (PubMed:17950006). Interacts with LCK (By similarity).
CC {ECO:0000250|UniProtKB:P09326, ECO:0000269|PubMed:1383383,
CC ECO:0000269|PubMed:17950006}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1383383};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1693656}. Secreted
CC {ECO:0000250|UniProtKB:P09326}.
CC -!- DISRUPTION PHENOTYPE: Deletion mice do not develop signs of
CC autoimmunity, but exhibit defects in induction of tolerance.
CC {ECO:0000269|PubMed:21278219}.
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DR EMBL; X53526; CAA37604.1; -; mRNA.
DR EMBL; X17501; CAA35542.1; -; mRNA.
DR EMBL; AK007741; BAB25228.1; -; mRNA.
DR EMBL; AK084984; BAC39328.1; -; mRNA.
DR EMBL; AK151601; BAE30541.1; -; mRNA.
DR CCDS; CCDS15501.1; -.
DR PIR; JL0143; JL0143.
DR RefSeq; NP_031675.1; NM_007649.4.
DR PDB; 2PTT; X-ray; 1.63 A; A=27-128.
DR PDB; 2PTV; X-ray; 1.66 A; A=27-128.
DR PDBsum; 2PTT; -.
DR PDBsum; 2PTV; -.
DR AlphaFoldDB; P18181; -.
DR SMR; P18181; -.
DR STRING; 10090.ENSMUSP00000064241; -.
DR GlyGen; P18181; 6 sites.
DR PhosphoSitePlus; P18181; -.
DR SwissPalm; P18181; -.
DR CPTAC; non-CPTAC-4020; -.
DR EPD; P18181; -.
DR MaxQB; P18181; -.
DR PaxDb; P18181; -.
DR PeptideAtlas; P18181; -.
DR PRIDE; P18181; -.
DR ProteomicsDB; 281137; -.
DR Antibodypedia; 3737; 1150 antibodies from 47 providers.
DR DNASU; 12506; -.
DR Ensembl; ENSMUST00000068584; ENSMUSP00000064241; ENSMUSG00000015355.
DR GeneID; 12506; -.
DR KEGG; mmu:12506; -.
DR UCSC; uc007doz.1; mouse.
DR CTD; 962; -.
DR MGI; MGI:88339; Cd48.
DR VEuPathDB; HostDB:ENSMUSG00000015355; -.
DR eggNOG; ENOG502SB68; Eukaryota.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_099885_0_0_1; -.
DR InParanoid; P18181; -.
DR OMA; YFNTKFK; -.
DR OrthoDB; 986849at2759; -.
DR PhylomeDB; P18181; -.
DR TreeFam; TF334964; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 12506; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Cd48; mouse.
DR EvolutionaryTrace; P18181; -.
DR PRO; PR:P18181; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P18181; protein.
DR Bgee; ENSMUSG00000015355; Expressed in mesenteric lymph node and 111 other tissues.
DR ExpressionAtlas; P18181; baseline and differential.
DR Genevisible; P18181; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003823; F:antigen binding; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0045576; P:mast cell activation; ISO:MGI.
DR GO; GO:0002819; P:regulation of adaptive immune response; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IDA:MGI.
DR GO; GO:0042110; P:T cell activation; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR033548; CD48.
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:SF47; PTHR12080:SF47; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 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 /evidence="ECO:0000269|PubMed:1383383"
FT CHAIN 23..217
FT /note="CD48 antigen"
FT /id="PRO_0000014883"
FT PROPEP 218..240
FT /note="Removed in mature form"
FT /id="PRO_0000014884"
FT DOMAIN 29..125
FT /note="Ig-like C2-type 1"
FT DOMAIN 129..209
FT /note="Ig-like C2-type 2"
FT LIPID 217
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000269|PubMed:1693656"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
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 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2PTT"
FT TURN 79..83
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2PTT"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2PTT"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 104..115
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:2PTT"
SQ SEQUENCE 240 AA; 27383 MW; F3BF6987A9E9C71E CRC64;
MCFIKQGWCL VLELLLLPLG TGFQGHSIPD INATTGSNVT LKIHKDPLGP YKRITWLHTK
NQKILEYNYN STKTIFESEF KGRVYLEENN GALHISNVRK EDKGTYYMRV LRETENELKI
TLEVFDPVPK PSIEINKTEA STDSCHLRLS CEVKDQHVDY TWYESSGPFP KKSPGYVLDL
IVTPQNKSTF YTCQVSNPVS SKNDTVYFTL PCDLARSSGV CWTATWLVVT TLIIHRILLT
