Full text data of CD58
CD58
(LFA3)
[Confidence: high (present in two of the MS resources)]
Lymphocyte function-associated antigen 3; Ag3 (Surface glycoprotein LFA-3; CD58; Flags: Precursor)
Lymphocyte function-associated antigen 3; Ag3 (Surface glycoprotein LFA-3; CD58; Flags: Precursor)
hRBCD
IPI00000059
IPI00000059 LFA-3 LFA-3 membrane n/a n/a n/a 1 1 n/a 1 n/a 4 n/a 1 1 n/a n/a n/a 1 1 1 1 1 integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00000059 LFA-3 LFA-3 membrane n/a n/a n/a 1 1 n/a 1 n/a 4 n/a 1 1 n/a n/a n/a 1 1 1 1 1 integral membrane protein n/a found at its expected molecular weight found at molecular weight
Comments
Isoform P19256-2 was detected.
Isoform P19256-2 was detected.
UniProt
P19256
ID LFA3_HUMAN Reviewed; 250 AA.
AC P19256; A8K7G5; Q5U053; Q6IB65; Q96KI9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1990, sequence version 1.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=Lymphocyte function-associated antigen 3;
DE Short=Ag3;
DE AltName: Full=Surface glycoprotein LFA-3;
DE AltName: CD_antigen=CD58;
DE Flags: Precursor;
GN Name=CD58; Synonyms=LFA3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP INTERACTION WITH CD2.
RC TISSUE=Erythrocyte;
RX PubMed=3309127; DOI=10.1084/jem.166.4.923;
RA Wallner B.P., Frey A.Z., Tizard R., Mattaliano R.J., Hession C.,
RA Sanders M.E., Dustin M.L., Springer T.A.;
RT "Primary structure of lymphocyte function-associated antigen 3 (LFA-
RT 3). The ligand of the T lymphocyte CD2 glycoprotein.";
RL J. Exp. Med. 166:923-932(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=3313052; DOI=10.1038/329840a0;
RA Seed B.;
RT "An LFA-3 cDNA encodes a phospholipid-linked membrane protein
RT homologous to its receptor CD2.";
RL Nature 329:840-842(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=9510189;
RA Wallich R., Brenner C., Brand Y., Roux M., Reister M., Meuer S.;
RT "Gene structure, promoter characterization, and basis for alternative
RT mRNA splicing of the human CD58 gene.";
RL J. Immunol. 160:2862-2871(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [10]
RP GPI-ANCHOR [LARGE SCALE ANALYSIS] (ISOFORM 2), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16602701; DOI=10.1021/pr050419u;
RA Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,
RA Brodbeck U., Peck S.C., Jensen O.N.;
RT "Modification-specific proteomics of plasma membrane proteins:
RT identification and characterization of glycosylphosphatidylinositol-
RT anchored proteins released upon phospholipase D treatment.";
RL J. Proteome Res. 5:935-943(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 29-123 IN COMPLEX WITH CD2,
RP AND MUTAGENESIS OF PHE-29; VAL-37; VAL-49; VAL-86; THR-113 AND
RP LEU-121.
RX PubMed=10380930; DOI=10.1016/S0092-8674(00)80790-4;
RA Wang J.H., Smolyar A., Tan K., Liu J.H., Kim M., Sun Z.Y., Wagner G.,
RA Reinherz E.L.;
RT "Structure of a heterophilic adhesion complex between the human CD2
RT and CD58 (LFA-3) counterreceptors.";
RL Cell 97:791-803(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-122.
RX PubMed=10200255; DOI=10.1073/pnas.96.8.4289;
RA Ikemizu S., Sparks L.M., van der Merwe P.A., Harlos K., Stuart D.I.,
RA Jones E.Y., Davis S.J.;
RT "Crystal structure of the CD2-binding domain of CD58 (lymphocyte
RT function-associated antigen 3) at 1.8-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4289-4294(1999).
CC -!- FUNCTION: Ligand of the T-lymphocyte CD2 glycoprotein. This
CC interaction is important in mediating thymocyte interactions with
CC thymic epithelial cells, antigen-independent and -dependent
CC interactions of T-lymphocytes with target cells and antigen-
CC presenting cells and the T-lymphocyte rosetting with erythrocytes.
CC In addition, the LFA-3/CD2 interaction may prime response by both
CC the CD2+ and LFA-3+ cells.
CC -!- SUBUNIT: Interacts with CD2.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Lipid-anchor, GPI-
CC anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=P19256-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P19256-2; Sequence=VSP_002522, VSP_002523;
CC Note=GPI-anchor amidated asparagine on Asn-235. May be produced
CC at very low levels due to a premature stop codon in the mRNA,
CC leading to nonsense-mediated mRNA decay;
CC Name=3;
CC IsoId=P19256-3; Sequence=VSP_038693;
CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Y00636; CAA68668.1; -; mRNA.
DR EMBL; X06296; CAA29622.1; -; mRNA.
DR EMBL; Y14780; CAA75083.1; -; Genomic_DNA.
DR EMBL; Y14781; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14782; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14783; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14784; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14780; CAA75084.1; -; Genomic_DNA.
DR EMBL; Y14781; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14782; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14783; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14784; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14785; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; AK291980; BAF84669.1; -; mRNA.
DR EMBL; CR456939; CAG33220.1; -; mRNA.
DR EMBL; BT019816; AAV38619.1; -; mRNA.
DR EMBL; BT019817; AAV38620.1; -; mRNA.
DR EMBL; AL390066; CAI19099.1; -; Genomic_DNA.
DR EMBL; AL355794; CAI19099.1; JOINED; Genomic_DNA.
DR EMBL; AL355794; CAI22762.1; -; Genomic_DNA.
DR EMBL; AL390066; CAI22762.1; JOINED; Genomic_DNA.
DR EMBL; CH471122; EAW56652.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56653.1; -; Genomic_DNA.
DR PIR; A28564; A28564.
DR RefSeq; NP_001138294.1; NM_001144822.1.
DR RefSeq; NP_001770.1; NM_001779.2.
DR UniGene; Hs.34341; -.
DR PDB; 1CCZ; X-ray; 1.80 A; A=29-122.
DR PDB; 1CI5; NMR; -; A=30-123.
DR PDB; 1QA9; X-ray; 3.20 A; B/D=29-123.
DR PDBsum; 1CCZ; -.
DR PDBsum; 1CI5; -.
DR PDBsum; 1QA9; -.
DR ProteinModelPortal; P19256; -.
DR SMR; P19256; 29-159.
DR IntAct; P19256; 4.
DR MINT; MINT-8201779; -.
DR STRING; 9606.ENSP00000358501; -.
DR ChEMBL; CHEMBL3790; -.
DR DMDM; 126225; -.
DR PaxDb; P19256; -.
DR PRIDE; P19256; -.
DR DNASU; 965; -.
DR Ensembl; ENST00000369489; ENSP00000358501; ENSG00000116815.
DR Ensembl; ENST00000457047; ENSP00000409080; ENSG00000116815.
DR Ensembl; ENST00000464088; ENSP00000432773; ENSG00000116815.
DR GeneID; 965; -.
DR KEGG; hsa:965; -.
DR UCSC; uc001egm.3; human.
DR CTD; 965; -.
DR GeneCards; GC01M117059; -.
DR HGNC; HGNC:1688; CD58.
DR MIM; 153420; gene.
DR neXtProt; NX_P19256; -.
DR PharmGKB; PA26227; -.
DR eggNOG; NOG76545; -.
DR HOGENOM; HOG000013140; -.
DR HOVERGEN; HBG003226; -.
DR InParanoid; P19256; -.
DR KO; K06492; -.
DR OMA; KDKVVEW; -.
DR OrthoDB; EOG7VHT02; -.
DR PhylomeDB; P19256; -.
DR Reactome; REACT_604; Hemostasis.
DR EvolutionaryTrace; P19256; -.
DR GenomeRNAi; 965; -.
DR NextBio; 4030; -.
DR PRO; PR:P19256; -.
DR ArrayExpress; P19256; -.
DR Bgee; P19256; -.
DR CleanEx; HS_CD58; -.
DR Genevestigator; P19256; -.
DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0016337; P:cell-cell adhesion; NAS:UniProtKB.
DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR015714; Lymphocyte_func-assoc_Ag_3.
DR PANTHER; PTHR21063:SF2; PTHR21063:SF2; 1.
DR SMART; SM00409; IG; 1.
DR PROSITE; PS50835; IG_LIKE; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Polymorphism;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 28
FT CHAIN 29 250 Lymphocyte function-associated antigen 3.
FT /FTId=PRO_0000014814.
FT TOPO_DOM 29 215 Extracellular (Potential).
FT TRANSMEM 216 238 Helical; (Potential).
FT TOPO_DOM 239 250 Cytoplasmic (Potential).
FT DOMAIN 30 121 Ig-like.
FT CARBOHYD 40 40 N-linked (GlcNAc...).
FT CARBOHYD 94 94 N-linked (GlcNAc...).
FT CARBOHYD 109 109 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 135 135 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 169 169 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 195 195 N-linked (GlcNAc...) (Potential).
FT DISULFID 142 187 By similarity.
FT VAR_SEQ 236 237 GI -> VL (in isoform 2).
FT /FTId=VSP_002522.
FT VAR_SEQ 238 250 Missing (in isoform 2).
FT /FTId=VSP_002523.
FT VAR_SEQ 248 250 NSN -> K (in isoform 3).
FT /FTId=VSP_038693.
FT VARIANT 15 15 S -> G (in dbSNP:rs17426456).
FT /FTId=VAR_049885.
FT MUTAGEN 29 29 F->S: No effect on CD2-binding.
FT MUTAGEN 37 37 V->K: No effect on CD2-binding.
FT MUTAGEN 49 49 V->Q: No effect on CD2-binding.
FT MUTAGEN 86 86 V->K: No effect on CD2-binding.
FT MUTAGEN 113 113 T->S: No effect on CD2-binding.
FT MUTAGEN 121 121 L->G: No effect on CD2-binding.
FT STRAND 30 36
FT STRAND 41 43
FT STRAND 54 58
FT STRAND 61 67
FT STRAND 70 73
FT HELIX 75 77
FT STRAND 80 83
FT TURN 85 87
FT STRAND 90 92
FT HELIX 97 99
FT STRAND 101 106
FT STRAND 114 121
SQ SEQUENCE 250 AA; 28147 MW; 34D635DF1D14FE2E CRC64;
MVAGSDAGRA LGVLSVVCLL HCFGFISCFS QQIYGVVYGN VTFHVPSNVP LKEVLWKKQK
DKVAELENSE FRAFSSFKNR VYLDTVSGSL TIYNLTSSDE DEYEMESPNI TDTMKFFLYV
LESLPSPTLT CALTNGSIEV QCMIPEHYNS HRGLIMYSWD CPMEQCKRNS TSIYFKMEND
LPQKIQCTLS NPLFNTTSSI ILTTCIPSSG HSRHRYALIP IPLAVITTCI VLYMNGILKC
DRKPDRTNSN
//
ID LFA3_HUMAN Reviewed; 250 AA.
AC P19256; A8K7G5; Q5U053; Q6IB65; Q96KI9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1990, sequence version 1.
DT 22-JAN-2014, entry version 145.
DE RecName: Full=Lymphocyte function-associated antigen 3;
DE Short=Ag3;
DE AltName: Full=Surface glycoprotein LFA-3;
DE AltName: CD_antigen=CD58;
DE Flags: Precursor;
GN Name=CD58; Synonyms=LFA3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP INTERACTION WITH CD2.
RC TISSUE=Erythrocyte;
RX PubMed=3309127; DOI=10.1084/jem.166.4.923;
RA Wallner B.P., Frey A.Z., Tizard R., Mattaliano R.J., Hession C.,
RA Sanders M.E., Dustin M.L., Springer T.A.;
RT "Primary structure of lymphocyte function-associated antigen 3 (LFA-
RT 3). The ligand of the T lymphocyte CD2 glycoprotein.";
RL J. Exp. Med. 166:923-932(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=3313052; DOI=10.1038/329840a0;
RA Seed B.;
RT "An LFA-3 cDNA encodes a phospholipid-linked membrane protein
RT homologous to its receptor CD2.";
RL Nature 329:840-842(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=9510189;
RA Wallich R., Brenner C., Brand Y., Roux M., Reister M., Meuer S.;
RT "Gene structure, promoter characterization, and basis for alternative
RT mRNA splicing of the human CD58 gene.";
RL J. Immunol. 160:2862-2871(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [10]
RP GPI-ANCHOR [LARGE SCALE ANALYSIS] (ISOFORM 2), AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16602701; DOI=10.1021/pr050419u;
RA Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,
RA Brodbeck U., Peck S.C., Jensen O.N.;
RT "Modification-specific proteomics of plasma membrane proteins:
RT identification and characterization of glycosylphosphatidylinositol-
RT anchored proteins released upon phospholipase D treatment.";
RL J. Proteome Res. 5:935-943(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 29-123 IN COMPLEX WITH CD2,
RP AND MUTAGENESIS OF PHE-29; VAL-37; VAL-49; VAL-86; THR-113 AND
RP LEU-121.
RX PubMed=10380930; DOI=10.1016/S0092-8674(00)80790-4;
RA Wang J.H., Smolyar A., Tan K., Liu J.H., Kim M., Sun Z.Y., Wagner G.,
RA Reinherz E.L.;
RT "Structure of a heterophilic adhesion complex between the human CD2
RT and CD58 (LFA-3) counterreceptors.";
RL Cell 97:791-803(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 29-122.
RX PubMed=10200255; DOI=10.1073/pnas.96.8.4289;
RA Ikemizu S., Sparks L.M., van der Merwe P.A., Harlos K., Stuart D.I.,
RA Jones E.Y., Davis S.J.;
RT "Crystal structure of the CD2-binding domain of CD58 (lymphocyte
RT function-associated antigen 3) at 1.8-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4289-4294(1999).
CC -!- FUNCTION: Ligand of the T-lymphocyte CD2 glycoprotein. This
CC interaction is important in mediating thymocyte interactions with
CC thymic epithelial cells, antigen-independent and -dependent
CC interactions of T-lymphocytes with target cells and antigen-
CC presenting cells and the T-lymphocyte rosetting with erythrocytes.
CC In addition, the LFA-3/CD2 interaction may prime response by both
CC the CD2+ and LFA-3+ cells.
CC -!- SUBUNIT: Interacts with CD2.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Lipid-anchor, GPI-
CC anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=P19256-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P19256-2; Sequence=VSP_002522, VSP_002523;
CC Note=GPI-anchor amidated asparagine on Asn-235. May be produced
CC at very low levels due to a premature stop codon in the mRNA,
CC leading to nonsense-mediated mRNA decay;
CC Name=3;
CC IsoId=P19256-3; Sequence=VSP_038693;
CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Y00636; CAA68668.1; -; mRNA.
DR EMBL; X06296; CAA29622.1; -; mRNA.
DR EMBL; Y14780; CAA75083.1; -; Genomic_DNA.
DR EMBL; Y14781; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14782; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14783; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14784; CAA75083.1; JOINED; Genomic_DNA.
DR EMBL; Y14780; CAA75084.1; -; Genomic_DNA.
DR EMBL; Y14781; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14782; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14783; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14784; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; Y14785; CAA75084.1; JOINED; Genomic_DNA.
DR EMBL; AK291980; BAF84669.1; -; mRNA.
DR EMBL; CR456939; CAG33220.1; -; mRNA.
DR EMBL; BT019816; AAV38619.1; -; mRNA.
DR EMBL; BT019817; AAV38620.1; -; mRNA.
DR EMBL; AL390066; CAI19099.1; -; Genomic_DNA.
DR EMBL; AL355794; CAI19099.1; JOINED; Genomic_DNA.
DR EMBL; AL355794; CAI22762.1; -; Genomic_DNA.
DR EMBL; AL390066; CAI22762.1; JOINED; Genomic_DNA.
DR EMBL; CH471122; EAW56652.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56653.1; -; Genomic_DNA.
DR PIR; A28564; A28564.
DR RefSeq; NP_001138294.1; NM_001144822.1.
DR RefSeq; NP_001770.1; NM_001779.2.
DR UniGene; Hs.34341; -.
DR PDB; 1CCZ; X-ray; 1.80 A; A=29-122.
DR PDB; 1CI5; NMR; -; A=30-123.
DR PDB; 1QA9; X-ray; 3.20 A; B/D=29-123.
DR PDBsum; 1CCZ; -.
DR PDBsum; 1CI5; -.
DR PDBsum; 1QA9; -.
DR ProteinModelPortal; P19256; -.
DR SMR; P19256; 29-159.
DR IntAct; P19256; 4.
DR MINT; MINT-8201779; -.
DR STRING; 9606.ENSP00000358501; -.
DR ChEMBL; CHEMBL3790; -.
DR DMDM; 126225; -.
DR PaxDb; P19256; -.
DR PRIDE; P19256; -.
DR DNASU; 965; -.
DR Ensembl; ENST00000369489; ENSP00000358501; ENSG00000116815.
DR Ensembl; ENST00000457047; ENSP00000409080; ENSG00000116815.
DR Ensembl; ENST00000464088; ENSP00000432773; ENSG00000116815.
DR GeneID; 965; -.
DR KEGG; hsa:965; -.
DR UCSC; uc001egm.3; human.
DR CTD; 965; -.
DR GeneCards; GC01M117059; -.
DR HGNC; HGNC:1688; CD58.
DR MIM; 153420; gene.
DR neXtProt; NX_P19256; -.
DR PharmGKB; PA26227; -.
DR eggNOG; NOG76545; -.
DR HOGENOM; HOG000013140; -.
DR HOVERGEN; HBG003226; -.
DR InParanoid; P19256; -.
DR KO; K06492; -.
DR OMA; KDKVVEW; -.
DR OrthoDB; EOG7VHT02; -.
DR PhylomeDB; P19256; -.
DR Reactome; REACT_604; Hemostasis.
DR EvolutionaryTrace; P19256; -.
DR GenomeRNAi; 965; -.
DR NextBio; 4030; -.
DR PRO; PR:P19256; -.
DR ArrayExpress; P19256; -.
DR Bgee; P19256; -.
DR CleanEx; HS_CD58; -.
DR Genevestigator; P19256; -.
DR GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0016337; P:cell-cell adhesion; NAS:UniProtKB.
DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR015714; Lymphocyte_func-assoc_Ag_3.
DR PANTHER; PTHR21063:SF2; PTHR21063:SF2; 1.
DR SMART; SM00409; IG; 1.
DR PROSITE; PS50835; IG_LIKE; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Polymorphism;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 28
FT CHAIN 29 250 Lymphocyte function-associated antigen 3.
FT /FTId=PRO_0000014814.
FT TOPO_DOM 29 215 Extracellular (Potential).
FT TRANSMEM 216 238 Helical; (Potential).
FT TOPO_DOM 239 250 Cytoplasmic (Potential).
FT DOMAIN 30 121 Ig-like.
FT CARBOHYD 40 40 N-linked (GlcNAc...).
FT CARBOHYD 94 94 N-linked (GlcNAc...).
FT CARBOHYD 109 109 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 135 135 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 169 169 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 195 195 N-linked (GlcNAc...) (Potential).
FT DISULFID 142 187 By similarity.
FT VAR_SEQ 236 237 GI -> VL (in isoform 2).
FT /FTId=VSP_002522.
FT VAR_SEQ 238 250 Missing (in isoform 2).
FT /FTId=VSP_002523.
FT VAR_SEQ 248 250 NSN -> K (in isoform 3).
FT /FTId=VSP_038693.
FT VARIANT 15 15 S -> G (in dbSNP:rs17426456).
FT /FTId=VAR_049885.
FT MUTAGEN 29 29 F->S: No effect on CD2-binding.
FT MUTAGEN 37 37 V->K: No effect on CD2-binding.
FT MUTAGEN 49 49 V->Q: No effect on CD2-binding.
FT MUTAGEN 86 86 V->K: No effect on CD2-binding.
FT MUTAGEN 113 113 T->S: No effect on CD2-binding.
FT MUTAGEN 121 121 L->G: No effect on CD2-binding.
FT STRAND 30 36
FT STRAND 41 43
FT STRAND 54 58
FT STRAND 61 67
FT STRAND 70 73
FT HELIX 75 77
FT STRAND 80 83
FT TURN 85 87
FT STRAND 90 92
FT HELIX 97 99
FT STRAND 101 106
FT STRAND 114 121
SQ SEQUENCE 250 AA; 28147 MW; 34D635DF1D14FE2E CRC64;
MVAGSDAGRA LGVLSVVCLL HCFGFISCFS QQIYGVVYGN VTFHVPSNVP LKEVLWKKQK
DKVAELENSE FRAFSSFKNR VYLDTVSGSL TIYNLTSSDE DEYEMESPNI TDTMKFFLYV
LESLPSPTLT CALTNGSIEV QCMIPEHYNS HRGLIMYSWD CPMEQCKRNS TSIYFKMEND
LPQKIQCTLS NPLFNTTSSI ILTTCIPSSG HSRHRYALIP IPLAVITTCI VLYMNGILKC
DRKPDRTNSN
//
MIM
153420
*RECORD*
*FIELD* NO
153420
*FIELD* TI
*153420 CD58 MOLECULE; CD58
;;LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN, TYPE 3; LFA3
read more*FIELD* TX
DESCRIPTION
The CD58 gene encodes a CD2 (186990) receptor. The presence of these 2
antigens on opposing cells optimizes immune recognition, facilitating
contacts between helper T lymphocytes and antigen-presenting cells as
well as between cytolytic effectors and target cells (Wang et al.,
1999).
CLONING
The LFA3 gene has been cloned (Barbosa, 1987).
Wallner et al. (1987) isolated the cDNA for CD58, which they called
LFA3, the ligand of the T lymphocyte CD2 molecule. The deduced protein
contains 222 amino acids and structurally resembles a typical
membrane-anchored protein. An extracellular domain with six N-linked
glycosylation sites is followed by a hydrophobic putative transmembrane
region and a short cytoplasmic domain. Northern blot analysis detected a
1.3-kb LFA3 transcript that was widely distributed in human tissues and
cell lines.
Sewell et al. (1988) noted that the amino acid sequences of the
extracellular domains of CD2 and CD58, which are predicted from their
cDNA sequences, show significant similarities, and both are members of
the immunoglobulin supergene family. They probably arose by duplication
of a common evolutionary precursor.
MAPPING
Barbosa et al. (1985, 1986) mapped the LFA3 gene to chromosome 1 by
study of mouse-human cell hybrids. There is some possibility that LFA3
is identical to the cell surface antigen identified by monoclonal
antibodies and known as MSK2 (158040). MSK1 (158030) maps to the short
arm of chromosome 1, and MSK2 to the long arm of chromosome 1.
By a combination of Southern blot analysis of somatic cell hybrid DNA
and in situ hybridization, Sewell et al. (1988) assigned the LFA3 gene
to chromosome 1p13, which is the same location as CD2.
BIOCHEMICAL FEATURES
- Crystal Structure
Wang et al. (1999) reported the crystal structure of the heterophilic
adhesion complex between the N-terminal domains of human CD2 and CD58 at
more than 3.2-angstrom resolution. A strikingly asymmetric, orthogonal,
face-to-face interaction involving the major beta sheets of the
respective immunoglobulin-like domains with poor shape complementarity
was revealed. These features explained CD2-CD58 dynamic binding,
offering insights into the interactions of related immunoglobulin
superfamily receptors.
MOLECULAR GENETICS
For a discussion of a possible association between variation in the CD58
gene and protection against multiple sclerosis, see MS (126200).
*FIELD* RF
1. Barbosa, J. A.: Personal Communication. West Haven, Conn. 1987.
2. Barbosa, J. A.; Mentzer, S. J.; Kamarck, M. E.; Hart, J.; Biro,
P. A.; Strominger, J. L.; Burakoff, S. J.: Gene mapping and somatic
cell hybrid analysis of the role of human lymphocyte function-associated
antigen-3 (LFA-3) in CTL-target cell interactions. J. Immun. 136:
3085-3091, 1986.
3. Barbosa, J. A.; Mentzer, S. J.; Kamarck, M. E.; Hart, J.; Strominger,
J. L.; Biro, P. A.; Burakoff, S. J.: Somatic cell hybrid analysis
of human lymphocyte function associated antigen-3 (LFA-3): gene mapping
and role in CTL-target cell interactions. ICSU Short Reports 2:
107-108, 1985.
4. Sewell, W. A.; Palmer, R. W.; Spurr, N. K.; Sheer, D.; Brown, M.
H.; Bell, Y.; Crumpton, M. J.: The human LFA-3 gene is located at
the same chromosome band as the gene for its receptor CD2. Immunogenetics 28:
278-282, 1988.
5. Wallner, B. P.; Frey, A. Z.; Tizard, R.; Mattaliano, R. J.; Hession,
C.; Sanders, M. E.; Dustin, M. L.; Springer, T. A.: Primary structure
of lymphocyte function-associated antigen 3 (LFA-3): the ligand of
the T lymphocyte CD2 glycoprotein. J. Exp. Med. 166: 923-932, 1987.
6. Wang, J.; Smolyar, A.; Tan, K.; Liu, J.; Kim, M.; Sun, Z. J.; Wagner,
G.; Reinherz, E. L.: Structure of a heterophilic adhesion complex
between the human CD2 and CD58 (LFA-3) counterreceptors. Cell 97:
791-803, 1999.
*FIELD* CN
Cassandra L. Kniffin - updated: 8/6/2009
Stylianos E. Antonarakis - updated: 7/8/1999
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
wwang: 08/17/2009
ckniffin: 8/6/2009
terry: 4/5/2000
mgross: 7/8/1999
warfield: 4/12/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 6/28/1989
carol: 6/13/1989
*RECORD*
*FIELD* NO
153420
*FIELD* TI
*153420 CD58 MOLECULE; CD58
;;LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN, TYPE 3; LFA3
read more*FIELD* TX
DESCRIPTION
The CD58 gene encodes a CD2 (186990) receptor. The presence of these 2
antigens on opposing cells optimizes immune recognition, facilitating
contacts between helper T lymphocytes and antigen-presenting cells as
well as between cytolytic effectors and target cells (Wang et al.,
1999).
CLONING
The LFA3 gene has been cloned (Barbosa, 1987).
Wallner et al. (1987) isolated the cDNA for CD58, which they called
LFA3, the ligand of the T lymphocyte CD2 molecule. The deduced protein
contains 222 amino acids and structurally resembles a typical
membrane-anchored protein. An extracellular domain with six N-linked
glycosylation sites is followed by a hydrophobic putative transmembrane
region and a short cytoplasmic domain. Northern blot analysis detected a
1.3-kb LFA3 transcript that was widely distributed in human tissues and
cell lines.
Sewell et al. (1988) noted that the amino acid sequences of the
extracellular domains of CD2 and CD58, which are predicted from their
cDNA sequences, show significant similarities, and both are members of
the immunoglobulin supergene family. They probably arose by duplication
of a common evolutionary precursor.
MAPPING
Barbosa et al. (1985, 1986) mapped the LFA3 gene to chromosome 1 by
study of mouse-human cell hybrids. There is some possibility that LFA3
is identical to the cell surface antigen identified by monoclonal
antibodies and known as MSK2 (158040). MSK1 (158030) maps to the short
arm of chromosome 1, and MSK2 to the long arm of chromosome 1.
By a combination of Southern blot analysis of somatic cell hybrid DNA
and in situ hybridization, Sewell et al. (1988) assigned the LFA3 gene
to chromosome 1p13, which is the same location as CD2.
BIOCHEMICAL FEATURES
- Crystal Structure
Wang et al. (1999) reported the crystal structure of the heterophilic
adhesion complex between the N-terminal domains of human CD2 and CD58 at
more than 3.2-angstrom resolution. A strikingly asymmetric, orthogonal,
face-to-face interaction involving the major beta sheets of the
respective immunoglobulin-like domains with poor shape complementarity
was revealed. These features explained CD2-CD58 dynamic binding,
offering insights into the interactions of related immunoglobulin
superfamily receptors.
MOLECULAR GENETICS
For a discussion of a possible association between variation in the CD58
gene and protection against multiple sclerosis, see MS (126200).
*FIELD* RF
1. Barbosa, J. A.: Personal Communication. West Haven, Conn. 1987.
2. Barbosa, J. A.; Mentzer, S. J.; Kamarck, M. E.; Hart, J.; Biro,
P. A.; Strominger, J. L.; Burakoff, S. J.: Gene mapping and somatic
cell hybrid analysis of the role of human lymphocyte function-associated
antigen-3 (LFA-3) in CTL-target cell interactions. J. Immun. 136:
3085-3091, 1986.
3. Barbosa, J. A.; Mentzer, S. J.; Kamarck, M. E.; Hart, J.; Strominger,
J. L.; Biro, P. A.; Burakoff, S. J.: Somatic cell hybrid analysis
of human lymphocyte function associated antigen-3 (LFA-3): gene mapping
and role in CTL-target cell interactions. ICSU Short Reports 2:
107-108, 1985.
4. Sewell, W. A.; Palmer, R. W.; Spurr, N. K.; Sheer, D.; Brown, M.
H.; Bell, Y.; Crumpton, M. J.: The human LFA-3 gene is located at
the same chromosome band as the gene for its receptor CD2. Immunogenetics 28:
278-282, 1988.
5. Wallner, B. P.; Frey, A. Z.; Tizard, R.; Mattaliano, R. J.; Hession,
C.; Sanders, M. E.; Dustin, M. L.; Springer, T. A.: Primary structure
of lymphocyte function-associated antigen 3 (LFA-3): the ligand of
the T lymphocyte CD2 glycoprotein. J. Exp. Med. 166: 923-932, 1987.
6. Wang, J.; Smolyar, A.; Tan, K.; Liu, J.; Kim, M.; Sun, Z. J.; Wagner,
G.; Reinherz, E. L.: Structure of a heterophilic adhesion complex
between the human CD2 and CD58 (LFA-3) counterreceptors. Cell 97:
791-803, 1999.
*FIELD* CN
Cassandra L. Kniffin - updated: 8/6/2009
Stylianos E. Antonarakis - updated: 7/8/1999
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
wwang: 08/17/2009
ckniffin: 8/6/2009
terry: 4/5/2000
mgross: 7/8/1999
warfield: 4/12/1994
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 6/28/1989
carol: 6/13/1989