ID CD2_HUMAN Reviewed; 351 AA.
AC P06729; Q96TE5;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 27-MAR-2024, entry version 237.
DE RecName: Full=T-cell surface antigen CD2;
DE AltName: Full=Erythrocyte receptor;
DE AltName: Full=LFA-2;
DE AltName: Full=LFA-3 receptor;
DE AltName: Full=Rosette receptor;
DE AltName: Full=T-cell surface antigen T11/Leu-5;
DE AltName: CD_antigen=CD2;
DE Flags: Precursor;
GN Name=CD2; Synonyms=SRBC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2894031; DOI=10.1073/pnas.85.5.1615;
RA Diamond D.J., Clayton L.K., Sayre P.H., Reinherz E.L.;
RT "Exon-intron organization and sequence comparison of human and murine T11
RT (CD2) genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1615-1619(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-266, AND SUBCELLULAR LOCATION.
RX PubMed=2437578; DOI=10.1073/pnas.84.10.3365;
RA Seed B., Aruffo A.;
RT "Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by
RT a rapid immunoselection procedure.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3365-3369(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3490670; DOI=10.1073/pnas.83.22.8718;
RA Sewell W.A., Brown M.H., Dunne J., Owen M.J., Crumpton M.J.;
RT "Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8718-8722(1986).
RN [4]
RP ERRATUM OF PUBMED:3490670, AND SEQUENCE REVISION.
RA Sewell W.A., Brown M.H., Dunne J., Owen M.J., Crumpton M.J.;
RL Proc. Natl. Acad. Sci. U.S.A. 84:7256-7256(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2883656; DOI=10.1073/pnas.84.9.2941;
RA Sayre P.H., Chang H.-C., Hussey R.E., Brown N.R., Richardson N.E.,
RA Spagnoli G., Clayton L.K., Reinherz E.L.;
RT "Molecular cloning and expression of T11 cDNAs reveal a receptor-like
RT structure on human T lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:2941-2945(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-266.
RX PubMed=2901953; DOI=10.1002/j.1460-2075.1988.tb02995.x;
RA Lang G., Wotton D., Owen M.J., Sewell W.A., Brown M.H., Mason D.Y.,
RA Crumpton M.J., Kioussis D.;
RT "The structure of the human CD2 gene and its expression in transgenic
RT mice.";
RL EMBO J. 7:1675-1682(1988).
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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 MRNA], AND VARIANT GLN-266.
RC TISSUE=Pancreas, and Spleen;
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 [9]
RP MUTAGENESIS OF LYS-67; GLN-70; TYR-110 AND ASP-111.
RX PubMed=2444890; DOI=10.1038/329842a0;
RA Peterson A., Seed B.;
RT "Monoclonal antibody and ligand binding sites of the T cell erythrocyte
RT receptor (CD2).";
RL Nature 329:842-846(1987).
RN [10]
RP CD59-BINDING DATA.
RX PubMed=1377404; DOI=10.1126/science.1377404;
RA Hahn W.C., Menu E., Bothwell A.L.M., Sims P.J., Bierer B.E.;
RT "Overlapping but nonidentical binding sites on CD2 for CD58 and a second
RT ligand CD59.";
RL Science 256:1805-1807(1992).
RN [11]
RP INTERACTION WITH PSTPIP1.
RX PubMed=9857189; DOI=10.1093/emboj/17.24.7320;
RA Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R.,
RA Sunder-Plassmann R., Reinherz E.L.;
RT "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic
RT domain and regulates CD2-triggered adhesion.";
RL EMBO J. 17:7320-7336(1998).
RN [12]
RP INTERACTION WITH FCGR3A, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23006327; DOI=10.1172/jci64837;
RA Grier J.T., Forbes L.R., Monaco-Shawver L., Oshinsky J., Atkinson T.P.,
RA Moody C., Pandey R., Campbell K.S., Orange J.S.;
RT "Human immunodeficiency-causing mutation defines CD16 in spontaneous NK
RT cell cytotoxicity.";
RL J. Clin. Invest. 122:3769-3780(2012).
RN [13] {ECO:0007744|PDB:1HNF}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 25-206, GLYCOSYLATION AT ASN-89;
RP ASN-141 AND ASN-150, AND DISULFIDE BONDS.
RX PubMed=7994575; DOI=10.1016/s0969-2126(94)00076-x;
RA Bodian D.L., Jones E.Y., Harlos K., Stuart D.I., Davis S.J.;
RT "Crystal structure of the extracellular region of the human cell adhesion
RT molecule CD2 at 2.5 A resolution.";
RL Structure 2:755-766(1994).
RN [14]
RP STRUCTURE BY NMR OF 25-129.
RX PubMed=7915183; DOI=10.1016/0969-2126(93)90009-6;
RA Withka J.M., Wyss D.F., Wagner G., Arulanandam A.R.N., Reinherz E.L.,
RA Recny M.A.;
RT "Structure of the glycosylated adhesion domain of human T lymphocyte
RT glycoprotein CD2.";
RL Structure 1:69-81(1993).
RN [15]
RP STRUCTURE BY NMR OF 25-129, AND GLYCOSYLATION AT ASN-89.
RX PubMed=7544493; DOI=10.1126/science.7544493;
RA Wyss D.F., Choi J.S., Li J., Knoppers M.H., Willis K.J., Arulanandam A.R.,
RA Smolyar A., Reinherz E.L., Wagner G.;
RT "Conformation and function of the N-linked glycan in the adhesion domain of
RT human CD2.";
RL Science 269:1273-1278(1995).
RN [16] {ECO:0007744|PDB:1QA9}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 28-129 IN COMPLEX WITH CD58, AND
RP INTERACTION WITH CD58.
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 and
RT CD58 (LFA-3) counterreceptors.";
RL Cell 97:791-803(1999).
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] TYR-217.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: CD2 interacts with lymphocyte function-associated antigen
CC CD58 (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and
CC other cell types. CD2 is implicated in the triggering of T-cells, the
CC cytoplasmic domain is implicated in the signaling function.
CC -!- SUBUNIT: Interacts with CD48 (By similarity). Interacts with CD58 (LFA-
CC 3) (PubMed:10380930). Interacts with CD2AP (By similarity). Interacts
CC with PSTPIP1 (PubMed:9857189). Interacts with FCGR3A; this interaction
CC modulates NK cell activation and cytotoxicity.
CC {ECO:0000250|UniProtKB:P08920, ECO:0000250|UniProtKB:P08921,
CC ECO:0000269|PubMed:23006327, ECO:0000269|PubMed:9857189}.
CC -!- INTERACTION:
CC P06729; Q9Y5K6: CD2AP; NbExp=4; IntAct=EBI-3912464, EBI-298152;
CC P06729; O95400: CD2BP2; NbExp=9; IntAct=EBI-3912464, EBI-768015;
CC P06729; Q96B97: SH3KBP1; NbExp=3; IntAct=EBI-3912464, EBI-346595;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23006327,
CC ECO:0000269|PubMed:2437578}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in natural killer cells (at protein
CC level). {ECO:0000269|PubMed:23006327}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD2 entry;
CC URL="https://en.wikipedia.org/wiki/CD2";
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DR EMBL; M19806; AAA53095.1; -; Genomic_DNA.
DR EMBL; M19798; AAA53095.1; JOINED; Genomic_DNA.
DR EMBL; M19800; AAA53095.1; JOINED; Genomic_DNA.
DR EMBL; M19802; AAA53095.1; JOINED; Genomic_DNA.
DR EMBL; M19804; AAA53095.1; JOINED; Genomic_DNA.
DR EMBL; M16445; AAA51738.1; -; mRNA.
DR EMBL; M14362; AAA35571.1; -; mRNA.
DR EMBL; M16336; AAA51946.1; -; mRNA.
DR EMBL; X07871; CAA30721.1; -; Genomic_DNA.
DR EMBL; X07872; CAA30721.1; JOINED; Genomic_DNA.
DR EMBL; X07873; CAA30721.1; JOINED; Genomic_DNA.
DR EMBL; X07874; CAA30721.1; JOINED; Genomic_DNA.
DR EMBL; AL135798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033583; AAH33583.1; -; mRNA.
DR CCDS; CCDS889.1; -.
DR PIR; A28967; RWHUC2.
DR RefSeq; NP_001315538.1; NM_001328609.1.
DR RefSeq; NP_001758.2; NM_001767.4.
DR PDB; 1CDB; NMR; -; A=25-129.
DR PDB; 1GYA; NMR; -; A=25-129.
DR PDB; 1HNF; X-ray; 2.50 A; A=25-206.
DR PDB; 1L2Z; NMR; -; B=294-304.
DR PDB; 1QA9; X-ray; 3.20 A; A/C=28-129.
DR PDB; 2J6O; X-ray; 2.22 A; C=324-333.
DR PDB; 2J7I; X-ray; 2.90 A; C/D=324-333.
DR PDBsum; 1CDB; -.
DR PDBsum; 1GYA; -.
DR PDBsum; 1HNF; -.
DR PDBsum; 1L2Z; -.
DR PDBsum; 1QA9; -.
DR PDBsum; 2J6O; -.
DR PDBsum; 2J7I; -.
DR AlphaFoldDB; P06729; -.
DR SMR; P06729; -.
DR BioGRID; 107352; 19.
DR ELM; P06729; -.
DR IntAct; P06729; 10.
DR MINT; P06729; -.
DR STRING; 9606.ENSP00000358490; -.
DR BindingDB; P06729; -.
DR ChEMBL; CHEMBL2040; -.
DR DrugBank; DB00092; Alefacept.
DR DrugBank; DB06371; Siplizumab.
DR DrugCentral; P06729; -.
DR UniLectin; P06729; -.
DR GlyConnect; 586; 8 N-Linked glycans.
DR GlyCosmos; P06729; 4 sites, 17 glycans.
DR GlyGen; P06729; 5 sites, 16 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P06729; -.
DR PhosphoSitePlus; P06729; -.
DR BioMuta; CD2; -.
DR DMDM; 160370002; -.
DR jPOST; P06729; -.
DR MassIVE; P06729; -.
DR PaxDb; 9606-ENSP00000358490; -.
DR PeptideAtlas; P06729; -.
DR ProteomicsDB; 51913; -.
DR ABCD; P06729; 4 sequenced antibodies.
DR Antibodypedia; 1086; 3237 antibodies from 54 providers.
DR DNASU; 914; -.
DR Ensembl; ENST00000369478.4; ENSP00000358490.3; ENSG00000116824.5.
DR GeneID; 914; -.
DR KEGG; hsa:914; -.
DR MANE-Select; ENST00000369478.4; ENSP00000358490.3; NM_001767.5; NP_001758.2.
DR AGR; HGNC:1639; -.
DR CTD; 914; -.
DR DisGeNET; 914; -.
DR GeneCards; CD2; -.
DR HGNC; HGNC:1639; CD2.
DR HPA; ENSG00000116824; Tissue enriched (lymphoid).
DR MIM; 186990; gene.
DR neXtProt; NX_P06729; -.
DR OpenTargets; ENSG00000116824; -.
DR PharmGKB; PA26198; -.
DR VEuPathDB; HostDB:ENSG00000116824; -.
DR eggNOG; ENOG502S5UN; Eukaryota.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_069390_0_0_1; -.
DR InParanoid; P06729; -.
DR OMA; DIPNFQM; -.
DR OrthoDB; 4584733at2759; -.
DR PhylomeDB; P06729; -.
DR TreeFam; TF335971; -.
DR PathwayCommons; P06729; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P06729; -.
DR BioGRID-ORCS; 914; 15 hits in 1159 CRISPR screens.
DR ChiTaRS; CD2; human.
DR EvolutionaryTrace; P06729; -.
DR GeneWiki; CD2; -.
DR GenomeRNAi; 914; -.
DR Pharos; P06729; Tclin.
DR PRO; PR:P06729; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P06729; Protein.
DR Bgee; ENSG00000116824; Expressed in granulocyte and 139 other cell types or tissues.
DR ExpressionAtlas; P06729; baseline and differential.
DR Genevisible; P06729; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0001766; P:membrane raft polarization; TAS:UniProtKB.
DR GO; GO:0030101; P:natural killer cell activation; IDA:UniProtKB.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB.
DR GO; GO:0030887; P:positive regulation of myeloid dendritic cell activation; NAS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
DR GO; GO:0032729; P:positive regulation of type II interferon production; IDA:UniProtKB.
DR GO; GO:0045580; P:regulation of T cell differentiation; NAS:UniProtKB.
DR GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
DR CDD; cd05775; IgV_CD2_like_N; 1.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR12080; SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE; 1.
DR PANTHER; PTHR12080:SF54; T-CELL SURFACE ANTIGEN CD2; 1.
DR Pfam; PF05790; C2-set; 1.
DR Pfam; PF07686; V-set; 1.
DR PRINTS; PR01870; CD2ANTIGEN.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT CHAIN 25..351
FT /note="T-cell surface antigen CD2"
FT /id="PRO_0000014600"
FT TOPO_DOM 25..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..128
FT /note="Ig-like V-type"
FT DOMAIN 129..209
FT /note="Ig-like C2-type"
FT REGION 61..75
FT /note="CD58 binding region 1"
FT /evidence="ECO:0000269|PubMed:2444890"
FT REGION 106..120
FT /note="CD58 binding region 2"
FT /evidence="ECO:0000269|PubMed:2444890"
FT REGION 237..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7994575,
FT ECO:0007744|PDB:1GYA, ECO:0007744|PDB:1HNF"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7994575,
FT ECO:0007744|PDB:1HNF"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7994575,
FT ECO:0007744|PDB:1HNF"
FT DISULFID 139..203
FT /evidence="ECO:0000269|PubMed:7994575"
FT DISULFID 146..186
FT /evidence="ECO:0000269|PubMed:7994575"
FT VARIANT 217
FT /note="C -> Y (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035504"
FT VARIANT 266
FT /note="H -> Q (in dbSNP:rs699738)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2437578, ECO:0000269|PubMed:2901953"
FT /id="VAR_017104"
FT VARIANT 339
FT /note="H -> N (in dbSNP:rs35880225)"
FT /id="VAR_033608"
FT MUTAGEN 67
FT /note="K->R: Loss of CD58 binding."
FT /evidence="ECO:0000269|PubMed:2444890"
FT MUTAGEN 70
FT /note="Q->K: Loss of CD58 binding."
FT /evidence="ECO:0000269|PubMed:2444890"
FT MUTAGEN 110
FT /note="Y->D: Loss of CD58 and CD59 binding."
FT /evidence="ECO:0000269|PubMed:2444890"
FT MUTAGEN 111
FT /note="D->H: Loss of CD58 and CD59 binding."
FT /evidence="ECO:0000269|PubMed:2444890"
FT CONFLICT 287
FT /note="G -> A (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..351
FT /note="HGAAENSLSPSSN -> MGQQKTHCPLPLIKKDRNCLFQ (in Ref. 3;
FT AAA51946)"
FT /evidence="ECO:0000305"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 52..61
FT /evidence="ECO:0007829|PDB:1HNF"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1HNF"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1HNF"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1QA9"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1HNF"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 116..127
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1HNF"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:1HNF"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:1HNF"
SQ SEQUENCE 351 AA; 39448 MW; A03D853C3B618917 CRC64;
MSFPCKFVAS FLLIFNVSSK GAVSKEITNA LETWGALGQD INLDIPSFQM SDDIDDIKWE
KTSDKKKIAQ FRKEKETFKE KDTYKLFKNG TLKIKHLKTD DQDIYKVSIY DTKGKNVLEK
IFDLKIQERV SKPKISWTCI NTTLTCEVMN GTDPELNLYQ DGKHLKLSQR VITHKWTTSL
SAKFKCTAGN KVSKESSVEP VSCPEKGLDI YLIIGICGGG SLLMVFVALL VFYITKRKKQ
RSRRNDEELE TRAHRVATEE RGRKPHQIPA STPQNPATSQ HPPPPPGHRS QAPSHRPPPP
GHRVQHQPQK RPPAPSGTQV HQQKGPPLPR PRVQPKPPHG AAENSLSPSS N
//
