CD59_HUMAN
ID CD59_HUMAN Reviewed; 128 AA.
AC P13987; E9PR17;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 230.
DE RecName: Full=CD59 glycoprotein;
DE AltName: Full=1F5 antigen;
DE AltName: Full=20 kDa homologous restriction factor;
DE Short=HRF-20;
DE Short=HRF20;
DE AltName: Full=MAC-inhibitory protein;
DE Short=MAC-IP;
DE AltName: Full=MEM43 antigen;
DE AltName: Full=Membrane attack complex inhibition factor;
DE Short=MACIF;
DE AltName: Full=Membrane inhibitor of reactive lysis;
DE Short=MIRL;
DE AltName: Full=Protectin;
DE AltName: CD_antigen=CD59;
DE Flags: Precursor;
GN Name=CD59; Synonyms=MIC11, MIN1, MIN2, MIN3, MSK21;
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 [MRNA].
RC TISSUE=T-cell;
RX PubMed=2475570; DOI=10.1084/jem.170.3.637;
RA Davies A., Simmons D.L., Hale G., Harrison R.A., Tighe H., Lachmann P.J.,
RA Waldmann H.;
RT "CD59, an LY-6-like protein expressed in human lymphoid cells, regulates
RT the action of the complement membrane attack complex on homologous cells.";
RL J. Exp. Med. 170:637-654(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1689664; DOI=10.1002/eji.1830200113;
RA Philbrick W.M., Palfree R.G.E., Roger G.E., Maher S.E., Bridgett M.M.,
RA Sirlin S., Bothwell A.L.M.;
RT "The CD59 antigen is a structural homologue of murine Ly-6 antigens but
RT lacks interferon inducibility.";
RL Eur. J. Immunol. 20:87-92(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2475111; DOI=10.1016/0006-291x(89)90852-8;
RA Okada H., Nagami Y., Takahashi K., Okada N., Hideshima T., Takizawa H.,
RA Kondo J.;
RT "20 KDa homologous restriction factor of complement resembles T cell
RT activating protein.";
RL Biochem. Biophys. Res. Commun. 162:1553-1559(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2606909; DOI=10.1093/oxfordjournals.jbchem.a122893;
RA Sugita Y., Tobe T., Oda E., Tomita M., Yasukawa K., Yamaji N., Takemoto T.,
RA Furuichi K., Takayama M., Yano S.;
RT "Molecular cloning and characterization of MACIF, an inhibitor of membrane
RT channel formation of complement.";
RL J. Biochem. 106:555-557(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1692709; DOI=10.1089/dna.1990.9.213;
RA Sawada R., Ohashi K., Anaguchi H., Okazaki H., Hattori M., Minato N.,
RA Naruto M.;
RT "Isolation and expression of the full-length cDNA encoding CD59 antigen of
RT human lymphocytes.";
RL DNA Cell Biol. 9:213-220(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1381503; DOI=10.1073/pnas.89.17.7876;
RA Petranka J.G., Fleenor D.E., Sykes K., Kaufman R.E., Rosse W.F.;
RT "Structure of the CD59-encoding gene: further evidence of a relationship to
RT murine lymphocyte antigen Ly-6 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7876-7879(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=1383553; DOI=10.1016/0022-2836(92)90239-g;
RA Tone M., Walsh L.A., Waldmann H.;
RT "Gene structure of human CD59 and demonstration that discrete mRNAs are
RT generated by alternative polyadenylation.";
RL J. Mol. Biol. 227:971-976(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-128.
RX PubMed=2476718; DOI=10.1093/nar/17.16.6728;
RA Sawada R., Ohashi K., Okano K., Hattori M., Minato N., Naruto M.;
RT "Complementary DNA sequence and deduced peptide sequence for CD59/MEM-43
RT antigen, the human homologue of murine lymphocyte antigen Ly-6C.";
RL Nucleic Acids Res. 17:6728-6728(1989).
RN [12]
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT
RP ASN-43, AND STRUCTURE OF CARBOHYDRATES.
RX PubMed=8670172; DOI=10.1042/bj3160923;
RA Meri S., Lehto T., Sutton C.W., Tyynelaa J., Baumann M.;
RT "Structural composition and functional characterization of soluble CD59:
RT heterogeneity of the oligosaccharide and glycophosphoinositol (GPI) anchor
RT revealed by laser-desorption mass spectrometric analysis.";
RL Biochem. J. 316:923-935(1996).
RN [13]
RP GPI-ANCHOR AT ASN-102, AND DISULFIDE BONDS.
RX PubMed=8276756; DOI=10.1093/oxfordjournals.jbchem.a124202;
RA Sugita Y., Nakano Y., Oda E., Noda K., Tobe T., Miura N.H., Tomita M.;
RT "Determination of carboxyl-terminal residue and disulfide bonds of MACIF
RT (CD59), a glycosyl-phosphatidylinositol-anchored membrane protein.";
RL J. Biochem. 114:473-477(1993).
RN [14]
RP INTERACTION WITH C8 AND C9.
RX PubMed=1377690; DOI=10.1016/s0021-9258(18)42266-1;
RA Ninomiya H., Sims P.J.;
RT "The human complement regulatory protein CD59 binds to the alpha-chain of
RT C8 and to the ''b'' domain of C9.";
RL J. Biol. Chem. 267:13675-13680(1992).
RN [15]
RP IDENTIFICATION OF COMPLEMENT INHIBITORY DOMAIN.
RX PubMed=9235986; DOI=10.1021/bi970832i;
RA Yu J., Dong S., Rushmere N.K., Morgan B.P., Abagyan R., Tomlinson S.;
RT "Mapping the regions of the complement inhibitor CD59 responsible for its
RT species selective activity.";
RL Biochemistry 36:9423-9428(1997).
RN [16]
RP MUTAGENESIS.
RX PubMed=9053451; DOI=10.1084/jem.185.3.507;
RA Bodian D.L., Davis S.J., Morgan B.P., Rushmere N.K.;
RT "Mutational analysis of the active site and antibody epitopes of the
RT complement-inhibitory glycoprotein, CD59.";
RL J. Exp. Med. 185:507-516(1997).
RN [17]
RP STRUCTURE OF CARBOHYDRATES, STRUCTURE OF THE GPI-ANCHOR, AND PROTEIN
RP SEQUENCE OF N-TERMINUS.
RX PubMed=9054419; DOI=10.1074/jbc.272.11.7229;
RA Rudd P.M., Morgan B.P., Wormald M.R., Harvey D.J., van den Berg C.W.,
RA Davis S.J., Ferguson M.A., Dwek R.A.;
RT "The glycosylation of the complement regulatory protein, human erythrocyte
RT CD59.";
RL J. Biol. Chem. 272:7229-7244(1997).
RN [18]
RP INHIBITION BY GLYCATION, GLYCATION AT LYS-66, AND MUTAGENESIS OF LYS-66 AND
RP HIS-69.
RX PubMed=10805801; DOI=10.1073/pnas.97.10.5450;
RA Acosta J., Hettinga J., Flueckiger R., Krumrei N., Goldfine A.,
RA Angarita L., Halperin J.;
RT "Molecular basis for a link between complement and the vascular
RT complications of diabetes.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5450-5455(2000).
RN [19]
RP GPI-ANCHOR AT ASN-102, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17566972; DOI=10.1002/pmic.200700068;
RA Omaetxebarria M.J., Elortza F., Rodriguez-Suarez E., Aloria K.,
RA Arizmendi J.M., Jensen O.N., Matthiesen R.;
RT "Computational approach for identification and characterization of GPI-
RT anchored peptides in proteomics experiments.";
RL Proteomics 7:1951-1960(2007).
RN [20]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-43.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER SER-25, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24]
RP STRUCTURE BY NMR OF 26-95.
RX PubMed=7512825; DOI=10.1021/bi00181a006;
RA Kieffer B., Driscoll P.C., Campbell I.D., Willis A.C., van der Merwe P.A.,
RA Davis S.J.;
RT "Three-dimensional solution structure of the extracellular region of the
RT complement regulatory protein CD59, a new cell-surface protein domain
RT related to snake venom neurotoxins.";
RL Biochemistry 33:4471-4482(1994).
RN [25]
RP STRUCTURE BY NMR OF 26-102.
RC TISSUE=Urine;
RX PubMed=7520819; DOI=10.1016/s0969-2126(00)00020-4;
RA Fletcher C.M., Harrison R.A., Lachmann P.J., Neuhaus D.;
RT "Structure of a soluble, glycosylated form of the human complement
RT regulatory protein CD59.";
RL Structure 2:185-199(1994).
RN [26]
RP INVOLVEMENT IN HACD59.
RX PubMed=1382994; DOI=10.1002/eji.1830221029;
RA Motoyama N., Okada N., Yamashina M., Okada H.;
RT "Paroxysmal nocturnal hemoglobinuria due to hereditary nucleotide deletion
RT in the HRF20 (CD59) gene.";
RL Eur. J. Immunol. 22:2669-2673(1992).
RN [27]
RP VARIANT HACD59 TYR-89.
RX PubMed=23149847; DOI=10.1182/blood-2012-07-441857;
RA Nevo Y., Ben-Zeev B., Tabib A., Straussberg R., Anikster Y., Shorer Z.,
RA Fattal-Valevski A., Ta-Shma A., Aharoni S., Rabie M., Zenvirt S.,
RA Goldshmidt H., Fellig Y., Shaag A., Mevorach D., Elpeleg O.;
RT "CD59 deficiency is associated with chronic hemolysis and childhood
RT relapsing immune-mediated polyneuropathy.";
RL Blood 121:129-135(2013).
CC -!- FUNCTION: Potent inhibitor of the complement membrane attack complex
CC (MAC) action. Acts by binding to the C8 and/or C9 complements of the
CC assembling MAC, thereby preventing incorporation of the multiple copies
CC of C9 required for complete formation of the osmolytic pore. This
CC inhibitor appears to be species-specific. Involved in signal
CC transduction for T-cell activation complexed to a protein tyrosine
CC kinase.
CC -!- FUNCTION: The soluble form from urine retains its specific complement
CC binding activity, but exhibits greatly reduced ability to inhibit MAC
CC assembly on cell membranes.
CC -!- SUBUNIT: Interacts with T-cell surface antigen CD2.
CC {ECO:0000269|PubMed:1377690}.
CC -!- INTERACTION:
CC P13987; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-297972, EBI-18304435;
CC P13987; P42858: HTT; NbExp=10; IntAct=EBI-297972, EBI-466029;
CC P13987; Q15363: TMED2; NbExp=4; IntAct=EBI-297972, EBI-998485;
CC P13987; Q778I9: C; Xeno; NbExp=4; IntAct=EBI-297972, EBI-8716052;
CC P13987; O35587: TMED10; Xeno; NbExp=5; IntAct=EBI-297972, EBI-4405327;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC Secreted. Note=Soluble form found in a number of tissues.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P13987-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13987-2; Sequence=VSP_060064;
CC -!- PTM: N- and O-glycosylated. The N-glycosylation mainly consists of a
CC family of biantennary complex-type structures with and without
CC lactosamine extensions and outer arm fucose residues. Also significant
CC amounts of triantennary complexes (22%). Variable sialylation also
CC present in the Asn-43 oligosaccharide. The predominant O-glycans are
CC mono-sialylated forms of the disaccharide, Gal-beta-1,3GalNAc, and
CC their sites of attachment are probably on Thr-76 and Thr-77. The GPI-
CC anchor of soluble urinary CD59 has no inositol-associated phospholipid,
CC but is composed of seven different GPI-anchor variants of one or more
CC monosaccharide units. Major variants contain sialic acid, mannose and
CC glucosamine. Sialic acid linked to an N-acetylhexosamine-galactose arm
CC is present in two variants. {ECO:0000269|PubMed:18780401,
CC ECO:0000269|PubMed:8670172}.
CC -!- PTM: Glycated. Glycation is found in diabetic subjects, but only at
CC minimal levels in nondiabetic subjects. Glycated CD59 lacks MAC-
CC inhibitory function and confers to vascular complications of diabetes.
CC -!- DISEASE: Hemolytic anemia, CD59-mediated, with or without
CC polyneuropathy (HACD59) [MIM:612300]: An autosomal recessive disorder
CC characterized by infantile onset of chronic hemolysis and a relapsing-
CC remitting polyneuropathy, often exacerbated by infection, and
CC manifested as hypotonia, limb muscle weakness, and hyporeflexia.
CC {ECO:0000269|PubMed:1382994, ECO:0000269|PubMed:23149847}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=CD59base; Note=CD59 mutation db;
CC URL="http://structure.bmc.lu.se/idbase/CD59base/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CD59ID985ch11p13.html";
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DR EMBL; M27909; AAA60543.1; -; mRNA.
DR EMBL; M95708; AAA60957.1; -; mRNA.
DR EMBL; X16447; CAA34467.1; -; mRNA.
DR EMBL; X17198; CAA35059.1; -; mRNA.
DR EMBL; M34671; AAA51952.1; -; mRNA.
DR EMBL; M84345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M84349; AAA88793.1; -; Genomic_DNA.
DR EMBL; M84346; AAA88793.1; JOINED; Genomic_DNA.
DR EMBL; M84348; AAA88793.1; JOINED; Genomic_DNA.
DR EMBL; Z14113; CAA78486.1; -; Genomic_DNA.
DR EMBL; Z14114; CAA78486.1; JOINED; Genomic_DNA.
DR EMBL; Z14115; CAA78486.1; JOINED; Genomic_DNA.
DR EMBL; BT007104; AAP35768.1; -; mRNA.
DR EMBL; AL049629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF455356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001506; AAH01506.1; -; mRNA.
DR CCDS; CCDS7886.1; -. [P13987-1]
DR PIR; A46252; RWHU59.
DR RefSeq; NP_000602.1; NM_000611.5. [P13987-1]
DR RefSeq; NP_001120695.1; NM_001127223.1. [P13987-1]
DR RefSeq; NP_001120697.1; NM_001127225.1. [P13987-1]
DR RefSeq; NP_001120698.1; NM_001127226.1. [P13987-1]
DR RefSeq; NP_001120699.1; NM_001127227.1. [P13987-1]
DR RefSeq; NP_976074.1; NM_203329.2. [P13987-1]
DR RefSeq; NP_976075.1; NM_203330.2. [P13987-1]
DR RefSeq; NP_976076.1; NM_203331.2. [P13987-1]
DR PDB; 1CDQ; NMR; -; A=26-102.
DR PDB; 1CDR; NMR; -; A=26-102.
DR PDB; 1CDS; NMR; -; A=26-102.
DR PDB; 1ERG; NMR; -; A=26-95.
DR PDB; 1ERH; NMR; -; A=26-95.
DR PDB; 2J8B; X-ray; 1.15 A; A=26-103.
DR PDB; 2OFS; X-ray; 2.12 A; A=26-99.
DR PDB; 2UWR; X-ray; 1.34 A; A=26-102.
DR PDB; 2UX2; X-ray; 1.80 A; A/B/C=26-102.
DR PDB; 4BIK; X-ray; 3.49 A; B/D=26-102.
DR PDB; 5IMT; X-ray; 2.70 A; D=26-102.
DR PDB; 5IMY; X-ray; 2.40 A; C/D=26-102.
DR PDB; 6ZD0; EM; 4.60 A; B/D/F=26-102.
DR PDBsum; 1CDQ; -.
DR PDBsum; 1CDR; -.
DR PDBsum; 1CDS; -.
DR PDBsum; 1ERG; -.
DR PDBsum; 1ERH; -.
DR PDBsum; 2J8B; -.
DR PDBsum; 2OFS; -.
DR PDBsum; 2UWR; -.
DR PDBsum; 2UX2; -.
DR PDBsum; 4BIK; -.
DR PDBsum; 5IMT; -.
DR PDBsum; 5IMY; -.
DR PDBsum; 6ZD0; -.
DR AlphaFoldDB; P13987; -.
DR SMR; P13987; -.
DR BioGRID; 107404; 79.
DR IntAct; P13987; 42.
DR MINT; P13987; -.
DR STRING; 9606.ENSP00000379191; -.
DR GlyConnect; 79; 115 N-Linked glycans (1 site), 17 O-Linked glycans (4 sites).
DR GlyGen; P13987; 7 sites, 138 N-linked glycans (2 sites), 7 O-linked glycans (4 sites).
DR iPTMnet; P13987; -.
DR PhosphoSitePlus; P13987; -.
DR SwissPalm; P13987; -.
DR BioMuta; CD59; -.
DR DMDM; 116021; -.
DR CPTAC; CPTAC-43; -.
DR CPTAC; CPTAC-44; -.
DR EPD; P13987; -.
DR jPOST; P13987; -.
DR MassIVE; P13987; -.
DR PaxDb; P13987; -.
DR PeptideAtlas; P13987; -.
DR PRIDE; P13987; -.
DR ProteomicsDB; 23185; -.
DR ProteomicsDB; 53014; -.
DR ABCD; P13987; 1 sequenced antibody.
DR Antibodypedia; 3667; 1988 antibodies from 45 providers.
DR DNASU; 966; -.
DR Ensembl; ENST00000351554.8; ENSP00000340210.3; ENSG00000085063.17. [P13987-1]
DR Ensembl; ENST00000395850.9; ENSP00000379191.3; ENSG00000085063.17. [P13987-1]
DR Ensembl; ENST00000415002.7; ENSP00000404822.2; ENSG00000085063.17. [P13987-1]
DR Ensembl; ENST00000437761.6; ENSP00000410182.2; ENSG00000085063.17. [P13987-1]
DR Ensembl; ENST00000445143.6; ENSP00000403511.2; ENSG00000085063.17. [P13987-1]
DR Ensembl; ENST00000527577.5; ENSP00000432942.1; ENSG00000085063.17. [P13987-1]
DR Ensembl; ENST00000642928.2; ENSP00000494884.1; ENSG00000085063.17. [P13987-1]
DR Ensembl; ENST00000651785.1; ENSP00000498879.1; ENSG00000085063.17. [P13987-1]
DR Ensembl; ENST00000652678.1; ENSP00000498448.1; ENSG00000085063.17. [P13987-1]
DR GeneID; 966; -.
DR KEGG; hsa:966; -.
DR MANE-Select; ENST00000642928.2; ENSP00000494884.1; NM_000611.6; NP_000602.1.
DR CTD; 966; -.
DR DisGeNET; 966; -.
DR GeneCards; CD59; -.
DR HGNC; HGNC:1689; CD59.
DR HPA; ENSG00000085063; Low tissue specificity.
DR MalaCards; CD59; -.
DR MIM; 107271; gene.
DR MIM; 612300; phenotype.
DR neXtProt; NX_P13987; -.
DR OpenTargets; ENSG00000085063; -.
DR Orphanet; 169464; Primary CD59 deficiency.
DR PharmGKB; PA26228; -.
DR VEuPathDB; HostDB:ENSG00000085063; -.
DR eggNOG; ENOG502SA4P; Eukaryota.
DR GeneTree; ENSGT00390000016309; -.
DR HOGENOM; CLU_147732_1_0_1; -.
DR InParanoid; P13987; -.
DR OMA; CSKQRDC; -.
DR OrthoDB; 1586315at2759; -.
DR PhylomeDB; P13987; -.
DR TreeFam; TF338524; -.
DR PathwayCommons; P13987; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-5694530; Cargo concentration in the ER.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-977606; Regulation of Complement cascade.
DR SignaLink; P13987; -.
DR BioGRID-ORCS; 966; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; CD59; human.
DR EvolutionaryTrace; P13987; -.
DR GeneWiki; CD59; -.
DR GenomeRNAi; 966; -.
DR Pharos; P13987; Tbio.
DR PRO; PR:P13987; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P13987; protein.
DR Bgee; ENSG00000085063; Expressed in stromal cell of endometrium and 209 other tissues.
DR ExpressionAtlas; P13987; baseline and differential.
DR Genevisible; P13987; HS.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0001848; F:complement binding; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0001971; P:negative regulation of activation of membrane attack complex; IBA:GO_Central.
DR GO; GO:0030449; P:regulation of complement activation; IDA:MGI.
DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; IDA:MGI.
DR CDD; cd00117; LU; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR018363; CD59_antigen_CS.
DR InterPro; IPR027101; CD59_glyco.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR PANTHER; PTHR10036:SF9; PTHR10036:SF9; 1.
DR Pfam; PF00021; UPAR_LY6; 1.
DR SMART; SM00134; LU; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00983; LY6_UPAR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycation;
KW Glycoprotein; GPI-anchor; Hereditary hemolytic anemia; Lipoprotein;
KW Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:9054419,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 26..102
FT /note="CD59 glycoprotein"
FT /id="PRO_0000036108"
FT PROPEP 103..128
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:9054419"
FT /id="PRO_0000036109"
FT DOMAIN 26..108
FT /note="UPAR/Ly6"
FT LIPID 102
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000269|PubMed:17566972,
FT ECO:0000269|PubMed:8276756"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18780401,
FT ECO:0000269|PubMed:8670172"
FT CARBOHYD 66
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:10805801"
FT CARBOHYD 76
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 77
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT DISULFID 28..51
FT /evidence="ECO:0000269|PubMed:8276756"
FT DISULFID 31..38
FT /evidence="ECO:0000269|PubMed:8276756"
FT DISULFID 44..64
FT /evidence="ECO:0000269|PubMed:8276756"
FT DISULFID 70..88
FT /evidence="ECO:0000269|PubMed:8276756"
FT DISULFID 89..94
FT /evidence="ECO:0000269|PubMed:8276756"
FT VAR_SEQ 103..128
FT /note="GGTSLSEKTVLLLVTPFLAAAWSLHP -> DTFLKALKDEKLQGLKTKQPGK
FT KSASLS (in isoform 2)"
FT /id="VSP_060064"
FT VARIANT 89
FT /note="C -> Y (in HACD59; dbSNP:rs397514767)"
FT /evidence="ECO:0000269|PubMed:23149847"
FT /id="VAR_070124"
FT MUTAGEN 29
FT /note="Y->R: No loss of function."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 33
FT /note="N->R,Q: No loss of function."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 37
FT /note="D->R: No loss of function."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 48
FT /note="F->R: Some loss of function. Some lysis."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 49
FT /note="D->R: Loss of function. Lysis."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 58
FT /note="L->E: No loss of function."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 63
FT /note="K->E: No loss of function."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 65
FT /note="W->E: Complete loss of function. Lysis."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 66
FT /note="K->D: No loss of function."
FT /evidence="ECO:0000269|PubMed:10805801"
FT MUTAGEN 66
FT /note="K->Q: Loss of glycation mediated inactivation."
FT /evidence="ECO:0000269|PubMed:10805801"
FT MUTAGEN 67
FT /note="F->K: No loss of function."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 69
FT /note="H->Q: Loss of glycation mediated inactivation."
FT /evidence="ECO:0000269|PubMed:10805801"
FT MUTAGEN 72
FT /note="F->E: Almost complete loss of function. Lysis."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 78
FT /note="R->E: Loss of function. Lysis."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 79
FT /note="L->D: No loss of function."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 81
FT /note="E->R: Almost complete loss of function. Lysis."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 82
FT /note="N->K: No loss of function."
FT /evidence="ECO:0000269|PubMed:9053451"
FT MUTAGEN 87
FT /note="Y->R: No loss of function."
FT /evidence="ECO:0000269|PubMed:9053451"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2J8B"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1ERG"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2J8B"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:2J8B"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2J8B"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2J8B"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:2J8B"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2J8B"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1CDR"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2J8B"
SQ SEQUENCE 128 AA; 14177 MW; 2F0D29CBE3C28505 CRC64;
MGIQGGSVLF GLLLVLAVFC HSGHSLQCYN CPNPTADCKT AVNCSSDFDA CLITKAGLQV
YNKCWKFEHC NFNDVTTRLR ENELTYYCCK KDLCNFNEQL ENGGTSLSEK TVLLLVTPFL
AAAWSLHP
