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CD59 glycoprotein (1F5 antigen) (20 kDa homologous restriction factor) (HRF-20) (HRF20) (MAC-inhibitory protein) (MAC-IP) (MEM43 antigen) (Membrane attack complex inhibition factor) (MACIF) (Membrane inhibitor of reactive lysis) (MIRL) (Protectin) (CD antigen CD59)

 CD59_HUMAN              Reviewed;         128 AA.
P13987;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
12-SEP-2018, entry version 206.
RecName: Full=CD59 glycoprotein;
AltName: Full=1F5 antigen;
AltName: Full=20 kDa homologous restriction factor;
Short=HRF-20;
Short=HRF20;
AltName: Full=MAC-inhibitory protein;
Short=MAC-IP;
AltName: Full=MEM43 antigen;
AltName: Full=Membrane attack complex inhibition factor;
Short=MACIF;
AltName: Full=Membrane inhibitor of reactive lysis;
Short=MIRL;
AltName: Full=Protectin;
AltName: CD_antigen=CD59;
Flags: Precursor;
Name=CD59; Synonyms=MIC11, MIN1, MIN2, MIN3, MSK21;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=T-cell;
PubMed=2475570; DOI=10.1084/jem.170.3.637;
Davies A., Simmons D.L., Hale G., Harrison R.A., Tighe H.,
Lachmann P.J., Waldmann H.;
"CD59, an LY-6-like protein expressed in human lymphoid cells,
regulates the action of the complement membrane attack complex on
homologous cells.";
J. Exp. Med. 170:637-654(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1689664; DOI=10.1002/eji.1830200113;
Philbrick W.M., Palfree R.G.E., Roger G.E., Maher S.E., Bridgett M.M.,
Sirlin S., Bothwell A.L.M.;
"The CD59 antigen is a structural homologue of murine Ly-6 antigens
but lacks interferon inducibility.";
Eur. J. Immunol. 20:87-92(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2475111; DOI=10.1016/0006-291X(89)90852-8;
Okada H., Nagami Y., Takahashi K., Okada N., Hideshima T.,
Takizawa H., Kondo J.;
"20 KDa homologous restriction factor of complement resembles T cell
activating protein.";
Biochem. Biophys. Res. Commun. 162:1553-1559(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2606909;
Sugita Y., Tobe T., Oda E., Tomita M., Yasukawa K., Yamaji N.,
Takemoto T., Furuichi K., Takayama M., Yano S.;
"Molecular cloning and characterization of MACIF, an inhibitor of
membrane channel formation of complement.";
J. Biochem. 106:555-557(1989).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1692709; DOI=10.1089/dna.1990.9.213;
Sawada R., Ohashi K., Anaguchi H., Okazaki H., Hattori M., Minato N.,
Naruto M.;
"Isolation and expression of the full-length cDNA encoding CD59
antigen of human lymphocytes.";
DNA Cell Biol. 9:213-220(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1381503; DOI=10.1073/pnas.89.17.7876;
Petranka J.G., Fleenor D.E., Sykes K., Kaufman R.E., Rosse W.F.;
"Structure of the CD59-encoding gene: further evidence of a
relationship to murine lymphocyte antigen Ly-6 protein.";
Proc. Natl. Acad. Sci. U.S.A. 89:7876-7879(1992).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=1383553; DOI=10.1016/0022-2836(92)90239-G;
Tone M., Walsh L.A., Waldmann H.;
"Gene structure of human CD59 and demonstration that discrete mRNAs
are generated by alternative polyadenylation.";
J. Mol. Biol. 227:971-976(1992).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 27-128.
PubMed=2476718; DOI=10.1093/nar/17.16.6728;
Sawada R., Ohashi K., Okano K., Hattori M., Minato N., Naruto M.;
"Complementary DNA sequence and deduced peptide sequence for CD59/MEM-
43 antigen, the human homologue of murine lymphocyte antigen Ly-6C.";
Nucleic Acids Res. 17:6728-6728(1989).
[11]
PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION
AT ASN-43, AND STRUCTURE OF CARBOHYDRATES.
PubMed=8670172; DOI=10.1042/bj3160923;
Meri S., Lehto T., Sutton C.W., Tyynelaa J., Baumann M.;
"Structural composition and functional characterization of soluble
CD59: heterogeneity of the oligosaccharide and glycophosphoinositol
(GPI) anchor revealed by laser-desorption mass spectrometric
analysis.";
Biochem. J. 316:923-935(1996).
[12]
GPI-ANCHOR AT ASN-102, AND DISULFIDE BONDS.
PubMed=8276756;
Sugita Y., Nakano Y., Oda E., Noda K., Tobe T., Miura N.H., Tomita M.;
"Determination of carboxyl-terminal residue and disulfide bonds of
MACIF (CD59), a glycosyl-phosphatidylinositol-anchored membrane
protein.";
J. Biochem. 114:473-477(1993).
[13]
INTERACTION WITH C8 AND C9.
PubMed=1377690;
Ninomiya H., Sims P.J.;
"The human complement regulatory protein CD59 binds to the alpha-chain
of C8 and to the ''b'' domain of C9.";
J. Biol. Chem. 267:13675-13680(1992).
[14]
IDENTIFICATION OF COMPLEMENT INHIBITORY DOMAIN.
PubMed=9235986; DOI=10.1021/bi970832i;
Yu J., Dong S., Rushmere N.K., Morgan B.P., Abagyan R., Tomlinson S.;
"Mapping the regions of the complement inhibitor CD59 responsible for
its species selective activity.";
Biochemistry 36:9423-9428(1997).
[15]
MUTAGENESIS.
PubMed=9053451; DOI=10.1084/jem.185.3.507;
Bodian D.L., Davis S.J., Morgan B.P., Rushmere N.K.;
"Mutational analysis of the active site and antibody epitopes of the
complement-inhibitory glycoprotein, CD59.";
J. Exp. Med. 185:507-516(1997).
[16]
STRUCTURE OF CARBOHYDRATES, STRUCTURE OF THE GPI-ANCHOR, AND PROTEIN
SEQUENCE OF N-TERMINUS.
PubMed=9054419; DOI=10.1074/jbc.272.11.7229;
Rudd P.M., Morgan B.P., Wormald M.R., Harvey D.J., van den Berg C.W.,
Davis S.J., Ferguson M.A., Dwek R.A.;
"The glycosylation of the complement regulatory protein, human
erythrocyte CD59.";
J. Biol. Chem. 272:7229-7244(1997).
[17]
INHIBITION BY GLYCATION, GLYCATION AT LYS-66, AND MUTAGENESIS OF
LYS-66 AND HIS-69.
PubMed=10805801; DOI=10.1073/pnas.97.10.5450;
Acosta J., Hettinga J., Flueckiger R., Krumrei N., Goldfine A.,
Angarita L., Halperin J.;
"Molecular basis for a link between complement and the vascular
complications of diabetes.";
Proc. Natl. Acad. Sci. U.S.A. 97:5450-5455(2000).
[18]
GPI-ANCHOR AT ASN-102, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17566972; DOI=10.1002/pmic.200700068;
Omaetxebarria M.J., Elortza F., Rodriguez-Suarez E., Aloria K.,
Arizmendi J.M., Jensen O.N., Matthiesen R.;
"Computational approach for identification and characterization of
GPI-anchored peptides in proteomics experiments.";
Proteomics 7:1951-1960(2007).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-43.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER SER-25, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[23]
STRUCTURE BY NMR OF 26-95.
PubMed=7512825; DOI=10.1021/bi00181a006;
Kieffer B., Driscoll P.C., Campbell I.D., Willis A.C.,
van der Merwe P.A., Davis S.J.;
"Three-dimensional solution structure of the extracellular region of
the complement regulatory protein CD59, a new cell-surface protein
domain related to snake venom neurotoxins.";
Biochemistry 33:4471-4482(1994).
[24]
STRUCTURE BY NMR OF 26-102.
TISSUE=Urine;
PubMed=7520819; DOI=10.1016/S0969-2126(00)00020-4;
Fletcher C.M., Harrison R.A., Lachmann P.J., Neuhaus D.;
"Structure of a soluble, glycosylated form of the human complement
regulatory protein CD59.";
Structure 2:185-199(1994).
[25]
INVOLVEMENT IN HACD59.
PubMed=1382994; DOI=10.1002/eji.1830221029;
Motoyama N., Okada N., Yamashina M., Okada H.;
"Paroxysmal nocturnal hemoglobinuria due to hereditary nucleotide
deletion in the HRF20 (CD59) gene.";
Eur. J. Immunol. 22:2669-2673(1992).
[26]
VARIANT HACD59 TYR-89.
PubMed=23149847; DOI=10.1182/blood-2012-07-441857;
Nevo Y., Ben-Zeev B., Tabib A., Straussberg R., Anikster Y.,
Shorer Z., Fattal-Valevski A., Ta-Shma A., Aharoni S., Rabie M.,
Zenvirt S., Goldshmidt H., Fellig Y., Shaag A., Mevorach D.,
Elpeleg O.;
"CD59 deficiency is associated with chronic hemolysis and childhood
relapsing immune-mediated polyneuropathy.";
Blood 121:129-135(2013).
-!- FUNCTION: Potent inhibitor of the complement membrane attack
complex (MAC) action. Acts by binding to the C8 and/or C9
complements of the assembling MAC, thereby preventing
incorporation of the multiple copies of C9 required for complete
formation of the osmolytic pore. This inhibitor appears to be
species-specific. Involved in signal transduction for T-cell
activation complexed to a protein tyrosine kinase.
-!- FUNCTION: The soluble form from urine retains its specific
complement binding activity, but exhibits greatly reduced ability
to inhibit MAC assembly on cell membranes.
-!- SUBUNIT: Interacts with T-cell surface antigen CD2.
{ECO:0000269|PubMed:1377690}.
-!- INTERACTION:
Q778I9:C (xeno); NbExp=4; IntAct=EBI-297972, EBI-8716052;
O35587:TMED10 (xeno); NbExp=5; IntAct=EBI-297972, EBI-4405327;
Q15363:TMED2; NbExp=4; IntAct=EBI-297972, EBI-998485;
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
Secreted. Note=Soluble form found in a number of tissues.
-!- PTM: N- and O-glycosylated. The N-glycosylation mainly consists of
a family of biantennary complex-type structures with and without
lactosamine extensions and outer arm fucose residues. Also
significant amounts of triantennary complexes (22%). Variable
sialylation also present in the Asn-43 oligosaccharide. The
predominant O-glycans are mono-sialylated forms of the
disaccharide, Gal-beta-1,3GalNAc, and their sites of attachment
are probably on Thr-76 and Thr-77. The GPI-anchor of soluble
urinary CD59 has no inositol-associated phospholipid, but is
composed of seven different GPI-anchor variants of one or more
monosaccharide units. Major variants contain sialic acid, mannose
and glucosamine. Sialic acid linked to an N-acetylhexosamine-
galactose arm is present in two variants.
{ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:8670172}.
-!- PTM: Glycated. Glycation is found in diabetic subjects, but only
at minimal levels in nondiabetic subjects. Glycated CD59 lacks
MAC-inhibitory function and confers to vascular complications of
diabetes.
-!- DISEASE: Hemolytic anemia, CD59-mediated, with or without
polyneuropathy (HACD59) [MIM:612300]: An autosomal recessive
disorder characterized by infantile onset of chronic hemolysis and
a relapsing-remitting polyneuropathy, often exacerbated by
infection, and manifested as hypotonia, limb muscle weakness, and
hyporeflexia. {ECO:0000269|PubMed:1382994,
ECO:0000269|PubMed:23149847}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=CD59base; Note=CD59 mutation db;
URL="http://structure.bmc.lu.se/idbase/CD59base/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CD59ID985ch11p13.html";
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EMBL; M27909; AAA60543.1; -; mRNA.
EMBL; M95708; AAA60957.1; -; mRNA.
EMBL; X16447; CAA34467.1; -; mRNA.
EMBL; X17198; CAA35059.1; -; mRNA.
EMBL; M34671; AAA51952.1; -; mRNA.
EMBL; M84345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M84349; AAA88793.1; -; Genomic_DNA.
EMBL; M84346; AAA88793.1; JOINED; Genomic_DNA.
EMBL; M84348; AAA88793.1; JOINED; Genomic_DNA.
EMBL; Z14113; CAA78486.1; -; Genomic_DNA.
EMBL; Z14114; CAA78486.1; JOINED; Genomic_DNA.
EMBL; Z14115; CAA78486.1; JOINED; Genomic_DNA.
EMBL; BT007104; AAP35768.1; -; mRNA.
EMBL; BC001506; AAH01506.1; -; mRNA.
CCDS; CCDS7886.1; -.
PIR; A46252; RWHU59.
RefSeq; NP_000602.1; NM_000611.5.
RefSeq; NP_001120695.1; NM_001127223.1.
RefSeq; NP_001120697.1; NM_001127225.1.
RefSeq; NP_001120698.1; NM_001127226.1.
RefSeq; NP_001120699.1; NM_001127227.1.
RefSeq; NP_976074.1; NM_203329.2.
RefSeq; NP_976075.1; NM_203330.2.
RefSeq; NP_976076.1; NM_203331.2.
UniGene; Hs.278573; -.
UniGene; Hs.709466; -.
UniGene; Hs.710641; -.
PDB; 1CDQ; NMR; -; A=26-102.
PDB; 1CDR; NMR; -; A=26-102.
PDB; 1CDS; NMR; -; A=26-102.
PDB; 1ERG; NMR; -; A=26-95.
PDB; 1ERH; NMR; -; A=26-95.
PDB; 2J8B; X-ray; 1.15 A; A=26-103.
PDB; 2OFS; X-ray; 2.12 A; A=26-99.
PDB; 2UWR; X-ray; 1.34 A; A=26-102.
PDB; 2UX2; X-ray; 1.80 A; A/B/C=26-102.
PDB; 4BIK; X-ray; 3.49 A; B/D=26-102.
PDB; 5IMT; X-ray; 2.70 A; D=26-102.
PDB; 5IMY; X-ray; 2.40 A; C/D=26-102.
PDBsum; 1CDQ; -.
PDBsum; 1CDR; -.
PDBsum; 1CDS; -.
PDBsum; 1ERG; -.
PDBsum; 1ERH; -.
PDBsum; 2J8B; -.
PDBsum; 2OFS; -.
PDBsum; 2UWR; -.
PDBsum; 2UX2; -.
PDBsum; 4BIK; -.
PDBsum; 5IMT; -.
PDBsum; 5IMY; -.
ProteinModelPortal; P13987; -.
SMR; P13987; -.
BioGrid; 107404; 37.
IntAct; P13987; 26.
MINT; P13987; -.
STRING; 9606.ENSP00000340210; -.
GlyConnect; 79; -.
iPTMnet; P13987; -.
PhosphoSitePlus; P13987; -.
SwissPalm; P13987; -.
UniCarbKB; P13987; -.
BioMuta; CD59; -.
DMDM; 116021; -.
EPD; P13987; -.
PaxDb; P13987; -.
PeptideAtlas; P13987; -.
PRIDE; P13987; -.
ProteomicsDB; 53014; -.
DNASU; 966; -.
Ensembl; ENST00000351554; ENSP00000340210; ENSG00000085063.
Ensembl; ENST00000395850; ENSP00000379191; ENSG00000085063.
Ensembl; ENST00000415002; ENSP00000404822; ENSG00000085063.
Ensembl; ENST00000426650; ENSP00000402425; ENSG00000085063.
Ensembl; ENST00000437761; ENSP00000410182; ENSG00000085063.
Ensembl; ENST00000445143; ENSP00000403511; ENSG00000085063.
Ensembl; ENST00000527577; ENSP00000432942; ENSG00000085063.
Ensembl; ENST00000642928; ENSP00000494884; ENSG00000085063.
GeneID; 966; -.
KEGG; hsa:966; -.
CTD; 966; -.
DisGeNET; 966; -.
EuPathDB; HostDB:ENSG00000085063.14; -.
GeneCards; CD59; -.
H-InvDB; HIX0171358; -.
HGNC; HGNC:1689; CD59.
HPA; CAB001448; -.
HPA; HPA026494; -.
MalaCards; CD59; -.
MIM; 107271; gene.
MIM; 612300; phenotype.
neXtProt; NX_P13987; -.
OpenTargets; ENSG00000085063; -.
Orphanet; 169464; Primary CD59 deficiency.
PharmGKB; PA26228; -.
eggNOG; ENOG410J39P; Eukaryota.
eggNOG; ENOG410ZEQP; LUCA.
GeneTree; ENSGT00390000016309; -.
HOGENOM; HOG000232180; -.
HOVERGEN; HBG005284; -.
InParanoid; P13987; -.
KO; K04008; -.
OMA; NSDLCNS; -.
PhylomeDB; P13987; -.
TreeFam; TF338524; -.
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-977606; Regulation of Complement cascade.
ChiTaRS; CD59; human.
EvolutionaryTrace; P13987; -.
GeneWiki; CD59; -.
GenomeRNAi; 966; -.
PRO; PR:P13987; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000085063; Expressed in 234 organ(s), highest expression level in chorionic villus.
CleanEx; HS_CD59; -.
ExpressionAtlas; P13987; baseline and differential.
Genevisible; P13987; HS.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0001848; F:complement binding; IBA:GO_Central.
GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
GO; GO:0001775; P:cell activation; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0001971; P:negative regulation of activation of membrane attack complex; IEA:InterPro.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; IBA:GO_Central.
InterPro; IPR018363; CD59_antigen_CS.
InterPro; IPR027101; CD59_glyco.
InterPro; IPR016054; LY6_UPA_recep-like.
PANTHER; PTHR10036:SF9; PTHR10036:SF9; 1.
Pfam; PF00021; UPAR_LY6; 1.
SMART; SM00134; LU; 1.
PROSITE; PS00983; LY6_UPAR; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycation; Glycoprotein; GPI-anchor; Hereditary hemolytic anemia;
Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
SIGNAL 1 25 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:9054419}.
CHAIN 26 102 CD59 glycoprotein.
/FTId=PRO_0000036108.
PROPEP 103 128 Removed in mature form.
{ECO:0000269|PubMed:9054419}.
/FTId=PRO_0000036109.
DOMAIN 26 108 UPAR/Ly6.
LIPID 102 102 GPI-anchor amidated asparagine.
{ECO:0000269|PubMed:17566972,
ECO:0000269|PubMed:8276756}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:8670172}.
CARBOHYD 66 66 N-linked (Glc) (glycation) lysine.
{ECO:0000269|PubMed:10805801}.
CARBOHYD 76 76 O-linked (GalNAc...) threonine.
{ECO:0000305}.
CARBOHYD 77 77 O-linked (GalNAc...) threonine.
{ECO:0000305}.
DISULFID 28 51 {ECO:0000269|PubMed:8276756}.
DISULFID 31 38 {ECO:0000269|PubMed:8276756}.
DISULFID 44 64 {ECO:0000269|PubMed:8276756}.
DISULFID 70 88 {ECO:0000269|PubMed:8276756}.
DISULFID 89 94 {ECO:0000269|PubMed:8276756}.
VARIANT 89 89 C -> Y (in HACD59; dbSNP:rs397514767).
{ECO:0000269|PubMed:23149847}.
/FTId=VAR_070124.
MUTAGEN 29 29 Y->R: No loss of function.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 33 33 N->R,Q: No loss of function.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 37 37 D->R: No loss of function.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 48 48 F->R: Some loss of function. Some lysis.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 49 49 D->R: Loss of function. Lysis.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 58 58 L->E: No loss of function.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 63 63 K->E: No loss of function.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 65 65 W->E: Complete loss of function. Lysis.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 66 66 K->D: No loss of function.
{ECO:0000269|PubMed:10805801}.
MUTAGEN 66 66 K->Q: Loss of glycation mediated
inactivation.
{ECO:0000269|PubMed:10805801}.
MUTAGEN 67 67 F->K: No loss of function.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 69 69 H->Q: Loss of glycation mediated
inactivation.
{ECO:0000269|PubMed:10805801}.
MUTAGEN 72 72 F->E: Almost complete loss of function.
Lysis. {ECO:0000269|PubMed:9053451}.
MUTAGEN 78 78 R->E: Loss of function. Lysis.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 79 79 L->D: No loss of function.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 81 81 E->R: Almost complete loss of function.
Lysis. {ECO:0000269|PubMed:9053451}.
MUTAGEN 82 82 N->K: No loss of function.
{ECO:0000269|PubMed:9053451}.
MUTAGEN 87 87 Y->R: No loss of function.
{ECO:0000269|PubMed:9053451}.
STRAND 27 29 {ECO:0000244|PDB:2J8B}.
STRAND 32 34 {ECO:0000244|PDB:1ERG}.
STRAND 41 43 {ECO:0000244|PDB:2J8B}.
STRAND 50 56 {ECO:0000244|PDB:2J8B}.
STRAND 59 65 {ECO:0000244|PDB:2J8B}.
HELIX 67 69 {ECO:0000244|PDB:2J8B}.
HELIX 72 79 {ECO:0000244|PDB:2J8B}.
STRAND 85 89 {ECO:0000244|PDB:2J8B}.
STRAND 91 93 {ECO:0000244|PDB:1CDR}.
HELIX 97 99 {ECO:0000244|PDB:2J8B}.
SEQUENCE 128 AA; 14177 MW; 2F0D29CBE3C28505 CRC64;
MGIQGGSVLF GLLLVLAVFC HSGHSLQCYN CPNPTADCKT AVNCSSDFDA CLITKAGLQV
YNKCWKFEHC NFNDVTTRLR ENELTYYCCK KDLCNFNEQL ENGGTSLSEK TVLLLVTPFL
AAAWSLHP


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