CD59 glycoprotein precursor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P13987 (CD59_HUMAN)

Last modified January 19, 2010. Version 125. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    CD59 glycoprotein
Alternative name(s):
    Membrane attack complex inhibition factor
      Short name=MACIF
    MAC-inhibitory protein
      Short name=MAC-IP
    Protectin
    MEM43 antigen
    Membrane inhibitor of reactive lysis
      Short name=MIRL
    20 kDa homologous restriction factor
    HRF-20
      Short name=HRF20
    1F5 antigen
    CD_antigen=CD59

Gene names

Name:	CD59
Synonyms:	MIC11, MIN1, MIN2, MIN3, MSK21

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	128 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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. The soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit MAC assembly on cell membranes.
Subunit structure	Interacts with T-cell surface antigen CD2. Ref.13
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor. Secreted. Note: Soluble form found in a number of tissues. Ref.12 Ref.16 Ref.18 Ref.19
Post-translational modification	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. Ref.16 Ref.11 Ref.20 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.
Involvement in disease	Defects in CD59 are the cause of CD59 deficiency [MIM:612300]. Ref.24
Sequence similarities	Contains 1 UPAR/Ly6 domain.

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Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Domain	Signal
PTM	Disulfide bond GPI-anchor Glycation Glycoprotein Lipoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	blood coagulation Ref.6 Traceable author statement. Source: ProtInc cell surface receptor linked signal transduction Traceable author statement. Source: ProtInc
Cellular component	anchored to external side of plasma membrane Inferred from direct assay. Source: MGI extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Ref.6 Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
EGFR	P00533	1	EBI-297972,EBI-297353

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

Chain

26 – 102

CD59 glycoprotein

PRO_0000036108

Propeptide

103 – 128

Removed in mature form

PRO_0000036109

Regions

Domain

26 – 108

UPAR/Ly6

Amino acid modifications

Modified residue

Phosphotyrosine Ref.21

Modified residue

Phosphotyrosine Ref.21

Lipidation

102

GPI-anchor amidated asparagine Ref.12 Ref.16 Ref.18 Ref.19

Glycosylation

N-linked (GlcNAc...) Ref.11 Ref.20

Glycosylation

N-linked (Glc) (glycation) Ref.17

Glycosylation

N-linked (Glc) (glycation) Ref.17

Glycosylation

O-linked (GlcNAc...) Probable

Glycosylation

O-linked (GlcNAc...) Probable

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Experimental info

Mutagenesis

Y → R: No loss of function.

Mutagenesis

N → R or Q: No loss of function.

Mutagenesis

D → R: No loss of function.

Mutagenesis

F → R: Some loss of function. Some lysis.

Mutagenesis

D → R: Loss of function. Lysis.

Mutagenesis

L → E: No loss of function.

Mutagenesis

K → E: No loss of function.

Mutagenesis

W → E: Complete loss of function. Lysis.

Mutagenesis

K → D: No loss of function. Ref.17

Mutagenesis

K → Q: Loss of glycation mediated inactivation. Ref.17

Mutagenesis

F → K: No loss of function.

Mutagenesis

H → Q: Loss of glycation mediated inactivation. Ref.17

Mutagenesis

F → E: Almost complete loss of function. Lysis.

Mutagenesis

R → E: Loss of function. Lysis.

Mutagenesis

L → D: No loss of function.

Mutagenesis

E → R: Almost complete loss of function. Lysis.

Mutagenesis

N → K: No loss of function.

Mutagenesis

Y → R: No loss of function.

Secondary structure

128

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P13987-1 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 2F0D29CBE3C28505
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FASTA

128

14,177

        10         20         30         40         50         60 
MGIQGGSVLF GLLLVLAVFC HSGHSLQCYN CPNPTADCKT AVNCSSDFDA CLITKAGLQV 

        70         80         90        100        110        120 
YNKCWKFEHC NFNDVTTRLR ENELTYYCCK KDLCNFNEQL ENGGTSLSEK TVLLLVTPFL 


AAAWSLHP

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CD59, an LY-6-like protein expressed in human lymphoid cells, regulates the action of the complement membrane attack complex on homologous cells." Davies A., Simmons D.L., Hale G., Harrison R.A., Tighe H., Lachmann P.J., Waldmann H. J. Exp. Med. 170:637-654(1989) [PubMed: 2475570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: T-cell.
[2]	"The CD59 antigen is a structural homologue of murine Ly-6 antigens but lacks interferon inducibility." Philbrick W.M., Palfree R.G.E., Roger G.E., Maher S.E., Bridgett M.M., Sirlin S., Bothwell A.L.M. Eur. J. Immunol. 20:87-92(1990) [PubMed: 1689664] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"20 KDa homologous restriction factor of complement resembles T cell activating protein." Okada H., Nagami Y., Takahashi K., Okada N., Hideshima T., Takizawa H., Kondo J. Biochem. Biophys. Res. Commun. 162:1553-1559(1989) [PubMed: 2475111] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Molecular cloning and characterization of MACIF, an inhibitor of membrane channel formation of complement." Sugita Y., Tobe T., Oda E., Tomita M., Yasukawa K., Yamaji N., Takemoto T., Furuichi K., Takayama M., Yano S. J. Biochem. 106:555-557(1989) [PubMed: 2606909] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Isolation and expression of the full-length cDNA encoding CD59 antigen of human lymphocytes." Sawada R., Ohashi K., Anaguchi H., Okazaki H., Hattori M., Minato N., Naruto M. DNA Cell Biol. 9:213-220(1990) [PubMed: 1692709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Structure of the CD59-encoding gene: further evidence of a relationship to murine lymphocyte antigen Ly-6 protein." Petranka J.G., Fleenor D.E., Sykes K., Kaufman R.E., Rosse W.F. Proc. Natl. Acad. Sci. U.S.A. 89:7876-7879(1992) [PubMed: 1381503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Gene structure of human CD59 and demonstration that discrete mRNAs are generated by alternative polyadenylation." Tone M., Walsh L.A., Waldmann H. J. Mol. Biol. 227:971-976(1992) [PubMed: 1383553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood.
[8]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[10]	"Complementary DNA sequence and deduced peptide sequence for CD59/MEM-43 antigen, the human homologue of murine lymphocyte antigen Ly-6C." Sawada R., Ohashi K., Okano K., Hattori M., Minato N., Naruto M. Nucleic Acids Res. 17:6728-6728(1989) [PubMed: 2476718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-128.
[11]	"Structural composition and functional characterization of soluble CD59: heterogeneity of the oligosaccharide and glycophosphoinositol (GPI) anchor revealed by laser-desorption mass spectrometric analysis." Meri S., Lehto T., Sutton C.W., Tyynelaa J., Baumann M. Biochem. J. 316:923-935(1996) [PubMed: 8670172] [Abstract] Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY, GLYCOSYLATION AT ASN-43, STRUCTURE OF CARBOHYDRATES.
[12]	"Determination of carboxyl-terminal residue and disulfide bonds of MACIF (CD59), a glycosyl-phosphatidylinositol-anchored membrane protein." Sugita Y., Nakano Y., Oda E., Noda K., Tobe T., Miura N.H., Tomita M. J. Biochem. 114:473-477(1993) [PubMed: 8276756] [Abstract] Cited for: GPI-ANCHOR AT ASN-102, DISULFIDE BONDS.
[13]	"The human complement regulatory protein CD59 binds to the alpha-chain of C8 and to the ''b'' domain of C9." Ninomiya H., Sims P.J. J. Biol. Chem. 267:13675-13680(1992) [PubMed: 1377690] [Abstract] Cited for: INTERACTION WITH C8 AND C9.
[14]	"Mapping the regions of the complement inhibitor CD59 responsible for its species selective activity." Yu J., Dong S., Rushmere N.K., Morgan B.P., Abagyan R., Tomlinson S. Biochemistry 36:9423-9428(1997) [PubMed: 9235986] [Abstract] Cited for: IDENTIFICATION OF COMPLEMENT INHIBITORY DOMAIN.
[15]	"Mutational analysis of the active site and antibody epitopes of the complement-inhibitory glycoprotein, CD59." Bodian D.L., Davis S.J., Morgan B.P., Rushmere N.K. J. Exp. Med. 185:507-516(1997) [PubMed: 9053451] [Abstract] Cited for: MUTAGENESIS.
[16]	"The glycosylation of the complement regulatory protein, human erythrocyte CD59." 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. J. Biol. Chem. 272:7229-7244(1997) [PubMed: 9054419] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATES, STRUCTURE OF THE GPI-ANCHOR, PROTEIN SEQUENCE OF N-TERMINUS.
[17]	"Molecular basis for a link between complement and the vascular complications of diabetes." Acosta J., Hettinga J., Flueckiger R., Krumrei N., Goldfine A., Angarita L., Halperin J. Proc. Natl. Acad. Sci. U.S.A. 97:5450-5455(2000) [PubMed: 10805801] [Abstract] Cited for: INHIBITION BY GLYCATION, GLYCATION AT LYS-66 AND HIS-69, MUTAGENESIS OF LYS-66 AND HIS-69.
[18]	"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins." Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N. Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed: 14517339] [Abstract] Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment." Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N. J. Proteome Res. 5:935-943(2006) [PubMed: 16602701] [Abstract] Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry." Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F. Proteomics 8:3833-3847(2008) [PubMed: 18780401] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-43, MASS SPECTROMETRY. Tissue: Milk.
[21]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29 AND TYR-86, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[22]	"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." Kieffer B., Driscoll P.C., Campbell I.D., Willis A.C., van der Merwe P.A., Davis S.J. Biochemistry 33:4471-4482(1994) [PubMed: 7512825] [Abstract] Cited for: STRUCTURE BY NMR OF 26-95.
[23]	"Structure of a soluble, glycosylated form of the human complement regulatory protein CD59." Fletcher C.M., Harrison R.A., Lachmann P.J., Neuhaus D. Structure 2:185-199(1994) [PubMed: 7520819] [Abstract] Cited for: STRUCTURE BY NMR OF 26-102. Tissue: Urine.
[24]	"Paroxysmal nocturnal hemoglobinuria due to hereditary nucleotide deletion in the HRF20 (CD59) gene." Motoyama N., Okada N., Yamashina M., Okada H. Eur. J. Immunol. 22:2669-2673(1992) [PubMed: 1382994] [Abstract] Cited for: INVOLVEMENT IN CD59 DEFICIENCY.
+	Additional computationally mapped references.

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Web resources

CD59base

CD59 mutation db

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M27909 mRNA. Translation: AAA60543.1.
M95708 mRNA. Translation: AAA60957.1.
X16447 mRNA. Translation: CAA34467.1.
X17198 mRNA. Translation: CAA35059.1.
M34671 mRNA. Translation: AAA51952.1.
M84345 Genomic DNA. No translation available.
M84349, M84346, M84348 Genomic DNA. Translation: AAA88793.1.
Z14113, Z14114, Z14115 Genomic DNA. Translation: CAA78486.1.
BT007104 mRNA. Translation: AAP35768.1.
BC001506 mRNA. Translation: AAH01506.1.

IPI

IPI00011302.

PIR

RWHU59. A46252.

RefSeq

NP_000602.1.
NP_001120695.1.
NP_001120697.1.
NP_001120698.1.
NP_001120699.1.
NP_976074.1.
NP_976075.1.
NP_976076.1.

UniGene

Hs.278573
Hs.709466
Hs.710641

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CDQ	NMR	-	A	26-102	[»]
1CDR	NMR	-	A	26-102	[»]
1CDS	NMR	-	A	26-102	[»]
1ERG	NMR	-	A	26-95	[»]
1ERH	NMR	-	A	26-95	[»]
2J8B	X-ray	1.15	A	26-103	[»]
2OFS	X-ray	2.12	A	26-99	[»]
2UWR	X-ray	1.34	A	26-102	[»]
2UX2	X-ray	1.80	A/B/C	26-102	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P13987. 3 interactions.

STRING

P13987.

PTM databases

GlycoSuiteDB

P13987.

Proteomic databases

PeptideAtlas

P13987.

PRIDE

P13987.

Genome annotation databases

Ensembl

ENST00000351554; ENSP00000340210; ENSG00000085063; Homo sapiens. [Genome view]
ENST00000395850; ENSP00000379191; ENSG00000085063; Homo sapiens. [Genome view]
ENST00000415002; ENSP00000404822; ENSG00000085063; Homo sapiens. [Genome view]
ENST00000418830; ENSP00000412062; ENSG00000085063; Homo sapiens. [Genome view]
ENST00000426650; ENSP00000402425; ENSG00000085063; Homo sapiens. [Genome view]
ENST00000437761; ENSP00000410182; ENSG00000085063; Homo sapiens. [Genome view]
ENST00000445143; ENSP00000403511; ENSG00000085063; Homo sapiens. [Genome view]

GeneID

966.

KEGG

hsa:966.

UCSC

uc001mus.2. human.

Organism-specific databases

CTD

966.

GeneCards

GC11M033681.

H-InvDB

HIX0009542.

HGNC

HGNC:1689. CD59.

HPA

CAB001448.
HPA026494.

MIM

107271. gene.
612300. phenotype.

PharmGKB

PA26228.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20873.

HOGENOM

HBG125973.

HOVERGEN

P13987.

InParanoid

P13987.

OMA

CHSGHSL.

OrthoDB

EOG94TRT3.

PhylomeDB

P13987.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6_traffickingpathway. Arf6 trafficking events.

Gene expression databases

ArrayExpress

P13987.

Bgee

P13987.

CleanEx

HS_CD59.

Genevestigator

P13987.

GermOnline

ENSG00000085063. Homo sapiens.

Family and domain databases

InterPro

IPR018363. CD59_antigen_CS.
IPR016054. LY6_UPA_recep-like.
IPR001526. LY6_UPAR.
[Graphical view]

Pfam

PF00021. UPAR_LY6. 1 hit.
[Graphical view]

SMART

SM00134. LU. 1 hit.
[Graphical view]

PROSITE

PS00983. LY6_UPAR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

4034.

SOURCE

Search...

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Entry information

Entry name

CD59_HUMAN

Accession

Primary (citable) accession number: P13987

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	January 19, 2010
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents