ID   CD59_CHLAE              Reviewed;         128 AA.
AC   Q28216;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=CD59 glycoprotein;
DE   AltName: Full=MAC-inhibitory protein;
DE            Short=MAC-IP;
DE   AltName: Full=Membrane attack complex inhibition factor;
DE            Short=MACIF;
DE   AltName: Full=Protectin;
DE   AltName: CD_antigen=CD59;
DE   Flags: Precursor;
GN   Name=CD59;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7528724; DOI=10.1007/bf00188435;
RA   Fodor W.L., Rollins S.A., Bianco-Caron S., Burton W.V., Guilmette E.R.,
RA   Rother R.P., Zavoico G.B., Squinto S.P.;
RT   "Primate terminal complement inhibitor homologues of human CD59.";
RL   Immunogenetics 41:51-51(1995).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with T-cell surface antigen CD2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- PTM: N- and O-glycosylated. {ECO:0000250}.
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DR   EMBL; L22863; AAA74126.1; -; Genomic_DNA.
DR   PIR; I36894; I36894.
DR   AlphaFoldDB; Q28216; -.
DR   SMR; Q28216; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001971; P:negative regulation of activation of membrane attack complex; IEA:InterPro.
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   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..102
FT                   /note="CD59 glycoprotein"
FT                   /id="PRO_0000036106"
FT   PROPEP          103..128
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036107"
FT   DOMAIN          26..108
FT                   /note="UPAR/Ly6"
FT   LIPID           102
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..51
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..38
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..64
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..88
FT                   /evidence="ECO:0000250"
FT   DISULFID        89..94
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   128 AA;  14007 MW;  9778DEF7F7F05152 CRC64;
     MGIQGGSVLF GLLLVLAVFC HSGHSLQCYN CPNPTTDCKT AINCSSGFDT CLIARAGLQV
     YNQCWKFANC NFNDISTLLK ESELQYFCCK KDLCNFNEQL ENGGTSLSEK TVVLLVTLLL
     AAAWCLHP