ID   CD59_SAISC              Reviewed;         131 AA.
AC   P47777;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
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   Saimiri sciureus (Common squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=9521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=7507185; DOI=10.1128/jvi.68.2.730-737.1994;
RA   Rother R.P., Rollins S.A., Fodor W.L., Albrecht J.-C., Setter E.,
RA   Fleckenstein B., Squinto S.P.;
RT   "Inhibition of complement-mediated cytolysis by the terminal complement
RT   inhibitor of herpesvirus saimiri.";
RL   J. Virol. 68:730-737(1994).
CC   -!- FUNCTION: Potent inhibitor of the complement membrane attack complex
CC       (MAC) action. Acts at or after the C5b-8 stage of MAC assembly.
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; L22859; AAA16747.1; -; mRNA.
DR   PIR; I56894; I56894.
DR   AlphaFoldDB; P47777; -.
DR   SMR; P47777; -.
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; 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   SMART; SM00134; LU; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..105
FT                   /note="CD59 glycoprotein"
FT                   /id="PRO_0000036126"
FT   PROPEP          106..131
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036127"
FT   DOMAIN          26..111
FT                   /note="UPAR/Ly6"
FT   LIPID           105
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..54
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..41
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..67
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        92..97
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   131 AA;  14355 MW;  47A739CBE9E4609E CRC64;
     MGIQGGSVLF GLLLVLAVFC HSGNSLQCYS CPLPTMESME CTASTNCTSN LDSCLIAKAG
     SGVYYRCWKF DDCSFKRISN QLSETQLKYH CCKKNLCNVK EVLENGGTTL SKKTILLLVT
     PFLAAAWSRH P