CD59_PAPSP
ID CD59_PAPSP Reviewed; 126 AA.
AC Q28785;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 85.
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 Papio sp. (Baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio; unclassified Papio.
OX NCBI_TaxID=61183;
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; L22862; AAA74127.1; -; Genomic_DNA.
DR PIR; I36914; I36914.
DR AlphaFoldDB; Q28785; -.
DR SMR; Q28785; -.
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..100
FT /note="CD59 glycoprotein"
FT /id="PRO_0000036116"
FT PROPEP 101..126
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036117"
FT DOMAIN 26..106
FT /note="UPAR/Ly6"
FT LIPID 100
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 126 AA; 13716 MW; 7900FF937871EBDC CRC64;
MGIQGGSVLF GLLLALAVFC HSGHSLQCYN CPNPTTNCKT AINCSSGFDT CLIARAGLQV
YNQCWKFANC NFNDISTLLK ESELQYFCCK EDLCNEQLEN GGTSLSEKTV LLLVTPLLAA
AWCLHP
