ID   CD59_RABIT              Reviewed;         124 AA.
AC   O77541;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 109.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-64.
RC   TISSUE=Erythrocyte, and Lymphocyte;
RX   PubMed=9553129; DOI=10.1074/jbc.273.17.10665;
RA   Zhao X.-J., Zhao J., Zhou Q., Sims P.J.;
RT   "Identity of the residues responsible for the species-restricted complement
RT   inhibitory function of human CD59.";
RL   J. Biol. Chem. 273:10665-10671(1998).
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.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- MISCELLANEOUS: The mature form of this CD59 contains an additional
CC       serine residue before the conserved N-terminal leucine residue found in
CC       all other CD59 homologs sequenced to date.
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DR   EMBL; AF040387; AAC23590.1; -; mRNA.
DR   RefSeq; NP_001076181.1; NM_001082712.1.
DR   AlphaFoldDB; O77541; -.
DR   SMR; O77541; -.
DR   STRING; 9986.ENSOCUP00000016507; -.
DR   GeneID; 100009459; -.
DR   KEGG; ocu:100009459; -.
DR   CTD; 966; -.
DR   eggNOG; ENOG502SA4P; Eukaryota.
DR   InParanoid; O77541; -.
DR   Proteomes; UP000001811; Unplaced.
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   Pfam; PF00021; UPAR_LY6; 1.
DR   SMART; SM00134; LU; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:9553129"
FT   CHAIN           25..101
FT                   /note="CD59 glycoprotein"
FT                   /id="PRO_0000036122"
FT   PROPEP          102..124
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036123"
FT   DOMAIN          25..101
FT                   /note="UPAR/Ly6"
FT   LIPID           101
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        37
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   124 AA;  13870 MW;  CEA64C816772CABD CRC64;
     MTSRGVHLLL RLLFLLAVFY SSDSSLMCYH CLLPSPNCST VTNCTPNHDA CLTAVSGPRV
     YRQCWRYEDC NFEFISNRLE ENSLKYNCCR KDLCNGPEDD GTALTGRTVL LVAPLLAAAR
     NLCL