CD59_PONAB
ID CD59_PONAB Reviewed; 128 AA.
AC Q5R510;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR861075; CAH93156.1; -; mRNA.
DR RefSeq; NP_001126861.1; NM_001133389.1.
DR AlphaFoldDB; Q5R510; -.
DR SMR; Q5R510; -.
DR STRING; 9601.ENSPPYP00000003871; -.
DR Ensembl; ENSPPYT00000004019; ENSPPYP00000003871; ENSPPYG00000003370.
DR GeneID; 100173870; -.
DR KEGG; pon:100173870; -.
DR CTD; 966; -.
DR eggNOG; ENOG502SA4P; Eukaryota.
DR GeneTree; ENSGT00390000016309; -.
DR HOGENOM; CLU_147732_1_0_1; -.
DR InParanoid; Q5R510; -.
DR OMA; CSKQRDC; -.
DR OrthoDB; 1586315at2759; -.
DR TreeFam; TF338524; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0001971; P:negative regulation of activation of membrane attack complex; IEA:InterPro.
DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..102
FT /note="CD59 glycoprotein"
FT /id="PRO_0000036120"
FT PROPEP 103..128
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036121"
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; 14020 MW; 7C853802F0C3E825 CRC64;
MGIQGGSVLF GLLLILAVFC HSGHSLQCYS CPNPTADCKT AVNCSSGFDA CLITKAGLRV
YNQCWKFEHC TFNEVTTRLK ESELTYHCCK KDLCNINEQL ENGGTSLSEK TVLLLVTPFL
AAAWSLHP
