CD59_PIG
ID CD59_PIG Reviewed; 123 AA.
AC O62680; Q9TR76; Q9XT94;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aortic endothelium;
RX PubMed=9558099;
RA Hinchliffe S.J., Rushmere N.K., Hanna S.M., Morgan B.P.;
RT "Molecular cloning and functional characterization of the pig analogue of
RT CD59: relevance to xenotransplantation.";
RL J. Immunol. 160:3924-3932(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-123, AND FUNCTION.
RC TISSUE=Aortic endothelium;
RX PubMed=9808497; DOI=10.1097/00007890-199810270-00021;
RA Maher S.E., Pflugh D.L., Larsen N.J., Rothschild M.F., Bothwell A.L.M.;
RT "Structure/function characterization of porcine CD59: expression,
RT chromosomal mapping, complement-inhibition, and costimulatory activity.";
RL Transplantation 66:1094-1100(1998).
RN [3]
RP PROTEIN SEQUENCE OF 26-64.
RC TISSUE=Erythrocyte;
RX PubMed=7533195; DOI=10.1016/0022-1759(94)00288-8;
RA van den Berg C.W., Harrison R.A., Morgan B.P.;
RT "A rapid method for the isolation of analogues of human CD59 by preparative
RT SDS-PAGE: application to pig CD59.";
RL J. Immunol. Methods 179:223-231(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.
CC {ECO:0000269|PubMed:9808497}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested (lung, testis
CC liver, kidney, spleen, heart and skeletal muscle). Highest levels in
CC lung and spleen, lowest levels in liver and skeletal muscle.
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DR EMBL; AF020302; AAC67231.1; -; mRNA.
DR EMBL; AF058328; AAD39837.1; -; mRNA.
DR RefSeq; NP_999335.1; NM_214170.1.
DR RefSeq; XP_005661088.1; XM_005661031.2.
DR AlphaFoldDB; O62680; -.
DR SMR; O62680; -.
DR STRING; 9823.ENSSSCP00000025898; -.
DR PaxDb; O62680; -.
DR PeptideAtlas; O62680; -.
DR PRIDE; O62680; -.
DR Ensembl; ENSSSCT00000026025; ENSSSCP00000025898; ENSSSCG00000024791.
DR Ensembl; ENSSSCT00005068056; ENSSSCP00005042308; ENSSSCG00005042427.
DR Ensembl; ENSSSCT00025025695; ENSSSCP00025010860; ENSSSCG00025018939.
DR Ensembl; ENSSSCT00035072171; ENSSSCP00035029307; ENSSSCG00035054075.
DR Ensembl; ENSSSCT00040084790; ENSSSCP00040037016; ENSSSCG00040062263.
DR Ensembl; ENSSSCT00045057486; ENSSSCP00045040202; ENSSSCG00045033618.
DR Ensembl; ENSSSCT00050052466; ENSSSCP00050022024; ENSSSCG00050038907.
DR Ensembl; ENSSSCT00055025697; ENSSSCP00055020421; ENSSSCG00055013062.
DR Ensembl; ENSSSCT00060042460; ENSSSCP00060018085; ENSSSCG00060031379.
DR Ensembl; ENSSSCT00065038021; ENSSSCP00065016037; ENSSSCG00065028199.
DR GeneID; 397347; -.
DR KEGG; ssc:397347; -.
DR CTD; 966; -.
DR VGNC; VGNC:99615; CD59.
DR eggNOG; ENOG502SA4P; Eukaryota.
DR GeneTree; ENSGT00390000016309; -.
DR HOGENOM; CLU_147732_1_0_1; -.
DR InParanoid; O62680; -.
DR OMA; CSKQRDC; -.
DR OrthoDB; 1586315at2759; -.
DR TreeFam; TF338524; -.
DR Reactome; R-SSC-204005; COPII-mediated vesicle transport.
DR Reactome; R-SSC-5694530; Cargo concentration in the ER.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Reactome; R-SSC-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SSC-977606; Regulation of Complement cascade.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000024791; Expressed in endocardial endothelium and 43 other tissues.
DR Genevisible; O62680; SS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001848; F:complement binding; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IDA:AgBase.
DR GO; GO:0001971; P:negative regulation of activation of membrane attack complex; IBA:GO_Central.
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 SMART; SM00134; LU; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00983; LY6_UPAR; 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..25
FT /evidence="ECO:0000269|PubMed:7533195"
FT CHAIN 26..98
FT /note="CD59 glycoprotein"
FT /id="PRO_0000036118"
FT PROPEP 99..123
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036119"
FT DOMAIN 26..103
FT /note="UPAR/Ly6"
FT LIPID 98
FT /note="GPI-anchor amidated serine"
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..65
FT /evidence="ECO:0000250"
FT DISULFID 71..89
FT /evidence="ECO:0000250"
FT DISULFID 90..95
FT /evidence="ECO:0000250"
FT CONFLICT 26
FT /note="L -> M (in Ref. 2; AAD39837)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="H -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 123 AA; 13790 MW; FD62ED3F93C91321 CRC64;
MGSKGGFILL WLLSILAVLC HLGHSLQCYN CINPAGSCTT AMNCSHNQDA CIFVEAVPPK
TYYQCWRFDE CNFDFISRNL AEKKLKYNCC RKDLCNKSDA TISSGKTALL VILLLVATWH
FCL
