CD59_RAT
ID CD59_RAT Reviewed; 126 AA.
AC P27274;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 142.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 23-64.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=7528012; DOI=10.1042/bj3040595;
RA Rushmere N.K., Harrison R.A., van den Berg C.W., Morgan B.P.;
RT "Molecular cloning of the rat analogue of human CD59: structural comparison
RT with human CD59 and identification of a putative active site.";
RL Biochem. J. 304:595-601(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 23-37.
RC TISSUE=Erythrocyte;
RX PubMed=1376109; DOI=10.1042/bj2840169;
RA Hughes T.R., Piddlesden S.J., Willams J.D., Harrison R.A., Morgan B.P.;
RT "Isolation and characterization of a membrane protein from rat erythrocytes
RT which inhibits lysis by the membrane attack complex of rat complement.";
RL Biochem. J. 284:169-176(1992).
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 -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- PTM: N-glycosylated.
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DR EMBL; U48255; AAA88909.1; -; mRNA.
DR EMBL; BC063176; AAH63176.1; -; mRNA.
DR PIR; S53340; S53340.
DR RefSeq; NP_037057.1; NM_012925.1.
DR AlphaFoldDB; P27274; -.
DR SMR; P27274; -.
DR BioGRID; 247442; 1.
DR IntAct; P27274; 1.
DR STRING; 10116.ENSRNOP00000060967; -.
DR GlyGen; P27274; 1 site.
DR iPTMnet; P27274; -.
DR PhosphoSitePlus; P27274; -.
DR SwissPalm; P27274; -.
DR PaxDb; P27274; -.
DR PRIDE; P27274; -.
DR Ensembl; ENSRNOT00000067085; ENSRNOP00000060967; ENSRNOG00000042821.
DR GeneID; 25407; -.
DR KEGG; rno:25407; -.
DR UCSC; RGD:2311; rat.
DR CTD; 966; -.
DR RGD; 2311; Cd59.
DR eggNOG; ENOG502SA4P; Eukaryota.
DR GeneTree; ENSGT00390000016309; -.
DR HOGENOM; CLU_147732_1_0_1; -.
DR InParanoid; P27274; -.
DR OMA; CSKQRDC; -.
DR OrthoDB; 1586315at2759; -.
DR PhylomeDB; P27274; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR PRO; PR:P27274; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000042821; Expressed in lung and 20 other tissues.
DR Genevisible; P27274; RN.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0043218; C:compact myelin; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0001848; F:complement binding; IDA:RGD.
DR GO; GO:0001971; P:negative regulation of activation of membrane attack complex; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0045916; P:negative regulation of complement activation; ISO:RGD.
DR GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; IMP:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:RGD.
DR GO; GO:0030449; P:regulation of complement activation; ISO:RGD.
DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; ISO:RGD.
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 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..22
FT /evidence="ECO:0000269|PubMed:1376109,
FT ECO:0000269|PubMed:7528012"
FT CHAIN 23..101
FT /note="CD59 glycoprotein"
FT /id="PRO_0000036124"
FT PROPEP 102..126
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036125"
FT DOMAIN 23..110
FT /note="UPAR/Ly6"
FT LIPID 101
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..48
FT /evidence="ECO:0000250"
FT DISULFID 28..35
FT /evidence="ECO:0000250"
FT DISULFID 41..61
FT /evidence="ECO:0000250"
FT DISULFID 67..85
FT /evidence="ECO:0000250"
FT DISULFID 86..91
FT /evidence="ECO:0000250"
SQ SEQUENCE 126 AA; 13790 MW; 54B9C58AB2073005 CRC64;
MRARRGFILL LLLAVLCSTG VSLRCYNCLD PVSSCKTNST CSPNLDACLV AVSGKQVYQQ
CWRFSDCNAK FILSRLEIAN VQYRCCQADL CNKSFEDKPN NGAISLLGKT ALLVTSVLAA
ILKPCF
