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CD59 glycoprotein (MAC-inhibitory protein) (MAC-IP) (Membrane attack complex inhibition factor) (MACIF) (Protectin) (CD antigen CD59)

 CD59_RAT                Reviewed;         126 AA.
P27274;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 125.
RecName: Full=CD59 glycoprotein;
AltName: Full=MAC-inhibitory protein;
Short=MAC-IP;
AltName: Full=Membrane attack complex inhibition factor;
Short=MACIF;
AltName: Full=Protectin;
AltName: CD_antigen=CD59;
Flags: Precursor;
Name=Cd59;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 23-64.
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=7528012; DOI=10.1042/bj3040595;
Rushmere N.K., Harrison R.A., van den Berg C.W., Morgan B.P.;
"Molecular cloning of the rat analogue of human CD59: structural
comparison with human CD59 and identification of a putative active
site.";
Biochem. J. 304:595-601(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 23-37.
TISSUE=Erythrocyte;
PubMed=1376109; DOI=10.1042/bj2840169;
Hughes T.R., Piddlesden S.J., Willams J.D., Harrison R.A.,
Morgan B.P.;
"Isolation and characterization of a membrane protein from rat
erythrocytes which inhibits lysis by the membrane attack complex of
rat complement.";
Biochem. J. 284:169-176(1992).
-!- FUNCTION: Potent inhibitor of the complement membrane attack
complex (MAC) action. Acts at or after the C5b-8 stage of MAC
assembly.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
-!- PTM: N-glycosylated.
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U48255; AAA88909.1; -; mRNA.
EMBL; BC063176; AAH63176.1; -; mRNA.
PIR; S53340; S53340.
RefSeq; NP_037057.1; NM_012925.1.
UniGene; Rn.1231; -.
ProteinModelPortal; P27274; -.
SMR; P27274; -.
IntAct; P27274; 1.
STRING; 10116.ENSRNOP00000060967; -.
iPTMnet; P27274; -.
PhosphoSitePlus; P27274; -.
SwissPalm; P27274; -.
PaxDb; P27274; -.
PRIDE; P27274; -.
Ensembl; ENSRNOT00000067085; ENSRNOP00000060967; ENSRNOG00000042821.
GeneID; 25407; -.
KEGG; rno:25407; -.
UCSC; RGD:2311; rat.
CTD; 966; -.
RGD; 2311; Cd59.
eggNOG; ENOG410J39P; Eukaryota.
eggNOG; ENOG410ZEQP; LUCA.
GeneTree; ENSGT00390000016309; -.
HOVERGEN; HBG005284; -.
InParanoid; P27274; -.
KO; K04008; -.
OMA; NSDLCNS; -.
OrthoDB; EOG091G11NF; -.
PhylomeDB; P27274; -.
Reactome; R-RNO-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-RNO-5694530; Cargo concentration in the ER.
Reactome; R-RNO-6798695; Neutrophil degranulation.
Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
Reactome; R-RNO-977606; Regulation of Complement cascade.
PRO; PR:P27274; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000042821; -.
Genevisible; P27274; RN.
GO; GO:0031362; C:anchored component of external side of plasma membrane; ISO:RGD.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0043218; C:compact myelin; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0031982; C:vesicle; ISO:RGD.
GO; GO:0001848; F:complement binding; IDA:RGD.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0001971; P:negative regulation of activation of membrane attack complex; IDA:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0045916; P:negative regulation of complement activation; ISO:RGD.
GO; GO:0045918; P:negative regulation of cytolysis; ISO:RGD.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:RGD.
GO; GO:0030449; P:regulation of complement activation; NAS:RGD.
InterPro; IPR018363; CD59_antigen_CS.
InterPro; IPR027101; CD59_glyco.
InterPro; IPR016054; LY6_UPA_recep-like.
PANTHER; PTHR10036:SF9; PTHR10036:SF9; 1.
Pfam; PF00021; UPAR_LY6; 1.
SMART; SM00134; LU; 1.
PROSITE; PS00983; LY6_UPAR; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
Reference proteome; Signal.
SIGNAL 1 22 {ECO:0000269|PubMed:1376109,
ECO:0000269|PubMed:7528012}.
CHAIN 23 101 CD59 glycoprotein.
/FTId=PRO_0000036124.
PROPEP 102 126 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000036125.
DOMAIN 23 110 UPAR/Ly6.
LIPID 101 101 GPI-anchor amidated asparagine.
{ECO:0000250}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 48 {ECO:0000250}.
DISULFID 28 35 {ECO:0000250}.
DISULFID 41 61 {ECO:0000250}.
DISULFID 67 85 {ECO:0000250}.
DISULFID 86 91 {ECO:0000250}.
SEQUENCE 126 AA; 13790 MW; 54B9C58AB2073005 CRC64;
MRARRGFILL LLLAVLCSTG VSLRCYNCLD PVSSCKTNST CSPNLDACLV AVSGKQVYQQ
CWRFSDCNAK FILSRLEIAN VQYRCCQADL CNKSFEDKPN NGAISLLGKT ALLVTSVLAA
ILKPCF


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