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CD59A glycoprotein (MAC-inhibitory protein) (MAC-IP) (Membrane attack complex inhibition factor) (MACIF) (Protectin) (CD antigen CD59)

 CD59A_MOUSE             Reviewed;         123 AA.
O55186; Q542R7;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
07-NOV-2018, entry version 134.
RecName: Full=CD59A 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=Cd59a; Synonyms=Cd59;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=9029105;
Powell M.B., Marchbank K.J., Rushmere N.K., van den Berg C.W.,
Morgan B.P.;
"Molecular cloning, chromosomal localization, expression, and
functional characterization of the mouse analogue of human CD59.";
J. Immunol. 158:1692-1702(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=10965140;
Holt D.S., Powell M.B., Rushmere N.K., Morgan B.P.;
"Genomic structure and chromosome location of the gene encoding mouse
CD59.";
Cytogenet. Cell Genet. 89:264-267(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Kidney, Medulla oblongata, Placenta, and Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
-!- FUNCTION: Potent inhibitor of the complement membrane attack
complex (MAC) action. Acts by binding to the C8 and/or C9
complements of the assembling MAC, thereby preventing
incorporation of the multiple copies of C9 required for complete
formation of the osmolytic pore (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
-!- TISSUE SPECIFICITY: Expressed in all tissues examined (liver,
kidney, spleen, thymus, brain and heart). Low levels in thymus.
Also expressed in mononuclear cells, erythrocytes and platelets.
Barely detected in neutrophils.
-----------------------------------------------------------------------
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EMBL; U60473; AAC00055.1; -; mRNA.
EMBL; AF247652; AAG15314.1; -; Genomic_DNA.
EMBL; AK002743; BAB22321.1; -; mRNA.
EMBL; AK005507; BAB24087.1; -; mRNA.
EMBL; AK018136; BAB31088.1; -; mRNA.
EMBL; AK080728; BAC37996.1; -; mRNA.
CCDS; CCDS16487.1; -.
RefSeq; NP_001104530.1; NM_001111060.2.
RefSeq; NP_031678.1; NM_007652.5.
RefSeq; XP_006498713.1; XM_006498650.3.
RefSeq; XP_006498714.1; XM_006498651.3.
UniGene; Mm.247265; -.
ProteinModelPortal; O55186; -.
SMR; O55186; -.
STRING; 10090.ENSMUSP00000048041; -.
MaxQB; O55186; -.
PaxDb; O55186; -.
PRIDE; O55186; -.
Ensembl; ENSMUST00000040423; ENSMUSP00000048041; ENSMUSG00000032679.
Ensembl; ENSMUST00000168176; ENSMUSP00000132774; ENSMUSG00000032679.
GeneID; 12509; -.
KEGG; mmu:12509; -.
UCSC; uc008ljo.3; mouse.
CTD; 12509; -.
MGI; MGI:109177; Cd59a.
eggNOG; ENOG410J39P; Eukaryota.
eggNOG; ENOG410ZEQP; LUCA.
GeneTree; ENSGT00390000016309; -.
HOGENOM; HOG000232180; -.
HOVERGEN; HBG005284; -.
InParanoid; O55186; -.
KO; K04008; -.
OMA; RCCNSNL; -.
OrthoDB; EOG091G11NF; -.
PhylomeDB; O55186; -.
TreeFam; TF338524; -.
Reactome; R-MMU-204005; COPII-mediated vesicle transport.
Reactome; R-MMU-5694530; Cargo concentration in the ER.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
Reactome; R-MMU-977606; Regulation of Complement cascade.
ChiTaRS; Cd59a; mouse.
PRO; PR:O55186; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000032679; Expressed in 239 organ(s), highest expression level in blood.
CleanEx; MM_CD59A; -.
ExpressionAtlas; O55186; baseline and differential.
Genevisible; O55186; MM.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0001848; F:complement binding; IBA:GO_Central.
GO; GO:0001971; P:negative regulation of activation of membrane attack complex; IDA:MGI.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:BHF-UCL.
GO; GO:0045916; P:negative regulation of complement activation; IDA:BHF-UCL.
GO; GO:0090272; P:negative regulation of fibroblast growth factor production; IDA:BHF-UCL.
GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
InterPro; IPR027101; CD59_glyco.
InterPro; IPR016054; LY6_UPA_recep-like.
PANTHER; PTHR10036:SF9; PTHR10036:SF9; 1.
SMART; SM00134; LU; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 96 CD59A glycoprotein.
/FTId=PRO_0000036112.
PROPEP 97 123 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000036113.
DOMAIN 24 96 UPAR/Ly6.
LIPID 96 96 GPI-anchor amidated serine.
{ECO:0000250}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 26 50 {ECO:0000250}.
DISULFID 29 37 {ECO:0000250}.
DISULFID 43 63 {ECO:0000250}.
DISULFID 69 87 {ECO:0000250}.
DISULFID 88 93 {ECO:0000250}.
SEQUENCE 123 AA; 13648 MW; AA6BF2C96F2A7374 CRC64;
MRAQRGLILL LLLLAVFCST AVSLTCYHCF QPVVSSCNMN STCSPDQDSC LYAVAGMQVY
QRCWKQSDCH GEIIMDQLEE TKLKFRCCQF NLCNKSDGSL GKTPLLGTSV LVAILNLCFL
SHL


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