CD59A_MOUSE
ID CD59A_MOUSE Reviewed; 123 AA.
AC O55186; Q542R7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=CD59A 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=Cd59a; Synonyms=Cd59;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=9029105;
RA Powell M.B., Marchbank K.J., Rushmere N.K., van den Berg C.W., Morgan B.P.;
RT "Molecular cloning, chromosomal localization, expression, and functional
RT characterization of the mouse analogue of human CD59.";
RL J. Immunol. 158:1692-1702(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10965140; DOI=10.1159/000015630;
RA Holt D.S., Powell M.B., Rushmere N.K., Morgan B.P.;
RT "Genomic structure and chromosome location of the gene encoding mouse
RT CD59.";
RL Cytogenet. Cell Genet. 89:264-267(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, Medulla oblongata, Placenta, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined (liver, kidney,
CC spleen, thymus, brain and heart). Low levels in thymus. Also expressed
CC in mononuclear cells, erythrocytes and platelets. Barely detected in
CC neutrophils.
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DR EMBL; U60473; AAC00055.1; -; mRNA.
DR EMBL; AF247652; AAG15314.1; -; Genomic_DNA.
DR EMBL; AK002743; BAB22321.1; -; mRNA.
DR EMBL; AK005507; BAB24087.1; -; mRNA.
DR EMBL; AK018136; BAB31088.1; -; mRNA.
DR EMBL; AK080728; BAC37996.1; -; mRNA.
DR CCDS; CCDS16487.1; -.
DR RefSeq; NP_001104530.1; NM_001111060.2.
DR RefSeq; NP_031678.1; NM_007652.5.
DR RefSeq; XP_006498713.1; XM_006498650.3.
DR RefSeq; XP_006498714.1; XM_006498651.3.
DR AlphaFoldDB; O55186; -.
DR SMR; O55186; -.
DR STRING; 10090.ENSMUSP00000048041; -.
DR GlyGen; O55186; 2 sites.
DR jPOST; O55186; -.
DR MaxQB; O55186; -.
DR PaxDb; O55186; -.
DR PRIDE; O55186; -.
DR ProteomicsDB; 265626; -.
DR DNASU; 12509; -.
DR Ensembl; ENSMUST00000040423; ENSMUSP00000048041; ENSMUSG00000032679.
DR Ensembl; ENSMUST00000168176; ENSMUSP00000132774; ENSMUSG00000032679.
DR GeneID; 12509; -.
DR KEGG; mmu:12509; -.
DR UCSC; uc008ljo.3; mouse.
DR CTD; 12509; -.
DR MGI; MGI:109177; Cd59a.
DR VEuPathDB; HostDB:ENSMUSG00000032679; -.
DR GeneTree; ENSGT00390000016309; -.
DR HOGENOM; CLU_147732_1_0_1; -.
DR InParanoid; O55186; -.
DR OMA; YSDCNFL; -.
DR OrthoDB; 1586315at2759; -.
DR PhylomeDB; O55186; -.
DR TreeFam; TF338524; -.
DR BioGRID-ORCS; 12509; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Cd59a; mouse.
DR PRO; PR:O55186; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O55186; protein.
DR Bgee; ENSMUSG00000032679; Expressed in heart right ventricle and 233 other tissues.
DR ExpressionAtlas; O55186; baseline and differential.
DR Genevisible; O55186; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0043218; C:compact myelin; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0001848; F:complement binding; ISO:MGI.
DR GO; GO:0001971; P:negative regulation of activation of membrane attack complex; IDA:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045916; P:negative regulation of complement activation; IDA:BHF-UCL.
DR GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; ISO:MGI.
DR GO; GO:0090272; P:negative regulation of fibroblast growth factor production; IDA:BHF-UCL.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0030449; P:regulation of complement activation; ISO:MGI.
DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; ISO:MGI.
DR CDD; cd00117; LU; 1.
DR Gene3D; 2.10.60.10; -; 1.
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.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..96
FT /note="CD59A glycoprotein"
FT /id="PRO_0000036112"
FT PROPEP 97..123
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036113"
FT DOMAIN 24..96
FT /note="UPAR/Ly6"
FT LIPID 96
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..50
FT /evidence="ECO:0000250"
FT DISULFID 29..37
FT /evidence="ECO:0000250"
FT DISULFID 43..63
FT /evidence="ECO:0000250"
FT DISULFID 69..87
FT /evidence="ECO:0000250"
FT DISULFID 88..93
FT /evidence="ECO:0000250"
SQ SEQUENCE 123 AA; 13648 MW; AA6BF2C96F2A7374 CRC64;
MRAQRGLILL LLLLAVFCST AVSLTCYHCF QPVVSSCNMN STCSPDQDSC LYAVAGMQVY
QRCWKQSDCH GEIIMDQLEE TKLKFRCCQF NLCNKSDGSL GKTPLLGTSV LVAILNLCFL
SHL
