CD59B_MOUSE
ID CD59B_MOUSE Reviewed; 129 AA.
AC P58019; Q920G7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=CD59B 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=Cd59b;
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, AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=10946279; DOI=10.4049/jimmunol.165.5.2528;
RA Qian Y.-M., Qin X., Miwa T., Sun X., Halperin J.A., Song W.-C.;
RT "Identification and functional characterization of a new gene encoding the
RT mouse terminal complement inhibitor CD59.";
RL J. Immunol. 165:2528-2534(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=11471050; DOI=10.1007/s00335-001-2060-8;
RA Qin X., Miwa T., Aktas H., Gao M., Lee C., Qian Y.M., Morton C.C.,
RA Shahsafaei A., Song W.C., Halperin J.A.;
RT "Genomic structure, functional comparison, and tissue distribution of mouse
RT Cd59a and Cd59b.";
RL Mamm. Genome 12:582-589(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
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: Widely expressed in the kidneys, brain, lungs,
CC spleen and testis (PubMed:11471050) Testis specific (PubMed:10946279).
CC {ECO:0000269|PubMed:10946279, ECO:0000269|PubMed:11471050}.
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DR EMBL; AF292401; AAL04434.1; -; Genomic_DNA.
DR EMBL; BX640578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX813317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139203; AAI39204.1; -; mRNA.
DR EMBL; BC145912; AAI45913.1; -; mRNA.
DR EMBL; BC171969; AAI71969.1; -; mRNA.
DR CCDS; CCDS16486.1; -.
DR RefSeq; NP_862906.1; NM_181858.1.
DR RefSeq; XP_006499865.1; XM_006499802.3.
DR RefSeq; XP_006499866.1; XM_006499803.3.
DR RefSeq; XP_006499867.1; XM_006499804.2.
DR RefSeq; XP_006499868.1; XM_006499805.2.
DR AlphaFoldDB; P58019; -.
DR SMR; P58019; -.
DR STRING; 10090.ENSMUSP00000087912; -.
DR GlyGen; P58019; 1 site.
DR PhosphoSitePlus; P58019; -.
DR PaxDb; P58019; -.
DR PRIDE; P58019; -.
DR ProteomicsDB; 280025; -.
DR DNASU; 333883; -.
DR Ensembl; ENSMUST00000090429; ENSMUSP00000087912; ENSMUSG00000068686.
DR Ensembl; ENSMUST00000111130; ENSMUSP00000106760; ENSMUSG00000068686.
DR Ensembl; ENSMUST00000129749; ENSMUSP00000117553; ENSMUSG00000068686.
DR GeneID; 333883; -.
DR KEGG; mmu:333883; -.
DR UCSC; uc008ljn.1; mouse.
DR CTD; 333883; -.
DR MGI; MGI:1888996; Cd59b.
DR VEuPathDB; HostDB:ENSMUSG00000068686; -.
DR eggNOG; ENOG502SA4P; Eukaryota.
DR GeneTree; ENSGT00390000016309; -.
DR HOGENOM; CLU_147732_1_0_1; -.
DR InParanoid; P58019; -.
DR OMA; TMIWILC; -.
DR OrthoDB; 1586315at2759; -.
DR PhylomeDB; P58019; -.
DR TreeFam; TF338524; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 333883; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Cd59b; mouse.
DR PRO; PR:P58019; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P58019; protein.
DR Bgee; ENSMUSG00000068686; Expressed in brown adipose tissue and 95 other tissues.
DR ExpressionAtlas; P58019; baseline and differential.
DR Genevisible; P58019; MM.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0043218; C:compact myelin; ISO: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:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045916; P:negative regulation of complement activation; IDA:MGI.
DR GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; ISO:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; 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..104
FT /note="CD59B glycoprotein"
FT /id="PRO_0000036114"
FT PROPEP 105..129
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000036115"
FT DOMAIN 24..107
FT /note="UPAR/Ly6"
FT LIPID 104
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..49
FT /evidence="ECO:0000250"
FT DISULFID 29..36
FT /evidence="ECO:0000250"
FT DISULFID 42..62
FT /evidence="ECO:0000250"
FT DISULFID 68..86
FT /evidence="ECO:0000250"
FT DISULFID 87..92
FT /evidence="ECO:0000250"
FT CONFLICT 30..32
FT /note="LDP -> FQF (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="D -> G (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 129 AA; 14227 MW; 3B80648C8C30F635 CRC64;
MRAQRGLILL LLLLAVFCST AVSLKCYNCL DPVSSCKINT TCSPNLDSCL YAVAGRQVYQ
QCWKLSDCNS NYIMSRLDVA GIQSKCCQWD LCNKNLDGLE EPNNAETSSL RKTALLGTSV
LVAILKFCF
