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Protein

CD59A glycoprotein

Gene

Cd59a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Biological processi

  • negative regulation of activation of membrane attack complex Source: BHF-UCL
  • negative regulation of angiogenesis Source: BHF-UCL
  • negative regulation of complement activation Source: BHF-UCL
  • negative regulation of fibroblast growth factor production Source: BHF-UCL
  • negative regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-MMU-5694530. Cargo concentration in the ER.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-977606. Regulation of Complement cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
CD59A glycoprotein
Alternative name(s):
MAC-inhibitory protein
Short name:
MAC-IP
Membrane attack complex inhibition factor
Short name:
MACIF
Protectin
CD_antigen: CD59
Gene namesi
Name:Cd59a
Synonyms:Cd59
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:109177. Cd59a.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • external side of plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 9673CD59A glycoproteinPRO_0000036112Add
BLAST
Propeptidei97 – 12327Removed in mature formBy similarityPRO_0000036113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 50By similarity
Disulfide bondi29 ↔ 37By similarity
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence analysis
Disulfide bondi43 ↔ 63By similarity
Disulfide bondi69 ↔ 87By similarity
Disulfide bondi88 ↔ 93By similarity
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence analysis
Lipidationi96 – 961GPI-anchor amidated serineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiO55186.
PaxDbiO55186.
PRIDEiO55186.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiO55186.
CleanExiMM_CD59A.
ExpressionAtlasiO55186. baseline and differential.
GenevisibleiO55186. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000048041.

Structurei

3D structure databases

ProteinModelPortaliO55186.
SMRiO55186. Positions 24-94.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 9673UPAR/Ly6Add
BLAST

Sequence similaritiesi

Contains 1 UPAR/Ly6 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J39P. Eukaryota.
ENOG410ZEQP. LUCA.
GeneTreeiENSGT00390000016309.
HOGENOMiHOG000232180.
HOVERGENiHBG005284.
InParanoidiO55186.
KOiK04008.
OrthoDBiEOG7PVWRQ.
PhylomeDBiO55186.
TreeFamiTF338524.

Family and domain databases

InterProiIPR027101. CD59_glyco.
IPR016054. LY6_UPA_recep-like.
[Graphical view]
PANTHERiPTHR10036:SF9. PTHR10036:SF9. 1 hit.
SMARTiSM00134. LU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O55186-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAQRGLILL LLLLAVFCST AVSLTCYHCF QPVVSSCNMN STCSPDQDSC
60 70 80 90 100
LYAVAGMQVY QRCWKQSDCH GEIIMDQLEE TKLKFRCCQF NLCNKSDGSL
110 120
GKTPLLGTSV LVAILNLCFL SHL
Length:123
Mass (Da):13,648
Last modified:June 1, 1998 - v1
Checksum:iAA6BF2C96F2A7374
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60473 mRNA. Translation: AAC00055.1.
AF247652 Genomic DNA. Translation: AAG15314.1.
AK002743 mRNA. Translation: BAB22321.1.
AK005507 mRNA. Translation: BAB24087.1.
AK018136 mRNA. Translation: BAB31088.1.
AK080728 mRNA. Translation: BAC37996.1.
CCDSiCCDS16487.1.
RefSeqiNP_001104530.1. NM_001111060.2.
NP_031678.1. NM_007652.5.
XP_006498713.1. XM_006498650.2.
XP_006498714.1. XM_006498651.2.
UniGeneiMm.247265.

Genome annotation databases

EnsembliENSMUST00000040423; ENSMUSP00000048041; ENSMUSG00000032679.
ENSMUST00000168176; ENSMUSP00000132774; ENSMUSG00000032679.
GeneIDi12509.
KEGGimmu:12509.
UCSCiuc008ljo.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60473 mRNA. Translation: AAC00055.1.
AF247652 Genomic DNA. Translation: AAG15314.1.
AK002743 mRNA. Translation: BAB22321.1.
AK005507 mRNA. Translation: BAB24087.1.
AK018136 mRNA. Translation: BAB31088.1.
AK080728 mRNA. Translation: BAC37996.1.
CCDSiCCDS16487.1.
RefSeqiNP_001104530.1. NM_001111060.2.
NP_031678.1. NM_007652.5.
XP_006498713.1. XM_006498650.2.
XP_006498714.1. XM_006498651.2.
UniGeneiMm.247265.

3D structure databases

ProteinModelPortaliO55186.
SMRiO55186. Positions 24-94.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000048041.

Proteomic databases

MaxQBiO55186.
PaxDbiO55186.
PRIDEiO55186.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040423; ENSMUSP00000048041; ENSMUSG00000032679.
ENSMUST00000168176; ENSMUSP00000132774; ENSMUSG00000032679.
GeneIDi12509.
KEGGimmu:12509.
UCSCiuc008ljo.3. mouse.

Organism-specific databases

CTDi12509.
MGIiMGI:109177. Cd59a.

Phylogenomic databases

eggNOGiENOG410J39P. Eukaryota.
ENOG410ZEQP. LUCA.
GeneTreeiENSGT00390000016309.
HOGENOMiHOG000232180.
HOVERGENiHBG005284.
InParanoidiO55186.
KOiK04008.
OrthoDBiEOG7PVWRQ.
PhylomeDBiO55186.
TreeFamiTF338524.

Enzyme and pathway databases

ReactomeiR-MMU-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-MMU-5694530. Cargo concentration in the ER.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-977606. Regulation of Complement cascade.

Miscellaneous databases

ChiTaRSiCd59a. mouse.
NextBioi281486.
PROiO55186.
SOURCEiSearch...

Gene expression databases

BgeeiO55186.
CleanExiMM_CD59A.
ExpressionAtlasiO55186. baseline and differential.
GenevisibleiO55186. MM.

Family and domain databases

InterProiIPR027101. CD59_glyco.
IPR016054. LY6_UPA_recep-like.
[Graphical view]
PANTHERiPTHR10036:SF9. PTHR10036:SF9. 1 hit.
SMARTiSM00134. LU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, chromosomal localization, expression, and functional characterization of the mouse analogue of human CD59."
    Powell M.B., Marchbank K.J., Rushmere N.K., van den Berg C.W., Morgan B.P.
    J. Immunol. 158:1692-1702(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "Genomic structure and chromosome location of the gene encoding mouse CD59."
    Holt D.S., Powell M.B., Rushmere N.K., Morgan B.P.
    Cytogenet. Cell Genet. 89:264-267(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney, Medulla oblongata, Placenta and Retina.

Entry informationi

Entry nameiCD59A_MOUSE
AccessioniPrimary (citable) accession number: O55186
Secondary accession number(s): Q542R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.