CPLM-000612

Genbank Nucleotide ID

Complement component 1 Q subcomponent-binding protein, mitochondrial

Protein Synonyms/Alias

GC1q-R protein; Glycoprotein gC1qBP; C1qBP

Mus musculus (Mouse)

Position	Peptide	Type	References
77	ALHTEGDKAFVEFLT	acetylation	[1]
88	EFLTDEIKEEKKIQK	acetylation	[1, 2, 3, 4, 5, 6]
91	TDEIKEEKKIQKHKS	acetylation	[1, 6, 7]
272	ITFLEDLKSFVKNQ*	acetylation	[1]
276	EDLKSFVKNQ*****	acetylation	[6]

[1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
[2] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
[3] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
[4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
[5] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
[7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]

Functional Description

Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular "heads" of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinty receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. In infection processes acts as an attachment site for microbial proteins. May play a role in antibacterial defense. Involved in regulation of antiviral response by inhibiting DDX58- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection.

REGION 73 90 C1q binding (By similarity).
REGION 165 209 Interation with MAVS (By similarity).
MOD_RES 88 88 N6-acetyllysine (By similarity).
MOD_RES 184 184 Phosphotyrosine (By similarity).
MOD_RES 197 197 Phosphoserine (By similarity).

Acetylation; Adaptive immunity; Apoptosis; Cell membrane; Complement pathway; Complete proteome; Cytoplasm; Direct protein sequencing; Immunity; Innate immunity; Membrane; Mitochondrion; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis; Secreted; Transcription; Transcription regulation; Transit peptide.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; ISS:UniProtKB.
GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO:0031690; F:adrenergic receptor binding; ISS:UniProtKB.
GO:0001849; F:complement component C1q binding; ISS:UniProtKB.
GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
GO:0030984; F:kininogen binding; ISS:UniProtKB.
GO:0097177; F:mitochondrial ribosome binding; IDA:UniProtKB.
GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO:0042256; P:mature ribosome assembly; IMP:UniProtKB.
GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO:0050687; P:negative regulation of defense response to virus; ISS:UniProtKB.
GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB.
GO:0032695; P:negative regulation of interleukin-12 production; ISS:UniProtKB.
GO:0039534; P:negative regulation of MDA-5 signaling pathway; ISS:UniProtKB.
GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
GO:0039536; P:negative regulation of RIG-I signaling pathway; ISS:UniProtKB.
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO:0014065; P:phosphatidylinositol 3-kinase cascade; ISS:UniProtKB.
GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO:2000510; P:positive regulation of dendritic cell chemotaxis; ISS:UniProtKB.
GO:0070131; P:positive regulation of mitochondrial translation; IMP:UniProtKB.
GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:UniProtKB.
GO:0051897; P:positive regulation of protein kinase B signaling cascade; ISS:UniProtKB.
GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO:1901165; P:positive regulation of trophoblast cell migration; ISS:UniProtKB.
GO:0030449; P:regulation of complement activation; ISS:UniProtKB.
GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.