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MT000095

UniProt Annotations

Entry Information
Gene Namecomplement component 1, q subcomponent binding protein
Protein EntryC1QBP_HUMAN
UniProt IDQ07021
SpeciesHuman
Comments
Comment typeDescription
Caution The subcellular location has been matter of debate. After being reported to be exclusively localized to mitochondria, demonstrations of promiscuous associations and locations have been rather considered as artifactual due to the extremely acidic character and the use of different tagged versions of the protein (PubMed:9305894, PubMed:11493647). However, by now the location to multiple compartments linked to diverse functions is accepted. The N-termini of the surface and secreted forms are identical to the reported processed mitochonddrial form. {ECO:0000305|PubMed:11493647, ECO:0000305|PubMed:9305894}.
Function 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 affinity 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, including Listeria monocytogenes internalin B and Staphylococcus aureus protein A. May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase. Involved in replication of Rubella virus. May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppresion of interleukin-12 production in monocyte-derived dendritic cells. Involved in regulation of antiviral response by inhibiting DDX58- and IFIH1- mediated signaling pathways probably involving its association with MAVS after viral infection. Involved in HIV-1 replication, presumably by contributing to splicing of viral RNA. {ECO:0000269|PubMed:10022843, ECO:0000269|PubMed:10479529, ECO:0000269|PubMed:10722602, ECO:0000269|PubMed:10747014, ECO:0000269|PubMed:11086025, ECO:0000269|PubMed:11859136, ECO:0000269|PubMed:12833064, ECO:0000269|PubMed:15243141, ECO:0000269|PubMed:16140380, ECO:0000269|PubMed:16177118, ECO:0000269|PubMed:17881511, ECO:0000269|PubMed:18676636, ECO:0000269|PubMed:19004836, ECO:0000269|PubMed:19164550, ECO:0000269|PubMed:20810993, ECO:0000269|PubMed:21536856, ECO:0000269|PubMed:21544310, ECO:0000269|PubMed:22700724, ECO:0000269|PubMed:8662673, ECO:0000269|PubMed:8710908, ECO:0000269|PubMed:9461517}.
Induction Enhanced cell surface expression upon platelet and monocyte activation. {ECO:0000269|PubMed:12574814, ECO:0000269|PubMed:16177118}.
Interaction P27958:- (xeno); NbExp=4; IntAct=EBI-347528, EBI-6377335; Q14004-2:CDK13; NbExp=6; IntAct=EBI-347528, EBI-6375898; Q8N726:CDKN2A; NbExp=3; IntAct=EBI-347528, EBI-625922; Q64364:Cdkn2a (xeno); NbExp=4; IntAct=EBI-347528, EBI-1202287; P00748:F12; NbExp=2; IntAct=EBI-347528, EBI-6378830; Q12948:FOXC1; NbExp=6; IntAct=EBI-347528, EBI-1175253; O00198:HRK; NbExp=7; IntAct=EBI-347528, EBI-701322; P01042:KNG1; NbExp=4; IntAct=EBI-347528, EBI-6378713; Q7Z434:MAVS; NbExp=5; IntAct=EBI-347528, EBI-995373; Q15139:PRKD1; NbExp=9; IntAct=EBI-347528, EBI-1181072; P04004:VTN; NbExp=8; IntAct=EBI-347528, EBI-1036653;
Similarity Belongs to the MAM33 family. {ECO:0000305}.
Subcellular Location Mitochondrion matrix. Nucleus. Cell membrane; Peripheral membrane protein; Extracellular side. Secreted. Cytoplasm. Nucleus, nucleolus. Note=Seems to be predominantly localized to mitochondria. Secreted by activated lymphocytes.
Subunit Homotrimer; three monomers form a donut-shaped structure with an unusually asymmetric charge distribution on the surface. Interacts with CDK13, HRK, VTN, NFYB, ADRA1B, FOXC1, DDX21, DDX50, NCL, SRSF1, SRSF9 and CDKN2A isoform smARF. Interacts with CD93; the association may represent a cell surface C1q receptor. Interacts with KRT1; the association represents a cell surface kininogen receptor. Interacts with CD209; the interaction is indicative for a C1q:C1QBP:CD209 signaling complex. Interacts with FBL and RRP1; the respective interactions with C1QBP are competetive. Probably associates with the mitoribosome. Interacts with MAVS; the interaction occurs upon viral transfection. Interacts with PPIF. Interacts with Rubella virus capsid protein; the interaction occurs in mitochondria. Interacts with Rubella virus protease p150, Staphylococcus aureus protein A/spa, HIV-1 Tat and HCV core protein. Interacts with U2AF1L4. {ECO:0000250|UniProtKB:O35658, ECO:0000269|PubMed:10022843, ECO:0000269|PubMed:10722602, ECO:0000269|PubMed:10823864, ECO:0000269|PubMed:11086025, ECO:0000269|PubMed:12034482, ECO:0000269|PubMed:15031724, ECO:0000269|PubMed:15243141, ECO:0000269|PubMed:16537587, ECO:0000269|PubMed:16721827, ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18676636, ECO:0000269|PubMed:19164550, ECO:0000269|PubMed:20950273, ECO:0000269|PubMed:21536856, ECO:0000269|PubMed:21544310, ECO:0000269|PubMed:22238231, ECO:0000269|PubMed:22700724, ECO:0000269|PubMed:8900153, ECO:0000269|PubMed:9233640}.
Tissue Specificity Expressed on cell surface of peripheral blood cells (at protein level); Surface expression is reported for macrophages and monocyte-derived dendritic cells. {ECO:0000269|PubMed:12574814, ECO:0000269|PubMed:8662673}.
Web Resource Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/c1qbp/";