| IED ID | IndEnz0002006169 |
| Enzyme Type ID | protease006169 |
| Protein Name |
Complement component 1 Q subcomponent-binding protein, mitochondrial ASF/SF2-associated protein p32 Glycoprotein gC1qBP C1qBP Hyaluronan-binding protein 1 Mitochondrial matrix protein p32 gC1q-R protein p33 SF2AP32 |
| Gene Name | C1QBP GC1QBP HABP1 SF2P32 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MLPLLRCVPRVLGSSVAGLRAAAPASPFRQLLQPAPRLCTRPFGLLSVRAGSERRPGLLRPRGPCACGCGCGSLHTDGDKAFVDFLSDEIKEERKIQKHKTLPKMSGGWELELNGTEAKLVRKVAGEKITVTFNINNSIPPTFDGEEEPSQGQKVEEQEPELTSTPNFVVEVIKNDDGKKALVLDCHYPEDEVGQEDEAESDIFSIREVSFQSTGESEWKDTNYTLNTDSLDWALYDHLMDFLADRGVDNTFADELVELSTALEHQEYITFLEDLKSFVKSQ |
| Enzyme Length | 282 |
| Uniprot Accession Number | Q07021 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, 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. Required for protein synthesis in mitochondria (PubMed:28942965). 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. May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase. May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppression 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. {ECO:0000269|PubMed:10022843, ECO:0000269|PubMed:10479529, ECO:0000269|PubMed:10722602, ECO:0000269|PubMed:11086025, ECO:0000269|PubMed:11859136, 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:28942965, ECO:0000269|PubMed:8662673, ECO:0000269|PubMed:8710908, ECO:0000269|PubMed:9461517}.; FUNCTION: (Microbial infection) Involved in HIV-1 replication, presumably by contributing to splicing of viral RNA. {ECO:0000269|PubMed:12833064}.; FUNCTION: (Microbial infection) In infection processes acts as an attachment site for microbial proteins, including Listeria monocytogenes internalin B (InlB) and Staphylococcus aureus protein A. {ECO:0000269|PubMed:10722602, ECO:0000269|PubMed:10747014, ECO:0000269|PubMed:12411480}.; FUNCTION: (Microbial infection) Involved in replication of Rubella virus. {ECO:0000269|PubMed:12034482}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (7); Chain (1); Helix (4); Modified residue (6); Mutagenesis (1); Natural variant (6); Region (3); Transit peptide (1); Turn (2) |
| Keywords | 3D-structure;Acetylation;Adaptive immunity;Apoptosis;Cell membrane;Complement pathway;Cytoplasm;Direct protein sequencing;Disease variant;Host-virus interaction;Immunity;Innate immunity;Membrane;Mitochondrion;Nucleus;Phosphoprotein;Primary mitochondrial disease;Reference proteome;Ribosome biogenesis;Secreted;Transcription;Transcription regulation;Transit peptide;mRNA processing;mRNA splicing |
| Interact With | P02647; Q14004-2; Q8N726; P00748; Q12948; O00198; Q13351; P01042; Q7Z434; Q05513; Q15139; Q8N3Z0; P04004; P67809; Q64364; O40955; P07566; P08563; P27958; P02745; P02746; P02747 |
| Induction | INDUCTION: Enhanced cell surface expression upon platelet and monocyte activation. {ECO:0000269|PubMed:12574814, ECO:0000269|PubMed:16177118}. |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:15031724, ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:19164550, ECO:0000269|PubMed:9305894}. Nucleus {ECO:0000269|PubMed:18676636}. Nucleus, nucleolus {ECO:0000269|PubMed:21536856, ECO:0000269|PubMed:32958672}. Cell membrane {ECO:0000269|PubMed:10747014, ECO:0000269|PubMed:11493647, ECO:0000269|PubMed:12574814, ECO:0000269|PubMed:8195709, ECO:0000269|PubMed:8662673, ECO:0000269|PubMed:9191880, ECO:0000269|PubMed:9233640}; Peripheral membrane protein {ECO:0000269|PubMed:12574814, ECO:0000269|PubMed:8662673, ECO:0000269|PubMed:9191880}; Extracellular side. Secreted. Cytoplasm {ECO:0000269|PubMed:11493647}. Note=Seems to be predominantly localized to mitochondria. Secreted by activated lymphocytes. Localizes to the nucleolus when coexpressed with POLGARF (PubMed:32958672). Interaction with POLGARF is likely to result in prevention of C1QBP maturation and redirection from mitochondria to nucleoli (PubMed:32958672). {ECO:0000269|PubMed:32958672}. |
| Modified Residue | MOD_RES 87; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 91; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 188; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:19690332"; MOD_RES 201; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 205; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 214; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:24275569" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1P32; 3RPX; 6SZW; |
| Mapped Pubmed ID | 10037681; 10490598; 10619026; 1066663; 10831594; 10873388; 11204562; 11830581; 11870091; 11986212; 12123826; 12220632; 12221077; 12443542; 12538033; 12783858; 12944405; 14559993; 14667819; 14691562; 14743216; 14996700; 15163734; 15231747; 15324660; 15467913; 15866170; 16039650; 16164755; 16212417; 16630611; 16641292; 16713569; 16797541; 16871385; 16893067; 17314511; 17446270; 17620599; 17892212; 17907801; 17932509; 17979178; 18158243; 18218625; 18226242; 18358546; 18460468; 18538737; 18757437; 18829452; 19156129; 19190731; 19423540; 19473882; 19523114; 19565630; 19738201; 19828637; 19913121; 20030946; 20085707; 20100866; 20101212; 20186120; 20360068; 20406964; 20438785; 20562859; 20591975; 20628086; 20660154; 20877624; 21156793; 21205079; 21248045; 21351730; 21536672; 21559373; 21576392; 21627988; 21699497; 21725590; 21911578; 21988832; 22008525; 22101277; 22118625; 22451658; 22771308; 22790947; 22992742; 23455153; 23692256; 23902751; 23924515; 23929393; 23986595; 23990920; 24128008; 24174616; 24255178; 24874554; 24955142; 25061661; 25091479; 25355318; 25355598; 25497084; 25528767; 25573962; 25609649; 25665578; 25794640; 25852190; 25909887; 26085152; 26496610; 26497555; 26638075; 26753982; 27183919; 27328359; 27835682; 28039537; 28107702; 28321; 28428626; 28576489; 28842250; 29035880; 29146911; 29358188; 29670170; 30159917; 31105010; 31155612; 31293051; 31844661; 31871319; 32559765; 34003581; 3484703; 3521732; 3886654; 4054110; 500690; 6604055; 7391081; 8344943; 8543060; 8571126; 8617235; 8662891; 874082; 8756646; 8816443; 9013646; 9111050; 9226169; 9418861; 9427705; 9535835; 9792683; 9829970; |
| Motif | |
| Gene Encoded By | |
| Mass | 31,362 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |