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Complement component 1 Q subcomponent-binding protein, mitochondrial (Globular head receptor of C1 complement protein) (Mitochondrial matrix protein p32)

 C1QBP_CHLAE             Reviewed;         282 AA.
Q9MZE0; Q95J15;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 2.
25-OCT-2017, entry version 58.
RecName: Full=Complement component 1 Q subcomponent-binding protein, mitochondrial;
AltName: Full=Globular head receptor of C1 complement protein;
AltName: Full=Mitochondrial matrix protein p32;
Flags: Precursor;
Name=C1QBP;
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus.
NCBI_TaxID=9534;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RUBELLA VIRUS CAPSID.
PubMed=10823864; DOI=10.1128/JVI.74.12.5569-5576.2000;
Beatch M.D., Hobman T.C.;
"Rubella virus capsid associates with host cell protein p32 and
localizes to mitochondria.";
J. Virol. 74:5569-5576(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Krishna Mohan K.V., Atreya C.D.;
"Complete coding sequence analysis of simian homolog of gC1Q-R.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, AND INTERACTION WITH LISTERIA MONOCYTOGENES INLB.
PubMed=10747014; DOI=10.1093/emboj/19.7.1458;
Braun L., Ghebrehiwet B., Cossart P.;
"gC1q-R/p32, a C1q-binding protein, is a receptor for the InlB
invasion protein of Listeria monocytogenes.";
EMBO J. 19:1458-1466(2000).
-!- 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. 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. 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. {ECO:0000269|PubMed:10747014}.
-!- 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 and SRSF9. 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
(By similarity). Interacts with Listeria monocytogenes inlb.
Interacts with Rubella virus capsid protein; the interaction
occurs in mitochondria. {ECO:0000250, ECO:0000269|PubMed:10747014,
ECO:0000269|PubMed:10823864}.
-!- INTERACTION:
P25147:inlB (xeno); NbExp=3; IntAct=EBI-6375765, EBI-1379295;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:10823864}. Nucleus {ECO:0000250}. Cell
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Extracellular side {ECO:0000250}. Secreted {ECO:0000250}.
Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}.
Note=Seems to be predominantly localized to mitochondria.
-!- SIMILARITY: Belongs to the MAM33 family. {ECO:0000305}.
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EMBL; AF238300; AAF74122.1; -; mRNA.
EMBL; AF283278; AAK83694.1; -; mRNA.
EMBL; AF283279; AAK83695.1; -; mRNA.
ProteinModelPortal; Q9MZE0; -.
SMR; Q9MZE0; -.
IntAct; Q9MZE0; 4.
PRIDE; Q9MZE0; -.
HOVERGEN; HBG000914; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0031690; F:adrenergic receptor binding; ISS:UniProtKB.
GO; GO:0001849; F:complement component C1q binding; ISS:UniProtKB.
GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
GO; GO:0030984; F:kininogen binding; ISS:UniProtKB.
GO; GO:0097177; F:mitochondrial ribosome binding; ISS:UniProtKB.
GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0042256; P:mature ribosome assembly; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0050687; P:negative regulation of defense response to virus; ISS:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB.
GO; GO:0032695; P:negative regulation of interleukin-12 production; ISS:UniProtKB.
GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; ISS:UniProtKB.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; ISS:UniProtKB.
GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO; GO:1901165; P:positive regulation of trophoblast cell migration; ISS:UniProtKB.
GO; GO:0030449; P:regulation of complement activation; ISS:UniProtKB.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.10.280.10; -; 1.
InterPro; IPR003428; MAM33.
InterPro; IPR036561; MAM33_sf.
PANTHER; PTHR10826; PTHR10826; 1.
Pfam; PF02330; MAM33; 1.
SUPFAM; SSF54529; SSF54529; 1.
1: Evidence at protein level;
Acetylation; Adaptive immunity; Apoptosis; Cell membrane;
Complement pathway; Cytoplasm; Host-virus interaction; Immunity;
Innate immunity; Membrane; Mitochondrion; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Ribosome biogenesis; Secreted;
Transcription; Transcription regulation; Transit peptide.
TRANSIT 1 70 Mitochondrion. {ECO:0000250}.
CHAIN 71 282 Complement component 1 Q subcomponent-
binding protein, mitochondrial.
/FTId=PRO_0000238677.
REGION 76 93 C1q binding. {ECO:0000250}.
REGION 168 213 Interaction with MAVS. {ECO:0000250}.
MOD_RES 91 91 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q07021}.
MOD_RES 188 188 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q07021}.
MOD_RES 201 201 Phosphoserine.
{ECO:0000250|UniProtKB:Q07021}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000250|UniProtKB:Q07021}.
CONFLICT 21 21 A -> P (in Ref. 1; AAF74122).
{ECO:0000305}.
CONFLICT 176 176 Missing (in Ref. 2; AAK83694/AAK83695).
{ECO:0000305}.
SEQUENCE 282 AA; 31416 MW; 67526590A80F5177 CRC64;
MLPLLRCVPR VLGSAVPSLR AAAPASPFRQ LLTPGPRLCA RPFGLLSVRA GSERRPGLLR
PRGPCACGCG CGLLHTEGDK AFVDFLNDEI KEERKIQKHK TLPKMSGGWE LELNGTEAKL
MRKVAGEKIT VTFNINNSIP PTFDGEEEPT QGQKVEEQEP ELTSTPNFVV EVIKNDDGKK
ALVLDCHYPE DEVGQEDEAE SDIFSIREVS FQSSGESEWK DTNYTLNTDS LDWALYDHLM
DFLADRGVDN TFADELVELS TALEHQEYIS FLEDLKSFVK SQ


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