C1QBP_RAT
ID C1QBP_RAT Reviewed; 279 AA.
AC O35796; Q6IRS5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Complement component 1 Q subcomponent-binding protein, mitochondrial;
DE AltName: Full=GC1q-R protein;
DE AltName: Full=Glycoprotein gC1qBP;
DE Short=C1qBP;
DE Flags: Precursor;
GN Name=C1qbp; Synonyms=Gc1qbp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9414106; DOI=10.1016/s0014-5793(97)01348-3;
RA Lynch N.J., Reid K.B., van den Berg R.H., Daha M.R., Leigh L.A.,
RA Ghebrehiwet B., Lim W.B., Schwaeble W.J.;
RT "Characterisation of the rat and mouse homologues of gC1qBP, a 33 kDa
RT glycoprotein that binds to the globular 'heads' of C1q.";
RL FEBS Lett. 418:111-114(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 205-217, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP INTERACTION WITH VGF.
RX PubMed=24106277; DOI=10.1074/jbc.m113.510917;
RA Chen Y.C., Pristera A., Ayub M., Swanwick R.S., Karu K., Hamada Y.,
RA Rice A.S., Okuse K.;
RT "Identification of a receptor for neuropeptide VGF and its role in
RT neuropathic pain.";
RL J. Biol. Chem. 288:34638-34646(2013).
CC -!- FUNCTION: Is believed to be a multifunctional and multicompartmental
CC protein involved in inflammation and infection processes, ribosome
CC biogenesis, protein synthesis in mitochondria, regulation of apoptosis,
CC transcriptional regulation and pre-mRNA splicing. At the cell surface
CC is thought to act as an endothelial receptor for plasma proteins of the
CC complement and kallikrein-kinin cascades. Putative receptor for C1q;
CC specifically binds to the globular 'heads' of C1q thus inhibiting C1;
CC may perform the receptor function through a complex with C1qR/CD93. In
CC complex with cytokeratin-1/KRT1 is a high affinity receptor for
CC kininogen-1/HMWK. Can also bind other plasma proteins, such as
CC coagulation factor XII leading to its autoactivation. May function to
CC bind initially fluid kininogen-1 to the cell membrane. The secreted
CC form may enhance both extrinsic and intrinsic coagulation pathways. It
CC is postulated that the cell surface form requires docking with
CC transmembrane proteins for downstream signaling which might be specific
CC for a cell-type or response. By acting as C1q receptor is involved in
CC chemotaxis of immature dendritic cells and neutrophils and is proposed
CC to signal through CD209/DC-SIGN on immature dendritic cells, through
CC integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and
CC through integrin beta-1 during endothelial cell adhesion and spreading.
CC Signaling involved in inhibition of innate immune response is
CC implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in
CC mitochondria. In mitochondrial translation may be involved in formation
CC of functional 55S mitoribosomes; the function seems to involve its RNA-
CC binding activity. May be involved in the nucleolar ribosome maturation
CC process; the function may involve the exchange of FBL for RRP1 in the
CC association with pre-ribosome particles. Involved in regulation of RNA
CC splicing by inhibiting the RNA-binding capacity of SRSF1 and its
CC phosphorylation. Is required for the nuclear translocation of splicing
CC factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated
CC apoptosis. May be involved in regulation of FOXC1 transcriptional
CC activity and NFY/CCAAT-binding factor complex-mediated transcription.
CC May play a role in antibacterial defense.
CC {ECO:0000250|UniProtKB:Q07021}.
CC -!- SUBUNIT: Homotrimer; three monomers form a donut-shaped structure with
CC an unusually asymmetric charge distribution on the surface. Interacts
CC with CDK13, HRK, VTN, NFYB, ADRA1B, FOXC1, DDX21, DDX50, NCL, SRSF1 and
CC SRSF9. Interacts with CD93; the association may represent a cell
CC surface C1q receptor. Interacts with KRT1; the association represents a
CC cell surface kininogen receptor. Interacts with CD209; the interaction
CC is indicative for a C1q:C1QBP:CD209 signaling complex. Interacts with
CC FBL and RRP1; the respective interactions with C1QBP are competitive.
CC Probably associates with the mitoribosome. Interacts with MAVS; the
CC interaction occurs upon viral transfection. Interacts with PPIF.
CC Interacts with U2AF1L4. Interacts with PLEKHN1. Interacts with VGF-
CC derived peptide TLQP-21 (PubMed:24106277).
CC {ECO:0000250|UniProtKB:O35658, ECO:0000250|UniProtKB:Q07021,
CC ECO:0000269|PubMed:24106277}.
CC -!- INTERACTION:
CC O35796; P18841: ADRA1B; Xeno; NbExp=5; IntAct=EBI-915544, EBI-6391008;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q07021}. Nucleus {ECO:0000250|UniProtKB:Q07021}.
CC Cell membrane {ECO:0000250|UniProtKB:Q07021}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q07021}; Extracellular side
CC {ECO:0000250|UniProtKB:Q07021}. Secreted
CC {ECO:0000250|UniProtKB:Q07021}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q07021}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q07021}. Note=Seems to be predominantly
CC localized to mitochondria. Secreted by activated lymphocytes.
CC {ECO:0000250|UniProtKB:Q07021}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9414106}.
CC -!- SIMILARITY: Belongs to the MAM33 family. {ECO:0000305}.
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DR EMBL; AJ001102; CAA04531.1; -; mRNA.
DR EMBL; BC070510; AAH70510.1; -; mRNA.
DR RefSeq; NP_062132.2; NM_019259.2.
DR AlphaFoldDB; O35796; -.
DR SMR; O35796; -.
DR BioGRID; 248302; 4.
DR IntAct; O35796; 9.
DR MINT; O35796; -.
DR STRING; 10116.ENSRNOP00000031020; -.
DR iPTMnet; O35796; -.
DR PhosphoSitePlus; O35796; -.
DR jPOST; O35796; -.
DR PaxDb; O35796; -.
DR PRIDE; O35796; -.
DR GeneID; 29681; -.
DR KEGG; rno:29681; -.
DR UCSC; RGD:2230; rat.
DR CTD; 708; -.
DR RGD; 2230; C1qbp.
DR VEuPathDB; HostDB:ENSRNOG00000006949; -.
DR eggNOG; KOG4024; Eukaryota.
DR HOGENOM; CLU_083914_0_0_1; -.
DR InParanoid; O35796; -.
DR OMA; YEHTAYV; -.
DR OrthoDB; 888304at2759; -.
DR PhylomeDB; O35796; -.
DR TreeFam; TF315160; -.
DR Reactome; R-RNO-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR PRO; PR:O35796; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000006949; Expressed in ovary and 20 other tissues.
DR Genevisible; O35796; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SynGO.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0048786; C:presynaptic active zone; IDA:SynGO.
DR GO; GO:0031690; F:adrenergic receptor binding; IDA:UniProtKB.
DR GO; GO:0001849; F:complement component C1q complex binding; IDA:RGD.
DR GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
DR GO; GO:0030984; F:kininogen binding; ISS:UniProtKB.
DR GO; GO:0097177; F:mitochondrial ribosome binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; IDA:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; TAS:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0042256; P:mature ribosome assembly; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0050687; P:negative regulation of defense response to virus; ISS:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; ISS:UniProtKB.
DR GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; ISS:UniProtKB.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:1901165; P:positive regulation of trophoblast cell migration; ISS:UniProtKB.
DR GO; GO:0030449; P:regulation of complement activation; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.10.280.10; -; 1.
DR InterPro; IPR003428; MAM33.
DR InterPro; IPR036561; MAM33_sf.
DR PANTHER; PTHR10826; PTHR10826; 1.
DR Pfam; PF02330; MAM33; 1.
DR SUPFAM; SSF54529; SSF54529; 1.
PE 1: Evidence at protein level;
KW Acetylation; Adaptive immunity; Apoptosis; Cell membrane;
KW Complement pathway; Cytoplasm; Direct protein sequencing; Immunity;
KW Innate immunity; Membrane; Mitochondrion; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis; Secreted;
KW Transcription; Transcription regulation; Transit peptide.
FT TRANSIT 1..71
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 72..279
FT /note="Complement component 1 Q subcomponent-binding
FT protein, mitochondrial"
FT /id="PRO_0000018592"
FT REGION 74..91
FT /note="C1q binding"
FT /evidence="ECO:0000250"
FT REGION 134..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..210
FT /note="Interaction with MAVS"
FT /evidence="ECO:0000250"
FT MOD_RES 89
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q07021"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35658"
FT MOD_RES 185
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q07021"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07021"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07021"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07021"
FT CONFLICT 63..64
FT /note="VP -> GS (in Ref. 1; CAA04531)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..70
FT /note="GCG -> AA (in Ref. 1; CAA04531)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="W -> G (in Ref. 1; CAA04531)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="E -> Q (in Ref. 1; CAA04531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 30997 MW; 54D238EFBCA6F41B CRC64;
MLPLLRCVPR ALGAAATGLR ASIPAPPLRH LLQPAPRPCL RPFGLLSVRA GSARRSGLLQ
PPVPCACGCG ALHTEGDKAF VEFLTDEIKE EKKIQKHKSL PKMSGDWELE VNGTEAKLLR
KVAGEKITVT FNINNSIPPT FDGEEEPSQG QKAEEQEPEL TSTPNFVVEV TKTDGKKTLV
LDCHYPEDEI GHEDEAESDI FSIKEVSFQT TGDSEWRDTN YTLNTDSLDW ALYDHLMDFL
ADRGVDNTFA DELVELSTAL EHQEYITFLE DLKSFVKSQ
