C1QBP_HUMAN
ID C1QBP_HUMAN Reviewed; 282 AA.
AC Q07021; Q2HXR8; Q9NNY8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Complement component 1 Q subcomponent-binding protein, mitochondrial;
DE AltName: Full=ASF/SF2-associated protein p32;
DE AltName: Full=Glycoprotein gC1qBP;
DE Short=C1qBP;
DE AltName: Full=Hyaluronan-binding protein 1;
DE AltName: Full=Mitochondrial matrix protein p32;
DE AltName: Full=gC1q-R protein;
DE AltName: Full=p33;
DE Short=SF2AP32 {ECO:0000303|PubMed:18191643};
DE Flags: Precursor;
GN Name=C1QBP; Synonyms=GC1QBP, HABP1, SF2P32;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 74; 76-93 AND 208-216.
RC TISSUE=Fibroblast;
RX PubMed=8262387; DOI=10.1016/0378-1119(93)90108-f;
RA Honore B., Madsen P., Rasmussen H.H., Vandekerckhove J., Celis J.E.,
RA Leffers H.;
RT "Cloning and expression of a cDNA covering the complete coding region of
RT the P32 subunit of human pre-mRNA splicing factor SF2.";
RL Gene 134:283-287(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8195709; DOI=10.1084/jem.179.6.1809;
RA Ghebrehiwet B., Lim B.L., Peerschke E.I., Willis A.C., Reid K.B.;
RT "Isolation, cDNA cloning, and overexpression of a 33-kD cell surface
RT glycoprotein that binds to the globular 'heads' of C1q.";
RL J. Exp. Med. 179:1809-1821(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11278463; DOI=10.1074/jbc.m009064200;
RA Tye A.J., Ghebrehiwet B., Guo N., Sastry K.N., Chow B.K.C.,
RA Peerschke E.I.B., Lim B.L.;
RT "The human gC1qR/p32 gene, C1qBP. Genomic organization and promoter
RT analysis.";
RL J. Biol. Chem. 276:17069-17075(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-282, AND PROTEIN SEQUENCE OF 74-114.
RX PubMed=1830244; DOI=10.1016/0092-8674(91)90627-b;
RA Krainer A.R., Mayeda A., Kozak D., Binns G.;
RT "Functional expression of cloned human splicing factor SF2: homology to
RT RNA-binding proteins, U1 70K, and Drosophila splicing regulators.";
RL Cell 66:383-394(1991).
RN [8]
RP PROTEIN SEQUENCE OF 74-88, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8662673; DOI=10.1074/jbc.271.22.13040;
RA Herwald H., Dedio J., Kellner R., Loos M., Muller-Esterl W.;
RT "Isolation and characterization of the kininogen-binding protein p33 from
RT endothelial cells. Identity with the gC1q receptor.";
RL J. Biol. Chem. 271:13040-13047(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 86-282.
RX PubMed=8567680; DOI=10.1074/jbc.271.4.2206;
RA Deb T.B., Datta K.;
RT "Molecular cloning of human fibroblast hyaluronic acid-binding protein
RT confirms its identity with P-32, a protein co-purified with splicing factor
RT SF2. Hyaluronic acid-binding protein as P-32 protein, co-purified with
RT splicing factor SF2.";
RL J. Biol. Chem. 271:2206-2212(1996).
RN [10]
RP INTERACTION WITH VTN.
RX PubMed=8900153; DOI=10.1074/jbc.271.43.26739;
RA Lim B.L., Reid K.B., Ghebrehiwet B., Peerschke E.I., Leigh L.A.,
RA Preissner K.T.;
RT "The binding protein for globular heads of complement C1q, gC1qR.
RT Functional expression and characterization as a novel vitronectin binding
RT factor.";
RL J. Biol. Chem. 271:26739-26744(1996).
RN [11]
RP FUNCTION.
RX PubMed=8710908; DOI=10.1073/pnas.93.16.8552;
RA Joseph K., Ghebrehiwet B., Peerschke E.I., Reid K.B., Kaplan A.P.;
RT "Identification of the zinc-dependent endothelial cell binding protein for
RT high molecular weight kininogen and factor XII: identity with the receptor
RT that binds to the globular 'heads' of C1q (gC1q-R).";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8552-8557(1996).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=9191880; DOI=10.1006/clin.1997.4374;
RA Peterson K.L., Zhang W., Lu P.D., Keilbaugh S.A., Peerschke E.I.,
RA Ghebrehiwet B.;
RT "The C1q-binding cell membrane proteins cC1q-R and gC1q-R are released from
RT activated cells: subcellular distribution and immunochemical
RT characterization.";
RL Clin. Immunol. Immunopathol. 84:17-26(1997).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=9305894; DOI=10.1074/jbc.272.39.24363;
RA Muta T., Kang D., Kitajima S., Fujiwara T., Hamasaki N.;
RT "p32 protein, a splicing factor 2-associated protein, is localized in
RT mitochondrial matrix and is functionally important in maintaining oxidative
RT phosphorylation.";
RL J. Biol. Chem. 272:24363-24370(1997).
RN [14]
RP INTERACTION WITH CD93, AND SUBCELLULAR LOCATION.
RX PubMed=9233640;
RA Ghebrehiwet B., Lu P.D., Zhang W., Keilbaugh S.A., Leigh L.E., Eggleton P.,
RA Reid K.B., Peerschke E.I.;
RT "Evidence that the two C1q binding membrane proteins, gC1q-R and cC1q-R,
RT associate to form a complex.";
RL J. Immunol. 159:1429-1436(1997).
RN [15]
RP FUNCTION.
RX PubMed=9461517; DOI=10.1042/bj3300247;
RA Leigh L.E., Ghebrehiwet B., Perera T.P., Bird I.N., Strong P., Kishore U.,
RA Reid K.B., Eggleton P.;
RT "C1q-mediated chemotaxis by human neutrophils: involvement of gClqR and G-
RT protein signalling mechanisms.";
RL Biochem. J. 330:247-254(1998).
RN [16]
RP FUNCTION.
RX PubMed=10479529; DOI=10.1006/clim.1999.4753;
RA Joseph K., Ghebrehiwet B., Kaplan A.P.;
RT "Cytokeratin 1 and gC1qR mediate high molecular weight kininogen binding to
RT endothelial cells.";
RL Clin. Immunol. 92:246-255(1999).
RN [17]
RP FUNCTION, AND INTERACTION WITH SRSF1 AND SRSF9.
RX PubMed=10022843; DOI=10.1093/emboj/18.4.1014;
RA Petersen-Mahrt S.K., Estmer C., Ohrmalm C., Matthews D.A., Russell W.C.,
RA Akusjarvi G.;
RT "The splicing factor-associated protein, p32, regulates RNA splicing by
RT inhibiting ASF/SF2 RNA binding and phosphorylation.";
RL EMBO J. 18:1014-1024(1999).
RN [18]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH L.MONOCYTOGENES INLB
RP (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=10747014; DOI=10.1093/emboj/19.7.1458;
RA Braun L., Ghebrehiwet B., Cossart P.;
RT "gC1q-R/p32, a C1q-binding protein, is a receptor for the InlB invasion
RT protein of Listeria monocytogenes.";
RL EMBO J. 19:1458-1466(2000).
RN [19]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH STAPHYLOCOCCUS AUREUS
RP SPA.
RX PubMed=10722602; DOI=10.1128/iai.68.4.2061-2068.2000;
RA Nguyen T., Ghebrehiwet B., Peerschke E.I.;
RT "Staphylococcus aureus protein A recognizes platelet gC1qR/p33: a novel
RT mechanism for staphylococcal interactions with platelets.";
RL Infect. Immun. 68:2061-2068(2000).
RN [20]
RP FUNCTION, AND INTERACTION WITH HCV CORE PROTEIN.
RX PubMed=11086025; DOI=10.1172/jci10323;
RA Kittlesen D.J., Chianese-Bullock K.A., Yao Z.Q., Braciale T.J., Hahn Y.S.;
RT "Interaction between complement receptor gC1qR and hepatitis C virus core
RT protein inhibits T-lymphocyte proliferation.";
RL J. Clin. Invest. 106:1239-1249(2000).
RN [21]
RP INTERACTION WITH RUBELLA VIRUS CAPSID PROTEIN.
RX PubMed=10823864; DOI=10.1128/jvi.74.12.5569-5576.2000;
RA Beatch M.D., Hobman T.C.;
RT "Rubella virus capsid associates with host cell protein p32 and localizes
RT to mitochondria.";
RL J. Virol. 74:5569-5576(2000).
RN [22]
RP SUBCELLULAR LOCATION.
RX PubMed=11493647; DOI=10.1242/jcs.114.11.2115;
RA van Leeuwen H.C., O'Hare P.;
RT "Retargeting of the mitochondrial protein p32/gC1Qr to a cytoplasmic
RT compartment and the cell surface.";
RL J. Cell Sci. 114:2115-2123(2001).
RN [23]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH L.MONOCYTOGENES INLB
RP (MICROBIAL INFECTION).
RX PubMed=12411480; DOI=10.1093/emboj/cdf558;
RA Marino M., Banerjee M., Jonquieres R., Cossart P., Ghosh P.;
RT "GW domains of the Listeria monocytogenes invasion protein InlB are SH3-
RT like and mediate binding to host ligands.";
RL EMBO J. 21:5623-5634(2002).
RN [24]
RP FUNCTION.
RX PubMed=11859136; DOI=10.4049/jimmunol.168.5.2441;
RA Feng X., Tonnesen M.G., Peerschke E.I., Ghebrehiwet B.;
RT "Cooperation of C1q receptors and integrins in C1q-mediated endothelial
RT cell adhesion and spreading.";
RL J. Immunol. 168:2441-2448(2002).
RN [25]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH RUBELLA VIRUS CAPSID
RP PROTEIN.
RX PubMed=12034482; DOI=10.1016/s0168-1702(02)00030-8;
RA Mohan K.V., Ghebrehiwet B., Atreya C.D.;
RT "The N-terminal conserved domain of rubella virus capsid interacts with the
RT C-terminal region of cellular p32 and overexpression of p32 enhances the
RT viral infectivity.";
RL Virus Res. 85:151-161(2002).
RN [26]
RP FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF GLY-107.
RX PubMed=12833064; DOI=10.1038/ncb1000;
RA Zheng Y.H., Yu H.F., Peterlin B.M.;
RT "Human p32 protein relieves a post-transcriptional block to HIV replication
RT in murine cells.";
RL Nat. Cell Biol. 5:611-618(2003).
RN [27]
RP ERRATUM OF PUBMED:12833064.
RA Zheng Y.H., Yu H.F., Peterlin B.M.;
RL Nat. Cell Biol. 5:839-839(2003).
RN [28]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12574814; DOI=10.1267/THRO03020331;
RA Peerschke E.I., Murphy T.K., Ghebrehiwet B.;
RT "Activation-dependent surface expression of gC1qR/p33 on human blood
RT platelets.";
RL Thromb. Haemost. 89:331-339(2003).
RN [29]
RP INTERACTION WITH HRK, AND SUBCELLULAR LOCATION.
RX PubMed=15031724; DOI=10.1038/sj.cdd.4401418;
RA Sunayama J., Ando Y., Itoh N., Tomiyama A., Sakurada K., Sugiyama A.,
RA Kang D., Tashiro F., Gotoh Y., Kuchino Y., Kitanaka C.;
RT "Physical and functional interaction between BH3-only protein Hrk and
RT mitochondrial pore-forming protein p32.";
RL Cell Death Differ. 11:771-781(2004).
RN [30]
RP FUNCTION, AND INTERACTION WITH NFYB.
RX PubMed=15243141; DOI=10.1093/nar/gkh692;
RA Chattopadhyay C., Hawke D., Kobayashi R., Maity S.N.;
RT "Human p32, interacts with B subunit of the CCAAT-binding factor, CBF/NF-Y,
RT and inhibits CBF-mediated transcription activation in vitro.";
RL Nucleic Acids Res. 32:3632-3641(2004).
RN [31]
RP FUNCTION, AND INDUCTION.
RX PubMed=16177118; DOI=10.4049/jimmunol.175.7.4706;
RA Waggoner S.N., Cruise M.W., Kassel R., Hahn Y.S.;
RT "gC1q receptor ligation selectively down-regulates human IL-12 production
RT through activation of the phosphoinositide 3-kinase pathway.";
RL J. Immunol. 175:4706-4714(2005).
RN [32]
RP ERRATUM OF PUBMED:16177118.
RA Waggoner S.N., Cruise M.W., Kassel R., Hahn Y.S.;
RL J. Immunol. 178:3332-3332(2007).
RN [33]
RP INTERACTION WITH CDK13.
RX PubMed=16721827; DOI=10.1002/jcb.20986;
RA Even Y., Durieux S., Escande M.L., Lozano J.C., Peaucellier G., Weil D.,
RA Geneviere A.M.;
RT "CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-
RT associated protein p32 and affects splicing in vivo.";
RL J. Cell. Biochem. 99:890-904(2006).
RN [34]
RP INTERACTION WITH HIV-1 TAT.
RX PubMed=16537587; DOI=10.1128/jvi.80.7.3189-3204.2006;
RA Berro R., Kehn K., de la Fuente C., Pumfery A., Adair R., Wade J.,
RA Colberg-Poley A.M., Hiscott J., Kashanchi F.;
RT "Acetylated Tat regulates human immunodeficiency virus type 1 splicing
RT through its interaction with the splicing regulator p32.";
RL J. Virol. 80:3189-3204(2006).
RN [35]
RP FUNCTION.
RX PubMed=16140380; DOI=10.1016/j.molimm.2005.07.030;
RA Vegh Z., Kew R.R., Gruber B.L., Ghebrehiwet B.;
RT "Chemotaxis of human monocyte-derived dendritic cells to complement
RT component C1q is mediated by the receptors gC1qR and cC1qR.";
RL Mol. Immunol. 43:1402-1407(2006).
RN [36]
RP FUNCTION.
RX PubMed=17881511; DOI=10.1189/jlb.0507268;
RA Waggoner S.N., Hall C.H., Hahn Y.S.;
RT "HCV core protein interaction with gC1q receptor inhibits Th1
RT differentiation of CD4+ T cells via suppression of dendritic cell IL-12
RT production.";
RL J. Leukoc. Biol. 82:1407-1419(2007).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [38]
RP INTERACTION WITH CDKN2A, AND SUBCELLULAR LOCATION.
RX PubMed=17486078; DOI=10.1038/sj.onc.1210485;
RA Reef S., Shifman O., Oren M., Kimchi A.;
RT "The autophagic inducer smARF interacts with and is stabilized by the
RT mitochondrial p32 protein.";
RL Oncogene 26:6677-6683(2007).
RN [39]
RP INTERACTION WITH PLEKHN1.
RX PubMed=18191643; DOI=10.1016/j.bbamcr.2007.12.009;
RA Sano E., Shono S., Tashiro K., Konishi H., Yamauchi E., Taniguchi H.;
RT "Novel tyrosine phosphorylated and cardiolipin-binding protein CLPABP
RT functions as mitochondrial RNA granule.";
RL Biochim. Biophys. Acta 1783:1036-1047(2008).
RN [40]
RP FUNCTION, INTERACTION WITH FOXC1, AND SUBCELLULAR LOCATION.
RX PubMed=18676636; DOI=10.1167/iovs.07-1625;
RA Huang L., Chi J., Berry F.B., Footz T.K., Sharp M.W., Walter M.A.;
RT "Human p32 is a novel FOXC1-interacting protein that regulates FOXC1
RT transcriptional activity in ocular cells.";
RL Invest. Ophthalmol. Vis. Sci. 49:5243-5249(2008).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [42]
RP FUNCTION.
RX PubMed=19004836; DOI=10.1074/jbc.m804246200;
RA Yadav G., Prasad R.L., Jha B.K., Rai V., Bhakuni V., Datta K.;
RT "Evidence for inhibitory interaction of hyaluronan-binding protein 1
RT (HABP1/p32/gC1qR) with Streptococcus pneumoniae hyaluronidase.";
RL J. Biol. Chem. 284:3897-3905(2009).
RN [43]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAVS.
RX PubMed=19164550; DOI=10.1073/pnas.0811029106;
RA Xu L., Xiao N., Liu F., Ren H., Gu J.;
RT "Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1530-1535(2009).
RN [44]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [45]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [46]
RP FUNCTION.
RX PubMed=20810993; DOI=10.4049/jimmunol.0903215;
RA Agostinis C., Bulla R., Tripodo C., Gismondi A., Stabile H., Bossi F.,
RA Guarnotta C., Garlanda C., De Seta F., Spessotto P., Santoni A.,
RA Ghebrehiwet B., Girardi G., Tedesco F.;
RT "An alternative role of C1q in cell migration and tissue remodeling:
RT contribution to trophoblast invasion and placental development.";
RL J. Immunol. 185:4420-4429(2010).
RN [47]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [48]
RP INTERACTION WITH PPIF.
RX PubMed=20950273; DOI=10.1042/bj20101431;
RA McGee A.M., Baines C.P.;
RT "Complement 1q-binding protein inhibits the mitochondrial permeability
RT transition pore and protects against oxidative stress-induced death.";
RL Biochem. J. 433:119-125(2011).
RN [49]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FBL; RRP1; DDX21;
RP DDX50 AND NCL.
RX PubMed=21536856; DOI=10.1074/mcp.m110.006148;
RA Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K.,
RA Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T.,
RA Takahashi N.;
RT "Splicing factor 2-associated protein p32 participates in ribosome
RT biogenesis by regulating the binding of Nop52 and fibrillarin to
RT preribosome particles.";
RL Mol. Cell. Proteomics 10:0-0(2011).
RN [50]
RP FUNCTION, AND INTERACTION WITH KRT1.
RX PubMed=21544310; DOI=10.1160/th10-09-0591;
RA Pixley R.A., Espinola R.G., Ghebrehiwet B., Joseph K., Kao A., Bdeir K.,
RA Cines D.B., Colman R.W.;
RT "Interaction of high-molecular-weight kininogen with endothelial cell
RT binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface
RT plasmon resonance (BiaCore).";
RL Thromb. Haemost. 105:1053-1059(2011).
RN [51]
RP FUNCTION, AND INTERACTION WITH CD209.
RX PubMed=22700724; DOI=10.1182/blood-2011-07-369728;
RA Hosszu K.K., Valentino A., Vinayagasundaram U., Vinayagasundaram R.,
RA Joyce M.G., Ji Y., Peerschke E.I., Ghebrehiwet B.;
RT "DC-SIGN, C1q, and gC1qR form a trimolecular receptor complex on the
RT surface of monocyte-derived immature dendritic cells.";
RL Blood 120:1228-1236(2012).
RN [52]
RP INTERACTION WITH RUBELLA VIRUS PROTEASE/METHYLTRANSFERASE P150.
RX PubMed=22238231; DOI=10.1099/vir.0.038901-0;
RA Suppiah S., Mousa H.A., Tzeng W.P., Matthews J.D., Frey T.K.;
RT "Binding of cellular p32 protein to the rubella virus P150 replicase
RT protein via PxxPxR motifs.";
RL J. Gen. Virol. 93:807-816(2012).
RN [53]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [54]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND THR-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [55]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER SER-73, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [56]
RP INTERACTION WITH POLGARF, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=32958672; DOI=10.1073/pnas.2001433117;
RA Loughran G., Zhdanov A.V., Mikhaylova M.S., Rozov F.N., Datskevich P.N.,
RA Kovalchuk S.I., Serebryakova M.V., Kiniry S.J., Michel A.M.,
RA O'Connor P.B.F., Papkovsky D.B., Atkins J.F., Baranov P.V., Shatsky I.N.,
RA Andreev D.E.;
RT "Unusually efficient CUG initiation of an overlapping reading frame in POLG
RT mRNA yields novel protein POLGARF.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:24936-24946(2020).
RN [57]
RP FUNCTION, INVOLVEMENT IN COXPD33, AND VARIANTS COXPD33 SER-186; TYR-188
RP DEL; LEU-204; TRP-247; PHE-275 AND PRO-275.
RX PubMed=28942965; DOI=10.1016/j.ajhg.2017.08.015;
RA Feichtinger R.G., Olahova M., Kishita Y., Garone C., Kremer L.S., Yagi M.,
RA Uchiumi T., Jourdain A.A., Thompson K., D'Souza A.R., Kopajtich R.,
RA Alston C.L., Koch J., Sperl W., Mastantuono E., Strom T.M., Wortmann S.B.,
RA Meitinger T., Pierre G., Chinnery P.F., Chrzanowska-Lightowlers Z.M.,
RA Lightowlers R.N., DiMauro S., Calvo S.E., Mootha V.K., Moggio M.,
RA Sciacco M., Comi G.P., Ronchi D., Murayama K., Ohtake A.,
RA Rebelo-Guiomar P., Kohda M., Kang D., Mayr J.A., Taylor R.W., Okazaki Y.,
RA Minczuk M., Prokisch H.;
RT "Biallelic C1QBP mutations cause severe neonatal-, childhood-, or later-
RT onset cardiomyopathy associated with combined respiratory-chain
RT deficiencies.";
RL Am. J. Hum. Genet. 101:525-538(2017).
RN [58]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX PubMed=10097078; DOI=10.1073/pnas.96.7.3572;
RA Jiang J., Zhang Y., Krainer A.R., Xu R.-M.;
RT "Crystal structure of human p32, a doughnut-shaped acidic mitochondrial
RT matrix protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3572-3577(1999).
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 (PubMed:28942965). In mitochondrial translation may be
CC involved in formation of functional 55S mitoribosomes; the function
CC seems to involve its RNA-binding activity. May be involved in the
CC nucleolar ribosome maturation process; the function may involve the
CC exchange of FBL for RRP1 in the association with pre-ribosome
CC particles. Involved in regulation of RNA splicing by inhibiting the
CC RNA-binding capacity of SRSF1 and its phosphorylation. Is required for
CC the nuclear translocation of splicing factor U2AF1L4. Involved in
CC regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes
CC mitochondrial CDKN2A isoform smARF. May be involved in regulation of
CC FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-
CC mediated transcription. May play a role in antibacterial defense as it
CC can bind to cell surface hyaluronan and inhibit Streptococcus
CC pneumoniae hyaluronate lyase. May be involved in modulation of the
CC immune response; ligation by HCV core protein is resulting in
CC suppression of interleukin-12 production in monocyte-derived dendritic
CC cells. Involved in regulation of antiviral response by inhibiting
CC DDX58- and IFIH1-mediated signaling pathways probably involving its
CC association with MAVS after viral infection.
CC {ECO:0000269|PubMed:10022843, ECO:0000269|PubMed:10479529,
CC ECO:0000269|PubMed:10722602, ECO:0000269|PubMed:11086025,
CC ECO:0000269|PubMed:11859136, ECO:0000269|PubMed:15243141,
CC ECO:0000269|PubMed:16140380, ECO:0000269|PubMed:16177118,
CC ECO:0000269|PubMed:17881511, ECO:0000269|PubMed:18676636,
CC ECO:0000269|PubMed:19004836, ECO:0000269|PubMed:19164550,
CC ECO:0000269|PubMed:20810993, ECO:0000269|PubMed:21536856,
CC ECO:0000269|PubMed:21544310, ECO:0000269|PubMed:22700724,
CC ECO:0000269|PubMed:28942965, ECO:0000269|PubMed:8662673,
CC ECO:0000269|PubMed:8710908, ECO:0000269|PubMed:9461517}.
CC -!- FUNCTION: (Microbial infection) Involved in HIV-1 replication,
CC presumably by contributing to splicing of viral RNA.
CC {ECO:0000269|PubMed:12833064}.
CC -!- FUNCTION: (Microbial infection) In infection processes acts as an
CC attachment site for microbial proteins, including Listeria
CC monocytogenes internalin B (InlB) and Staphylococcus aureus protein A.
CC {ECO:0000269|PubMed:10722602, ECO:0000269|PubMed:10747014,
CC ECO:0000269|PubMed:12411480}.
CC -!- FUNCTION: (Microbial infection) Involved in replication of Rubella
CC virus. {ECO:0000269|PubMed:12034482}.
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,
CC SRSF9 and CDKN2A isoform smARF. Interacts with CD93; the association
CC may represent a cell surface C1q receptor. Interacts with KRT1; the
CC association represents a cell surface kininogen receptor. Interacts
CC with CD209; the interaction is indicative for a C1q:C1QBP:CD209
CC signaling complex. Interacts with FBL and RRP1; the respective
CC interactions with C1QBP are competitive. Probably associates with the
CC mitoribosome. Interacts with MAVS; the interaction occurs upon viral
CC transfection. Interacts with PPIF. Interacts with U2AF1L4. Interacts
CC with PLEKHN1 (PubMed:18191643). Interacts with VGF-derived peptide
CC TLQP-21 (By similarity). Interacts with POLGARF which is produced from
CC an alternative reading frame of the POLG gene; the interaction results
CC in nucleolar localization of C1QBP, probably due to prevention of C1QBP
CC maturation and redirection from mitochondria to nucleoli
CC (PubMed:32958672). {ECO:0000250|UniProtKB:O35658,
CC ECO:0000250|UniProtKB:O35796, ECO:0000269|PubMed:10022843,
CC ECO:0000269|PubMed:11086025, ECO:0000269|PubMed:15031724,
CC ECO:0000269|PubMed:15243141, ECO:0000269|PubMed:16721827,
CC ECO:0000269|PubMed:17486078, ECO:0000269|PubMed:18191643,
CC ECO:0000269|PubMed:18676636, ECO:0000269|PubMed:19164550,
CC ECO:0000269|PubMed:20950273, ECO:0000269|PubMed:21536856,
CC ECO:0000269|PubMed:21544310, ECO:0000269|PubMed:22700724,
CC ECO:0000269|PubMed:32958672, ECO:0000269|PubMed:8900153,
CC ECO:0000269|PubMed:9233640}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Rubella virus capsid
CC protein; the interaction occurs in mitochondria (PubMed:10823864,
CC PubMed:12034482). Interacts with Rubella virus
CC protease/methyltransferase p150 (PubMed:22238231).
CC {ECO:0000269|PubMed:10823864, ECO:0000269|PubMed:12034482,
CC ECO:0000269|PubMed:22238231}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC protein A/spa. {ECO:0000269|PubMed:10722602}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC protein A/spa, HIV-1 Tat and HCV core protein.
CC {ECO:0000269|PubMed:10722602}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat and HCV core
CC protein. {ECO:0000269|PubMed:16537587}.
CC -!- SUBUNIT: (Microbial infection) Interacts with L.monocytogenes
CC internalin B. {ECO:0000269|PubMed:10747014,
CC ECO:0000269|PubMed:12411480}.
CC -!- INTERACTION:
CC Q07021; P02647: APOA1; NbExp=2; IntAct=EBI-347528, EBI-701692;
CC Q07021; Q14004-2: CDK13; NbExp=6; IntAct=EBI-347528, EBI-6375898;
CC Q07021; Q8N726: CDKN2A; NbExp=3; IntAct=EBI-347528, EBI-625922;
CC Q07021; P00748: F12; NbExp=2; IntAct=EBI-347528, EBI-6378830;
CC Q07021; Q12948: FOXC1; NbExp=6; IntAct=EBI-347528, EBI-1175253;
CC Q07021; O00198: HRK; NbExp=7; IntAct=EBI-347528, EBI-701322;
CC Q07021; Q13351: KLF1; NbExp=3; IntAct=EBI-347528, EBI-8284732;
CC Q07021; P01042: KNG1; NbExp=4; IntAct=EBI-347528, EBI-6378713;
CC Q07021; Q7Z434: MAVS; NbExp=5; IntAct=EBI-347528, EBI-995373;
CC Q07021; Q05513: PRKCZ; NbExp=4; IntAct=EBI-347528, EBI-295351;
CC Q07021; Q15139: PRKD1; NbExp=9; IntAct=EBI-347528, EBI-1181072;
CC Q07021; Q8N3Z0: PRSS35; NbExp=4; IntAct=EBI-347528, EBI-20628340;
CC Q07021; P04004: VTN; NbExp=9; IntAct=EBI-347528, EBI-1036653;
CC Q07021; P67809: YBX1; NbExp=7; IntAct=EBI-347528, EBI-354065;
CC Q07021; Q64364: Cdkn2a; Xeno; NbExp=4; IntAct=EBI-347528, EBI-1202287;
CC Q07021; PRO_0000240177 [O40955]; Xeno; NbExp=2; IntAct=EBI-347528, EBI-6383633;
CC Q07021; PRO_0000041308 [P07566]; Xeno; NbExp=3; IntAct=EBI-347528, EBI-6377932;
CC Q07021; PRO_0000041302 [P08563]; Xeno; NbExp=3; IntAct=EBI-347528, EBI-11478341;
CC Q07021; PRO_0000037566 [P27958]; Xeno; NbExp=4; IntAct=EBI-347528, EBI-6377335;
CC PRO_0000018590; P02745: C1QA; NbExp=6; IntAct=EBI-14032968, EBI-1220209;
CC PRO_0000018590; P02746: C1QB; NbExp=4; IntAct=EBI-14032968, EBI-2813376;
CC PRO_0000018590; P02747: C1QC; NbExp=4; IntAct=EBI-14032968, EBI-1220222;
CC PRO_0000018590; P0DTC4: E; Xeno; NbExp=3; IntAct=EBI-14032968, EBI-25475850;
CC PRO_0000018590; P0DTC2: S; Xeno; NbExp=2; IntAct=EBI-14032968, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:15031724, ECO:0000269|PubMed:17486078,
CC ECO:0000269|PubMed:19164550, ECO:0000269|PubMed:9305894}. Nucleus
CC {ECO:0000269|PubMed:18676636}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:21536856, ECO:0000269|PubMed:32958672}. Cell
CC membrane {ECO:0000269|PubMed:10747014, ECO:0000269|PubMed:11493647,
CC ECO:0000269|PubMed:12574814, ECO:0000269|PubMed:8195709,
CC ECO:0000269|PubMed:8662673, ECO:0000269|PubMed:9191880,
CC ECO:0000269|PubMed:9233640}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12574814, ECO:0000269|PubMed:8662673,
CC ECO:0000269|PubMed:9191880}; Extracellular side. Secreted. Cytoplasm
CC {ECO:0000269|PubMed:11493647}. Note=Seems to be predominantly localized
CC to mitochondria. Secreted by activated lymphocytes. Localizes to the
CC nucleolus when coexpressed with POLGARF (PubMed:32958672). Interaction
CC with POLGARF is likely to result in prevention of C1QBP maturation and
CC redirection from mitochondria to nucleoli (PubMed:32958672).
CC {ECO:0000269|PubMed:32958672}.
CC -!- TISSUE SPECIFICITY: Expressed on cell surface of peripheral blood cells
CC (at protein level); Surface expression is reported for macrophages and
CC monocyte-derived dendritic cells. {ECO:0000269|PubMed:12574814,
CC ECO:0000269|PubMed:8662673}.
CC -!- INDUCTION: Enhanced cell surface expression upon platelet and monocyte
CC activation. {ECO:0000269|PubMed:12574814, ECO:0000269|PubMed:16177118}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 33 (COXPD33)
CC [MIM:617713]: An autosomal recessive disorder caused by multiple
CC mitochondrial respiratory chain defects and impaired mitochondrial
CC energy metabolism. Clinical manifestations are highly variable.
CC Affected infants present with cardiomyopathy accompanied by
CC multisystemic features involving liver, kidney, and brain. Death in
CC infancy is observed in some patients. Children and adults present with
CC myopathy and progressive external ophthalmoplegia.
CC {ECO:0000269|PubMed:28942965}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the MAM33 family. {ECO:0000305}.
CC -!- CAUTION: The subcellular location has been matter of debate. After
CC being reported to be exclusively localized to mitochondria,
CC demonstrations of promiscuous associations and locations were
CC considered as artifactual due to the extremely acidic character and the
CC use of different tagged versions of the protein (PubMed:9305894,
CC PubMed:11493647). However, its location to multiple compartments linked
CC to diverse functions is now accepted. The N-termini of the surface and
CC secreted forms are identical to the reported processed mitochondrial
CC form. {ECO:0000305|PubMed:11493647, ECO:0000305|PubMed:9305894}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/c1qbp/";
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DR EMBL; L04636; AAA16315.1; -; mRNA.
DR EMBL; X75913; CAA53512.1; -; mRNA.
DR EMBL; AF338439; AAK26580.1; -; Genomic_DNA.
DR EMBL; BT019898; AAV38701.1; -; mRNA.
DR EMBL; BT019899; AAV38702.1; -; mRNA.
DR EMBL; DQ372108; ABC79624.1; -; Genomic_DNA.
DR EMBL; BC000435; AAH00435.1; -; mRNA.
DR EMBL; BC013731; AAH13731.1; -; mRNA.
DR EMBL; M69039; AAA73055.1; -; mRNA.
DR EMBL; AF275902; AAF78763.1; -; mRNA.
DR CCDS; CCDS11071.1; -.
DR PIR; JT0762; JT0762.
DR RefSeq; NP_001203.1; NM_001212.3.
DR PDB; 1P32; X-ray; 2.25 A; A/B/C=74-282.
DR PDB; 3RPX; X-ray; 2.65 A; A/B/C=96-282.
DR PDB; 6SZW; X-ray; 3.14 A; A/B/C=74-282.
DR PDBsum; 1P32; -.
DR PDBsum; 3RPX; -.
DR PDBsum; 6SZW; -.
DR AlphaFoldDB; Q07021; -.
DR SMR; Q07021; -.
DR BioGRID; 107169; 754.
DR CORUM; Q07021; -.
DR DIP; DIP-31164N; -.
DR IntAct; Q07021; 274.
DR MINT; Q07021; -.
DR STRING; 9606.ENSP00000225698; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB08818; Hyaluronic acid.
DR TCDB; 9.B.103.1.1; the putative ca(2+) uniporter (gc1qr) family.
DR GlyGen; Q07021; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q07021; -.
DR PhosphoSitePlus; Q07021; -.
DR SwissPalm; Q07021; -.
DR BioMuta; C1QBP; -.
DR DMDM; 730772; -.
DR DOSAC-COBS-2DPAGE; Q07021; -.
DR OGP; Q07021; -.
DR CPTAC; CPTAC-176; -.
DR EPD; Q07021; -.
DR jPOST; Q07021; -.
DR MassIVE; Q07021; -.
DR MaxQB; Q07021; -.
DR PaxDb; Q07021; -.
DR PeptideAtlas; Q07021; -.
DR PRIDE; Q07021; -.
DR ProteomicsDB; 58500; -.
DR TopDownProteomics; Q07021; -.
DR Antibodypedia; 11562; 556 antibodies from 38 providers.
DR DNASU; 708; -.
DR Ensembl; ENST00000225698.8; ENSP00000225698.4; ENSG00000108561.8.
DR GeneID; 708; -.
DR KEGG; hsa:708; -.
DR MANE-Select; ENST00000225698.8; ENSP00000225698.4; NM_001212.4; NP_001203.1.
DR UCSC; uc002gby.2; human.
DR CTD; 708; -.
DR DisGeNET; 708; -.
DR GeneCards; C1QBP; -.
DR HGNC; HGNC:1243; C1QBP.
DR HPA; ENSG00000108561; Low tissue specificity.
DR MalaCards; C1QBP; -.
DR MIM; 601269; gene.
DR MIM; 617713; phenotype.
DR neXtProt; NX_Q07021; -.
DR OpenTargets; ENSG00000108561; -.
DR PharmGKB; PA25624; -.
DR VEuPathDB; HostDB:ENSG00000108561; -.
DR eggNOG; KOG4024; Eukaryota.
DR GeneTree; ENSGT00390000018406; -.
DR InParanoid; Q07021; -.
DR OMA; YEHTAYV; -.
DR OrthoDB; 888304at2759; -.
DR PhylomeDB; Q07021; -.
DR TreeFam; TF315160; -.
DR PathwayCommons; Q07021; -.
DR Reactome; R-HSA-111471; Apoptotic factor-mediated response.
DR Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9645722; Defective Intrinsic Pathway for Apoptosis Due to p14ARF Loss of Function.
DR SignaLink; Q07021; -.
DR SIGNOR; Q07021; -.
DR BioGRID-ORCS; 708; 219 hits in 1082 CRISPR screens.
DR ChiTaRS; C1QBP; human.
DR EvolutionaryTrace; Q07021; -.
DR GeneWiki; C1QBP; -.
DR GenomeRNAi; 708; -.
DR Pharos; Q07021; Tbio.
DR PRO; PR:Q07021; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q07021; protein.
DR Bgee; ENSG00000108561; Expressed in mucosa of transverse colon and 203 other tissues.
DR ExpressionAtlas; Q07021; baseline and differential.
DR Genevisible; Q07021; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:CACAO.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR GO; GO:0031690; F:adrenergic receptor binding; ISS:UniProtKB.
DR GO; GO:0001849; F:complement component C1q complex binding; IDA:UniProtKB.
DR GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
DR GO; GO:0030984; F:kininogen binding; IDA: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; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; IDA: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:ProtInc.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0042256; P:mature ribosome assembly; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:UniProtKB.
DR GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; IDA:UniProtKB.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:1901165; P:positive regulation of trophoblast cell migration; IMP:UniProtKB.
DR GO; GO:0030449; P:regulation of complement activation; IDA: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 3D-structure; Acetylation; Adaptive immunity; Apoptosis; Cell membrane;
KW Complement pathway; Cytoplasm; Direct protein sequencing; Disease variant;
KW Host-virus interaction; Immunity; Innate immunity; Membrane; Mitochondrion;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome; Ribosome biogenesis;
KW Secreted; Transcription; Transcription regulation; Transit peptide.
FT TRANSIT 1..73
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1830244,
FT ECO:0000269|PubMed:8662673, ECO:0007744|PubMed:25944712"
FT CHAIN 74..282
FT /note="Complement component 1 Q subcomponent-binding
FT protein, mitochondrial"
FT /id="PRO_0000018590"
FT REGION 76..93
FT /note="C1q binding"
FT REGION 138..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..213
FT /note="Interaction with MAVS"
FT /evidence="ECO:0000269|PubMed:19164550"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 188
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17693683,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 186
FT /note="C -> S (in COXPD33; unknown pathological
FT significance; dbSNP:rs748497469)"
FT /evidence="ECO:0000269|PubMed:28942965"
FT /id="VAR_080391"
FT VARIANT 188
FT /note="Missing (in COXPD33; unknown pathological
FT significance; dbSNP:rs755568057)"
FT /evidence="ECO:0000269|PubMed:28942965"
FT /id="VAR_080392"
FT VARIANT 204
FT /note="F -> L (in COXPD33; unknown pathological
FT significance; dbSNP:rs767427194)"
FT /evidence="ECO:0000269|PubMed:28942965"
FT /id="VAR_080393"
FT VARIANT 247
FT /note="G -> W (in COXPD33; dbSNP:rs1394499137)"
FT /evidence="ECO:0000269|PubMed:28942965"
FT /id="VAR_080394"
FT VARIANT 275
FT /note="L -> F (in COXPD33; unknown pathological
FT significance; dbSNP:rs1555532484)"
FT /evidence="ECO:0000269|PubMed:28942965"
FT /id="VAR_080395"
FT VARIANT 275
FT /note="L -> P (in COXPD33; dbSNP:rs1555532483)"
FT /evidence="ECO:0000269|PubMed:28942965"
FT /id="VAR_080396"
FT MUTAGEN 107
FT /note="G->D: Impairs HIV RNA splicing in mouse cells."
FT /evidence="ECO:0000269|PubMed:12833064"
FT HELIX 77..96
FT /evidence="ECO:0007829|PDB:1P32"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:3RPX"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1P32"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:1P32"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:1P32"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:1P32"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1P32"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:1P32"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6SZW"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:1P32"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:1P32"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:1P32"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1P32"
FT HELIX 250..280
FT /evidence="ECO:0007829|PDB:1P32"
SQ SEQUENCE 282 AA; 31362 MW; 2F747FA73BB1314B CRC64;
MLPLLRCVPR VLGSSVAGLR AAAPASPFRQ LLQPAPRLCT RPFGLLSVRA GSERRPGLLR
PRGPCACGCG CGSLHTDGDK AFVDFLSDEI KEERKIQKHK TLPKMSGGWE LELNGTEAKL
VRKVAGEKIT VTFNINNSIP PTFDGEEEPS QGQKVEEQEP ELTSTPNFVV EVIKNDDGKK
ALVLDCHYPE DEVGQEDEAE SDIFSIREVS FQSTGESEWK DTNYTLNTDS LDWALYDHLM
DFLADRGVDN TFADELVELS TALEHQEYIT FLEDLKSFVK SQ
