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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)

 C1QBP_HUMAN             Reviewed;         282 AA.
Q07021; Q2HXR8; Q9NNY8;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
12-SEP-2018, entry version 187.
RecName: Full=Complement component 1 Q subcomponent-binding protein, mitochondrial;
AltName: Full=ASF/SF2-associated protein p32;
AltName: Full=Glycoprotein gC1qBP;
Short=C1qBP;
AltName: Full=Hyaluronan-binding protein 1;
AltName: Full=Mitochondrial matrix protein p32;
AltName: Full=gC1q-R protein;
AltName: Full=p33;
Flags: Precursor;
Name=C1QBP; Synonyms=GC1QBP, HABP1, SF2P32;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 74; 76-93 AND
208-216.
TISSUE=Fibroblast;
PubMed=8262387; DOI=10.1016/0378-1119(93)90108-F;
Honore B., Madsen P., Rasmussen H.H., Vandekerckhove J., Celis J.E.,
Leffers H.;
"Cloning and expression of a cDNA covering the complete coding region
of the P32 subunit of human pre-mRNA splicing factor SF2.";
Gene 134:283-287(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR
LOCATION.
PubMed=8195709; DOI=10.1084/jem.179.6.1809;
Ghebrehiwet B., Lim B.L., Peerschke E.I., Willis A.C., Reid K.B.;
"Isolation, cDNA cloning, and overexpression of a 33-kD cell surface
glycoprotein that binds to the globular 'heads' of C1q.";
J. Exp. Med. 179:1809-1821(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11278463; DOI=10.1074/jbc.M009064200;
Tye A.J., Ghebrehiwet B., Guo N., Sastry K.N., Chow B.K.C.,
Peerschke E.I.B., Lim B.L.;
"The human gC1qR/p32 gene, C1qBP. Genomic organization and promoter
analysis.";
J. Biol. Chem. 276:17069-17075(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-282, AND PROTEIN SEQUENCE OF 74-114.
PubMed=1830244; DOI=10.1016/0092-8674(91)90627-B;
Krainer A.R., Mayeda A., Kozak D., Binns G.;
"Functional expression of cloned human splicing factor SF2: homology
to RNA-binding proteins, U1 70K, and Drosophila splicing regulators.";
Cell 66:383-394(1991).
[8]
PROTEIN SEQUENCE OF 74-88, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=8662673; DOI=10.1074/jbc.271.22.13040;
Herwald H., Dedio J., Kellner R., Loos M., Muller-Esterl W.;
"Isolation and characterization of the kininogen-binding protein p33
from endothelial cells. Identity with the gC1q receptor.";
J. Biol. Chem. 271:13040-13047(1996).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 86-282.
PubMed=8567680; DOI=10.1074/jbc.271.4.2206;
Deb T.B., Datta K.;
"Molecular cloning of human fibroblast hyaluronic acid-binding protein
confirms its identity with P-32, a protein co-purified with splicing
factor SF2. Hyaluronic acid-binding protein as P-32 protein, co-
purified with splicing factor SF2.";
J. Biol. Chem. 271:2206-2212(1996).
[10]
INTERACTION WITH VTN.
PubMed=8900153; DOI=10.1074/jbc.271.43.26739;
Lim B.L., Reid K.B., Ghebrehiwet B., Peerschke E.I., Leigh L.A.,
Preissner K.T.;
"The binding protein for globular heads of complement C1q, gC1qR.
Functional expression and characterization as a novel vitronectin
binding factor.";
J. Biol. Chem. 271:26739-26744(1996).
[11]
FUNCTION.
PubMed=8710908; DOI=10.1073/pnas.93.16.8552;
Joseph K., Ghebrehiwet B., Peerschke E.I., Reid K.B., Kaplan A.P.;
"Identification of the zinc-dependent endothelial cell binding protein
for high molecular weight kininogen and factor XII: identity with the
receptor that binds to the globular 'heads' of C1q (gC1q-R).";
Proc. Natl. Acad. Sci. U.S.A. 93:8552-8557(1996).
[12]
SUBCELLULAR LOCATION.
PubMed=9191880; DOI=10.1006/clin.1997.4374;
Peterson K.L., Zhang W., Lu P.D., Keilbaugh S.A., Peerschke E.I.,
Ghebrehiwet B.;
"The C1q-binding cell membrane proteins cC1q-R and gC1q-R are released
from activated cells: subcellular distribution and immunochemical
characterization.";
Clin. Immunol. Immunopathol. 84:17-26(1997).
[13]
SUBCELLULAR LOCATION.
PubMed=9305894; DOI=10.1074/jbc.272.39.24363;
Muta T., Kang D., Kitajima S., Fujiwara T., Hamasaki N.;
"p32 protein, a splicing factor 2-associated protein, is localized in
mitochondrial matrix and is functionally important in maintaining
oxidative phosphorylation.";
J. Biol. Chem. 272:24363-24370(1997).
[14]
INTERACTION WITH CD93, AND SUBCELLULAR LOCATION.
PubMed=9233640;
Ghebrehiwet B., Lu P.D., Zhang W., Keilbaugh S.A., Leigh L.E.,
Eggleton P., Reid K.B., Peerschke E.I.;
"Evidence that the two C1q binding membrane proteins, gC1q-R and cC1q-
R, associate to form a complex.";
J. Immunol. 159:1429-1436(1997).
[15]
FUNCTION.
PubMed=9461517; DOI=10.1042/bj3300247;
Leigh L.E., Ghebrehiwet B., Perera T.P., Bird I.N., Strong P.,
Kishore U., Reid K.B., Eggleton P.;
"C1q-mediated chemotaxis by human neutrophils: involvement of gClqR
and G-protein signalling mechanisms.";
Biochem. J. 330:247-254(1998).
[16]
FUNCTION.
PubMed=10479529; DOI=10.1006/clim.1999.4753;
Joseph K., Ghebrehiwet B., Kaplan A.P.;
"Cytokeratin 1 and gC1qR mediate high molecular weight kininogen
binding to endothelial cells.";
Clin. Immunol. 92:246-255(1999).
[17]
FUNCTION, AND INTERACTION WITH SRSF1 AND SRSF9.
PubMed=10022843; DOI=10.1093/emboj/18.4.1014;
Petersen-Mahrt S.K., Estmer C., Ohrmalm C., Matthews D.A.,
Russell W.C., Akusjarvi G.;
"The splicing factor-associated protein, p32, regulates RNA splicing
by inhibiting ASF/SF2 RNA binding and phosphorylation.";
EMBO J. 18:1014-1024(1999).
[18]
FUNCTION (MICROBIAL INFECTION).
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).
[19]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH STAPHYLOCOCCUS
AUREUS SPA.
PubMed=10722602; DOI=10.1128/IAI.68.4.2061-2068.2000;
Nguyen T., Ghebrehiwet B., Peerschke E.I.;
"Staphylococcus aureus protein A recognizes platelet gC1qR/p33: a
novel mechanism for staphylococcal interactions with platelets.";
Infect. Immun. 68:2061-2068(2000).
[20]
FUNCTION, AND INTERACTION WITH HCV CORE PROTEIN.
PubMed=11086025; DOI=10.1172/JCI10323;
Kittlesen D.J., Chianese-Bullock K.A., Yao Z.Q., Braciale T.J.,
Hahn Y.S.;
"Interaction between complement receptor gC1qR and hepatitis C virus
core protein inhibits T-lymphocyte proliferation.";
J. Clin. Invest. 106:1239-1249(2000).
[21]
INTERACTION WITH RUBELLA VIRUS CAPSID PROTEIN.
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).
[22]
SUBCELLULAR LOCATION.
PubMed=11493647;
van Leeuwen H.C., O'Hare P.;
"Retargeting of the mitochondrial protein p32/gC1Qr to a cytoplasmic
compartment and the cell surface.";
J. Cell Sci. 114:2115-2123(2001).
[23]
FUNCTION.
PubMed=11859136; DOI=10.4049/jimmunol.168.5.2441;
Feng X., Tonnesen M.G., Peerschke E.I., Ghebrehiwet B.;
"Cooperation of C1q receptors and integrins in C1q-mediated
endothelial cell adhesion and spreading.";
J. Immunol. 168:2441-2448(2002).
[24]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH RUBELLA VIRUS
CAPSID PROTEIN.
PubMed=12034482; DOI=10.1016/S0168-1702(02)00030-8;
Mohan K.V., Ghebrehiwet B., Atreya C.D.;
"The N-terminal conserved domain of rubella virus capsid interacts
with the C-terminal region of cellular p32 and overexpression of p32
enhances the viral infectivity.";
Virus Res. 85:151-161(2002).
[25]
FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF GLY-107.
PubMed=12833064; DOI=10.1038/ncb1000;
Zheng Y.H., Yu H.F., Peterlin B.M.;
"Human p32 protein relieves a post-transcriptional block to HIV
replication in murine cells.";
Nat. Cell Biol. 5:611-618(2003).
[26]
ERRATUM.
Zheng Y.H., Yu H.F., Peterlin B.M.;
Nat. Cell Biol. 5:839-839(2003).
[27]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=12574814; DOI=10.1267/THRO03020331;
Peerschke E.I., Murphy T.K., Ghebrehiwet B.;
"Activation-dependent surface expression of gC1qR/p33 on human blood
platelets.";
Thromb. Haemost. 89:331-339(2003).
[28]
INTERACTION WITH HRK, AND SUBCELLULAR LOCATION.
PubMed=15031724; DOI=10.1038/sj.cdd.4401418;
Sunayama J., Ando Y., Itoh N., Tomiyama A., Sakurada K., Sugiyama A.,
Kang D., Tashiro F., Gotoh Y., Kuchino Y., Kitanaka C.;
"Physical and functional interaction between BH3-only protein Hrk and
mitochondrial pore-forming protein p32.";
Cell Death Differ. 11:771-781(2004).
[29]
FUNCTION, AND INTERACTION WITH NFYB.
PubMed=15243141; DOI=10.1093/nar/gkh692;
Chattopadhyay C., Hawke D., Kobayashi R., Maity S.N.;
"Human p32, interacts with B subunit of the CCAAT-binding factor,
CBF/NF-Y, and inhibits CBF-mediated transcription activation in
vitro.";
Nucleic Acids Res. 32:3632-3641(2004).
[30]
FUNCTION, AND INDUCTION.
PubMed=16177118; DOI=10.4049/jimmunol.175.7.4706;
Waggoner S.N., Cruise M.W., Kassel R., Hahn Y.S.;
"gC1q receptor ligation selectively down-regulates human IL-12
production through activation of the phosphoinositide 3-kinase
pathway.";
J. Immunol. 175:4706-4714(2005).
[31]
ERRATUM.
Waggoner S.N., Cruise M.W., Kassel R., Hahn Y.S.;
J. Immunol. 178:3332-3332(2007).
[32]
INTERACTION WITH CDK13.
PubMed=16721827; DOI=10.1002/jcb.20986;
Even Y., Durieux S., Escande M.L., Lozano J.C., Peaucellier G.,
Weil D., Geneviere A.M.;
"CDC2L5, a Cdk-like kinase with RS domain, interacts with the ASF/SF2-
associated protein p32 and affects splicing in vivo.";
J. Cell. Biochem. 99:890-904(2006).
[33]
INTERACTION WITH HIV-1 TAT.
PubMed=16537587; DOI=10.1128/JVI.80.7.3189-3204.2006;
Berro R., Kehn K., de la Fuente C., Pumfery A., Adair R., Wade J.,
Colberg-Poley A.M., Hiscott J., Kashanchi F.;
"Acetylated Tat regulates human immunodeficiency virus type 1 splicing
through its interaction with the splicing regulator p32.";
J. Virol. 80:3189-3204(2006).
[34]
FUNCTION.
PubMed=16140380; DOI=10.1016/j.molimm.2005.07.030;
Vegh Z., Kew R.R., Gruber B.L., Ghebrehiwet B.;
"Chemotaxis of human monocyte-derived dendritic cells to complement
component C1q is mediated by the receptors gC1qR and cC1qR.";
Mol. Immunol. 43:1402-1407(2006).
[35]
FUNCTION.
PubMed=17881511; DOI=10.1189/jlb.0507268;
Waggoner S.N., Hall C.H., Hahn Y.S.;
"HCV core protein interaction with gC1q receptor inhibits Th1
differentiation of CD4+ T cells via suppression of dendritic cell IL-
12 production.";
J. Leukoc. Biol. 82:1407-1419(2007).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[37]
INTERACTION WITH CDKN2A, AND SUBCELLULAR LOCATION.
PubMed=17486078; DOI=10.1038/sj.onc.1210485;
Reef S., Shifman O., Oren M., Kimchi A.;
"The autophagic inducer smARF interacts with and is stabilized by the
mitochondrial p32 protein.";
Oncogene 26:6677-6683(2007).
[38]
FUNCTION, INTERACTION WITH FOXC1, AND SUBCELLULAR LOCATION.
PubMed=18676636; DOI=10.1167/iovs.07-1625;
Huang L., Chi J., Berry F.B., Footz T.K., Sharp M.W., Walter M.A.;
"Human p32 is a novel FOXC1-interacting protein that regulates FOXC1
transcriptional activity in ocular cells.";
Invest. Ophthalmol. Vis. Sci. 49:5243-5249(2008).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[40]
FUNCTION.
PubMed=19004836; DOI=10.1074/jbc.M804246200;
Yadav G., Prasad R.L., Jha B.K., Rai V., Bhakuni V., Datta K.;
"Evidence for inhibitory interaction of hyaluronan-binding protein 1
(HABP1/p32/gC1qR) with Streptococcus pneumoniae hyaluronidase.";
J. Biol. Chem. 284:3897-3905(2009).
[41]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAVS.
PubMed=19164550; DOI=10.1073/pnas.0811029106;
Xu L., Xiao N., Liu F., Ren H., Gu J.;
"Inhibition of RIG-I and MDA5-dependent antiviral response by gC1qR at
mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 106:1530-1535(2009).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[43]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[44]
FUNCTION.
PubMed=20810993; DOI=10.4049/jimmunol.0903215;
Agostinis C., Bulla R., Tripodo C., Gismondi A., Stabile H., Bossi F.,
Guarnotta C., Garlanda C., De Seta F., Spessotto P., Santoni A.,
Ghebrehiwet B., Girardi G., Tedesco F.;
"An alternative role of C1q in cell migration and tissue remodeling:
contribution to trophoblast invasion and placental development.";
J. Immunol. 185:4420-4429(2010).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[46]
INTERACTION WITH PPIF.
PubMed=20950273; DOI=10.1042/BJ20101431;
McGee A.M., Baines C.P.;
"Complement 1q-binding protein inhibits the mitochondrial permeability
transition pore and protects against oxidative stress-induced death.";
Biochem. J. 433:119-125(2011).
[47]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FBL; RRP1; DDX21;
DDX50 AND NCL.
PubMed=21536856; DOI=10.1074/mcp.M110.006148;
Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K.,
Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T.,
Takahashi N.;
"Splicing factor 2-associated protein p32 participates in ribosome
biogenesis by regulating the binding of Nop52 and fibrillarin to
preribosome particles.";
Mol. Cell. Proteomics 10:0-0(2011).
[48]
FUNCTION, AND INTERACTION WITH KRT1.
PubMed=21544310; DOI=10.1160/TH10-09-0591;
Pixley R.A., Espinola R.G., Ghebrehiwet B., Joseph K., Kao A.,
Bdeir K., Cines D.B., Colman R.W.;
"Interaction of high-molecular-weight kininogen with endothelial cell
binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface
plasmon resonance (BiaCore).";
Thromb. Haemost. 105:1053-1059(2011).
[49]
FUNCTION, AND INTERACTION WITH CD209.
PubMed=22700724; DOI=10.1182/blood-2011-07-369728;
Hosszu K.K., Valentino A., Vinayagasundaram U., Vinayagasundaram R.,
Joyce M.G., Ji Y., Peerschke E.I., Ghebrehiwet B.;
"DC-SIGN, C1q, and gC1qR form a trimolecular receptor complex on the
surface of monocyte-derived immature dendritic cells.";
Blood 120:1228-1236(2012).
[50]
INTERACTION WITH RUBELLA VIRUS PROTEASE P150.
PubMed=22238231; DOI=10.1099/vir.0.038901-0;
Suppiah S., Mousa H.A., Tzeng W.P., Matthews J.D., Frey T.K.;
"Binding of cellular p32 protein to the rubella virus P150 replicase
protein via PxxPxR motifs.";
J. Gen. Virol. 93:807-816(2012).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[52]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND THR-214, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[53]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER SER-73, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[54]
FUNCTION, INVOLVEMENT IN COXPD33, AND VARIANTS COXPD33 SER-186;
TYR-188 DEL; LEU-204; TRP-247; PHE-275 AND PRO-275.
PubMed=28942965; DOI=10.1016/j.ajhg.2017.08.015;
Feichtinger R.G., Olahova M., Kishita Y., Garone C., Kremer L.S.,
Yagi M., Uchiumi T., Jourdain A.A., Thompson K., D'Souza A.R.,
Kopajtich R., Alston C.L., Koch J., Sperl W., Mastantuono E.,
Strom T.M., Wortmann S.B., Meitinger T., Pierre G., Chinnery P.F.,
Chrzanowska-Lightowlers Z.M., Lightowlers R.N., DiMauro S.,
Calvo S.E., Mootha V.K., Moggio M., Sciacco M., Comi G.P., Ronchi D.,
Murayama K., Ohtake A., Rebelo-Guiomar P., Kohda M., Kang D.,
Mayr J.A., Taylor R.W., Okazaki Y., Minczuk M., Prokisch H.;
"Biallelic C1QBP mutations cause severe neonatal-, childhood-, or
later-onset cardiomyopathy associated with combined respiratory-chain
deficiencies.";
Am. J. Hum. Genet. 101:525-538(2017).
[55]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
PubMed=10097078; DOI=10.1073/pnas.96.7.3572;
Jiang J., Zhang Y., Krainer A.R., Xu R.-M.;
"Crystal structure of human p32, a doughnut-shaped acidic
mitochondrial matrix protein.";
Proc. Natl. Acad. Sci. U.S.A. 96:3572-3577(1999).
-!- 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 and Staphylococcus aureus protein A.
{ECO:0000269|PubMed:10722602, ECO:0000269|PubMed:10747014}.
-!- FUNCTION: (Microbial infection) Involved in replication of Rubella
virus. {ECO:0000269|PubMed:12034482}.
-!- 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 U2AF1L4.
{ECO:0000250|UniProtKB:O35658, ECO:0000269|PubMed:10022843,
ECO:0000269|PubMed:11086025, ECO:0000269|PubMed:15031724,
ECO:0000269|PubMed:15243141, 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:22700724, ECO:0000269|PubMed:8900153,
ECO:0000269|PubMed:9233640}.
-!- SUBUNIT: (Microbial infection) Interacts with Rubella virus capsid
protein; the interaction occurs in mitochondria. Interacts with
Rubella virus protease p150. {ECO:0000269|PubMed:10823864,
ECO:0000269|PubMed:12034482, ECO:0000269|PubMed:22238231}.
-!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus
aureus protein A/spa. {ECO:0000269|PubMed:10722602}.
-!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus
aureus protein A/spa, HIV-1 Tat and HCV core protein.
{ECO:0000269|PubMed:10722602}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat and HCV
core protein. {ECO:0000269|PubMed:16537587}.
-!- INTERACTION:
P27958:- (xeno); NbExp=4; IntAct=EBI-347528, EBI-6377335;
P02745:C1QA; NbExp=5; IntAct=EBI-14032968, EBI-1220209;
P02746:C1QB; NbExp=4; IntAct=EBI-14032968, EBI-2813376;
P02747:C1QC; NbExp=4; IntAct=EBI-14032968, EBI-1220222;
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;
Q05513:PRKCZ; NbExp=2; IntAct=EBI-347528, EBI-295351;
Q15139:PRKD1; NbExp=9; IntAct=EBI-347528, EBI-1181072;
P04004:VTN; NbExp=8; IntAct=EBI-347528, EBI-1036653;
P67809:YBX1; NbExp=6; IntAct=EBI-347528, EBI-354065;
-!- 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}. Cell membrane
{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}. Nucleus, nucleolus
{ECO:0000269|PubMed:21536856}. Note=Seems to be predominantly
localized to mitochondria. Secreted by activated lymphocytes.
-!- 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}.
-!- INDUCTION: Enhanced cell surface expression upon platelet and
monocyte activation. {ECO:0000269|PubMed:12574814,
ECO:0000269|PubMed:16177118}.
-!- DISEASE: Combined oxidative phosphorylation deficiency 33
(COXPD33) [MIM:617713]: An autosomal recessive disorder caused by
multiple mitochondrial respiratory chain defects and impaired
mitochondrial energy metabolism. Clinical manifestations are
highly variable. Affected infants present with cardiomyopathy
accompanied by multisystemic features involving liver, kidney, and
brain. Death in infancy is observed in some patients. Children and
adults present with myopathy and progressive external
ophthalmoplegia. {ECO:0000269|PubMed:28942965}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the MAM33 family. {ECO:0000305}.
-!- 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 mitochondrial form.
{ECO:0000305|PubMed:11493647, ECO:0000305|PubMed:9305894}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/c1qbp/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L04636; AAA16315.1; -; mRNA.
EMBL; X75913; CAA53512.1; -; mRNA.
EMBL; AF338439; AAK26580.1; -; Genomic_DNA.
EMBL; BT019898; AAV38701.1; -; mRNA.
EMBL; BT019899; AAV38702.1; -; mRNA.
EMBL; DQ372108; ABC79624.1; -; Genomic_DNA.
EMBL; BC000435; AAH00435.1; -; mRNA.
EMBL; BC013731; AAH13731.1; -; mRNA.
EMBL; M69039; AAA73055.1; -; mRNA.
EMBL; AF275902; AAF78763.1; -; mRNA.
CCDS; CCDS11071.1; -.
PIR; JT0762; JT0762.
RefSeq; NP_001203.1; NM_001212.3.
UniGene; Hs.555866; -.
PDB; 1P32; X-ray; 2.25 A; A/B/C=74-282.
PDB; 3RPX; X-ray; 2.65 A; A/B/C=96-282.
PDBsum; 1P32; -.
PDBsum; 3RPX; -.
ProteinModelPortal; Q07021; -.
SMR; Q07021; -.
BioGrid; 107169; 329.
CORUM; Q07021; -.
DIP; DIP-31164N; -.
IntAct; Q07021; 95.
MINT; Q07021; -.
STRING; 9606.ENSP00000225698; -.
DrugBank; DB08818; Hyaluronic acid.
TCDB; 9.B.103.1.1; the putative ca(2+) uniporter (gc1qr) family.
iPTMnet; Q07021; -.
PhosphoSitePlus; Q07021; -.
SwissPalm; Q07021; -.
BioMuta; C1QBP; -.
DMDM; 730772; -.
DOSAC-COBS-2DPAGE; Q07021; -.
OGP; Q07021; -.
EPD; Q07021; -.
MaxQB; Q07021; -.
PaxDb; Q07021; -.
PeptideAtlas; Q07021; -.
PRIDE; Q07021; -.
ProteomicsDB; 58500; -.
TopDownProteomics; Q07021; -.
DNASU; 708; -.
Ensembl; ENST00000225698; ENSP00000225698; ENSG00000108561.
GeneID; 708; -.
KEGG; hsa:708; -.
UCSC; uc002gby.2; human.
CTD; 708; -.
DisGeNET; 708; -.
EuPathDB; HostDB:ENSG00000108561.8; -.
GeneCards; C1QBP; -.
HGNC; HGNC:1243; C1QBP.
HPA; HPA026483; -.
MalaCards; C1QBP; -.
MIM; 601269; gene.
MIM; 617713; phenotype.
neXtProt; NX_Q07021; -.
OpenTargets; ENSG00000108561; -.
PharmGKB; PA25624; -.
eggNOG; KOG4024; Eukaryota.
eggNOG; ENOG4111G4Z; LUCA.
GeneTree; ENSGT00390000018406; -.
HOGENOM; HOG000046272; -.
HOVERGEN; HBG000914; -.
InParanoid; Q07021; -.
KO; K15414; -.
OMA; ATHYEHS; -.
OrthoDB; EOG091G0IZD; -.
PhylomeDB; Q07021; -.
TreeFam; TF315160; -.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
SIGNOR; Q07021; -.
ChiTaRS; C1QBP; human.
EvolutionaryTrace; Q07021; -.
GeneWiki; C1QBP; -.
GenomeRNAi; 708; -.
PMAP-CutDB; Q07021; -.
PRO; PR:Q07021; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108561; Expressed in 222 organ(s), highest expression level in frontal cortex.
CleanEx; HS_C1QBP; -.
ExpressionAtlas; Q07021; baseline and differential.
Genevisible; Q07021; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0031690; F:adrenergic receptor binding; ISS:UniProtKB.
GO; GO:0001849; F:complement component C1q binding; IDA:UniProtKB.
GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
GO; GO:0030984; F:kininogen binding; IDA:UniProtKB.
GO; GO:0097177; F:mitochondrial ribosome binding; ISS:UniProtKB.
GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0042256; P:mature ribosome assembly; IMP:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:UniProtKB.
GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; IDA:UniProtKB.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB.
GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
GO; GO:1901165; P:positive regulation of trophoblast cell migration; IMP:UniProtKB.
GO; GO:0030449; P:regulation of complement activation; IDA: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;
3D-structure; Acetylation; Adaptive immunity; Apoptosis;
Cell membrane; Complement pathway; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Host-virus interaction;
Immunity; Innate immunity; Membrane; Mitochondrion; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Primary mitochondrial disease;
Reference proteome; Ribosome biogenesis; Secreted; Transcription;
Transcription regulation; Transit peptide.
TRANSIT 1 73 Mitochondrion.
{ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:1830244,
ECO:0000269|PubMed:8662673}.
CHAIN 74 282 Complement component 1 Q subcomponent-
binding protein, mitochondrial.
/FTId=PRO_0000018590.
REGION 76 93 C1q binding.
REGION 168 213 Interaction with MAVS.
{ECO:0000269|PubMed:19164550}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 91 91 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 188 188 Phosphotyrosine.
{ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:19690332}.
MOD_RES 201 201 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 214 214 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
VARIANT 186 186 C -> S (in COXPD33; unknown pathological
significance; dbSNP:rs748497469).
{ECO:0000269|PubMed:28942965}.
/FTId=VAR_080391.
VARIANT 188 188 Missing (in COXPD33; unknown pathological
significance).
{ECO:0000269|PubMed:28942965}.
/FTId=VAR_080392.
VARIANT 204 204 F -> L (in COXPD33; unknown pathological
significance; dbSNP:rs767427194).
{ECO:0000269|PubMed:28942965}.
/FTId=VAR_080393.
VARIANT 247 247 G -> W (in COXPD33).
{ECO:0000269|PubMed:28942965}.
/FTId=VAR_080394.
VARIANT 275 275 L -> F (in COXPD33; unknown pathological
significance).
{ECO:0000269|PubMed:28942965}.
/FTId=VAR_080395.
VARIANT 275 275 L -> P (in COXPD33).
{ECO:0000269|PubMed:28942965}.
/FTId=VAR_080396.
MUTAGEN 107 107 G->D: Impairs HIV RNA splicing in mouse
cells. {ECO:0000269|PubMed:12833064}.
HELIX 77 96 {ECO:0000244|PDB:1P32}.
TURN 106 108 {ECO:0000244|PDB:3RPX}.
STRAND 110 114 {ECO:0000244|PDB:1P32}.
STRAND 117 124 {ECO:0000244|PDB:1P32}.
STRAND 127 134 {ECO:0000244|PDB:1P32}.
STRAND 168 174 {ECO:0000244|PDB:1P32}.
HELIX 175 177 {ECO:0000244|PDB:1P32}.
STRAND 180 187 {ECO:0000244|PDB:1P32}.
STRAND 205 213 {ECO:0000244|PDB:1P32}.
STRAND 225 228 {ECO:0000244|PDB:1P32}.
HELIX 233 244 {ECO:0000244|PDB:1P32}.
TURN 245 247 {ECO:0000244|PDB:1P32}.
HELIX 250 280 {ECO:0000244|PDB:1P32}.
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


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