MCM7_MOUSE
ID MCM7_MOUSE Reviewed; 719 AA.
AC Q61881;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=DNA replication licensing factor MCM7;
DE EC=3.6.4.12;
DE AltName: Full=CDC47 homolog;
GN Name=Mcm7; Synonyms=Cdc47, Mcmd7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=8566808; DOI=10.1016/0378-1119(95)00713-x;
RA Takizawa N., Kimura H., Sugimoto K.;
RT "Sequence of mouse CDC47, a member of the minichromosome maintenance (Mcm)
RT family involved in the DNA replication licensing system.";
RL Gene 167:343-344(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION IN THE MCM2-7 COMPLEX.
RX PubMed=10567526; DOI=10.1128/mcb.19.12.8003;
RA You Z., Komamura Y., Ishimi Y.;
RT "Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase
RT activity.";
RL Mol. Cell. Biol. 19:8003-8015(1999).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE MCM2-7 COMPLEX, MUTAGENESIS OF
RP 387-LYS-SER-388 AND 445-ASP-GLU-446, AND CATALYTIC ACTIVITY.
RX PubMed=12207017; DOI=10.1074/jbc.m205769200;
RA You Z., Ishimi Y., Masai H., Hanaoka F.;
RT "Roles of Mcm7 and Mcm4 subunits in the DNA helicase activity of the mouse
RT Mcm4/6/7 complex.";
RL J. Biol. Chem. 277:42471-42479(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC is the putative replicative helicase essential for 'once per cell
CC cycle' DNA replication initiation and elongation in eukaryotic cells.
CC The active ATPase sites in the MCM2-7 ring are formed through the
CC interaction surfaces of two neighboring subunits such that a critical
CC structure of a conserved arginine finger motif is provided in trans
CC relative to the ATP-binding site of the Walker A box of the adjacent
CC subunit. The six ATPase active sites, however, are likely to contribute
CC differentially to the complex helicase activity. Uncomplexed form does
CC not show ATPase or DNA helicase (PubMed:12207017). Required for S-phase
CC checkpoint activation upon UV-induced damage.
CC {ECO:0000250|UniProtKB:P33993, ECO:0000269|PubMed:12207017}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:12207017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:12207017};
CC -!- SUBUNIT: Component of the MCM2-7 complex. The complex forms a toroidal
CC hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-
CC MCM3-MCM5. Interacts with the ATR-ATRIP complex and with RAD17.
CC Interacts with TIPIN. Interacts with MCMBP. Interacts with ANKRD17.
CC Component of the replisome complex composed of at least DONSON, MCM2,
CC MCM7, PCNA and TICRR (By similarity). Component of the CMG helicase
CC complex, composed of the MCM2-7 complex, the GINS complex and CDC45 (By
CC similarity). {ECO:0000250|UniProtKB:P33993,
CC ECO:0000250|UniProtKB:Q91876}.
CC -!- INTERACTION:
CC Q61881; P46414: Cdkn1b; NbExp=2; IntAct=EBI-457180, EBI-1005742;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91876}.
CC Chromosome {ECO:0000250|UniProtKB:Q91876}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250|UniProtKB:Q91876}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250|UniProtKB:P33993}.
CC -!- PTM: Ubiquitinated by traip when forks converge following formation of
CC DNA interstrand cross-links. Short ubiquitin chains on MCM7 promote
CC recruitment of DNA glycosylase NEIL3. If the interstrand cross-link
CC cannot be cleaved by NEIL3, the ubiquitin chains continue to grow on
CC MCM7, promoting the unloading of the CMG helicase complex by the
CC VCP/p97 ATPase. {ECO:0000250|UniProtKB:Q91876}.
CC -!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins yielded a
CC variety of dimeric, trimeric and tetrameric complexes with unclear
CC biological significance. Specifically a MCM467 subcomplex is shown to
CC have in vitro helicase activity which is inhibited by the MCM2 subunit.
CC The MCM2-7 hexamer is the proposed physiological active complex.
CC {ECO:0000269|PubMed:10567526}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; D26091; BAA05084.1; -; mRNA.
DR EMBL; BC065164; AAH65164.1; -; mRNA.
DR EMBL; BC066024; AAH66024.1; -; mRNA.
DR CCDS; CCDS19793.1; -.
DR PIR; JC4580; JC4580.
DR RefSeq; NP_032594.1; NM_008568.2.
DR AlphaFoldDB; Q61881; -.
DR SMR; Q61881; -.
DR BioGRID; 201350; 27.
DR ComplexPortal; CPX-2941; MCM complex.
DR CORUM; Q61881; -.
DR DIP; DIP-45877N; -.
DR IntAct; Q61881; 3.
DR MINT; Q61881; -.
DR STRING; 10090.ENSMUSP00000000505; -.
DR iPTMnet; Q61881; -.
DR PhosphoSitePlus; Q61881; -.
DR SwissPalm; Q61881; -.
DR EPD; Q61881; -.
DR MaxQB; Q61881; -.
DR PaxDb; Q61881; -.
DR PRIDE; Q61881; -.
DR ProteomicsDB; 295841; -.
DR Antibodypedia; 1289; 1186 antibodies from 45 providers.
DR DNASU; 17220; -.
DR Ensembl; ENSMUST00000000505; ENSMUSP00000000505; ENSMUSG00000029730.
DR GeneID; 17220; -.
DR KEGG; mmu:17220; -.
DR UCSC; uc009aeu.1; mouse.
DR CTD; 4176; -.
DR MGI; MGI:1298398; Mcm7.
DR VEuPathDB; HostDB:ENSMUSG00000029730; -.
DR eggNOG; KOG0482; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; Q61881; -.
DR OMA; NAYTCDR; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q61881; -.
DR TreeFam; TF300400; -.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR Reactome; R-MMU-69052; Switching of origins to a post-replicative state.
DR BioGRID-ORCS; 17220; 26 hits in 74 CRISPR screens.
DR ChiTaRS; Mcm7; mouse.
DR PRO; PR:Q61881; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q61881; protein.
DR Bgee; ENSMUSG00000029730; Expressed in ventricular zone and 126 other tissues.
DR ExpressionAtlas; Q61881; baseline and differential.
DR Genevisible; Q61881; MM.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042555; C:MCM complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IDA:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IPI:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IPI:MGI.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
DR GO; GO:0042325; P:regulation of phosphorylation; ISO:MGI.
DR CDD; cd17758; MCM7; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008050; MCM7.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; PTHR11630; 1.
DR PANTHER; PTHR11630:SF26; PTHR11630:SF26; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01663; MCMPROTEIN7.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell cycle; Chromosome; DNA replication;
KW DNA-binding; Glycoprotein; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT CHAIN 2..719
FT /note="DNA replication licensing factor MCM7"
FT /id="PRO_0000194120"
FT DOMAIN 332..538
FT /note="MCM"
FT REGION 521..564
FT /note="Interaction with RAD17"
FT /evidence="ECO:0000250"
FT REGION 577..719
FT /note="Interaction with ATRIP"
FT /evidence="ECO:0000250"
FT MOTIF 513..516
FT /note="Arginine finger"
FT BINDING 381..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT MUTAGEN 387..388
FT /note="KS->AA: Almost abolishes MCM complex DNA helicase
FT activity. Strongly decreases MCM complex ATPase activity.
FT No effect on MCM complex formation. No effect on ATP and
FT ssDNA binding."
FT /evidence="ECO:0000269|PubMed:12207017"
FT MUTAGEN 445..446
FT /note="DE->AA: Strongly decreases MCM complex ATPase and
FT DNA helicase activities. No effect on MCM complex
FT formation. No effect on ATP and ssDNA binding."
FT /evidence="ECO:0000269|PubMed:12207017"
SQ SEQUENCE 719 AA; 81211 MW; 019AE8E04BB8EB3C CRC64;
MALKDYAIEK EKVKKFLQEF YYENELGKKQ FKYGTQLVHL AHREQVALYV DLDDIAEDDP
ELVDSICENA KRYSRLFGDV VQELLPEYKE KEVVNKDVLD VYIEHRLMME QRSRDPGAVR
NPQNQYPSEL MRRFELYFRG PSSSKPRVIR EVRADSVGKL LTVRGIVTRV SEVKPRMVVA
TYTCDQCGAE TYQPIQSPTF MPLIMCPSQE CQTNRSGGRL YLQTRGSKFV KFQEMKIQEH
SDQVPVGNIP RSITVVLEGE NTRIAQPGDH VSVTGIFLPV LRTGFQQMAQ GLLSETYLEA
HWIVKMTKSD DDVSGAGELS SEELKQIAEE DFYEKLAASI APEIYGHEDV KKALLLLLVG
GVDQSPQGMK IRGNIHICLM GDPGVAKSQL LSYIDRLAPR SQYTTGRGSS GVGLTAAVLR
DSVSGELTLE GGALVLADQG VCCIDEFDKM AEADRTAIHE VMEQQTISIA KAGILTTLNA
RCSILAAANP AYGRYNPRRS LEQNVQLPAA LLSRFDLLWL IQDRPDRDND LRLAQHITYV
HQHSRQPPAQ FEPLDMKLMR RYIAMCHERQ PTVPESLADY ITAAYVEMRR EARASKDATY
TSARTLLAIL RLSTALARLR MVDIVEKEDV NEAIRLMEMS KDSLLGEKGQ TARTQRPADV
IFATIRELVS RGRSVHFSEA EQRCISRGFT PAQFQAALDE YEELNVWQVN TSRTRITFV
