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   24-JAN-2024, entry version 194.
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,
RC   Spleen, 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).
RN   [6]
RP   UBIQUITINATION.
RX   PubMed=33590678; DOI=10.15252/embr.202052164;
RA   Villa F., Fujisawa R., Ainsworth J., Nishimura K., Lie-A-Ling M.,
RA   Lacaud G., Labib K.P.;
RT   "CUL2LRR1, TRAIP and p97 control CMG helicase disassembly in the mammalian
RT   cell cycle.";
RL   EMBO Rep. 22:e52164-e52164(2021).
CC   -!- FUNCTION: Acts as a component of the MCM2-7 complex (MCM complex) which
CC       is the replicative helicase essential for 'once per cell cycle' DNA
CC       replication initiation and elongation in eukaryotic cells. Core
CC       component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that
CC       unwinds template DNA during replication, and around which the replisome
CC       is built. The active ATPase sites in the MCM2-7 ring are formed through
CC       the interaction surfaces of two neighboring subunits such that a
CC       critical structure of a conserved arginine finger motif is provided in
CC       trans relative to the ATP-binding site of the Walker A box of the
CC       adjacent subunit. The six ATPase active sites, however, are likely to
CC       contribute differentially to the complex helicase activity (By
CC       similarity). Uncomplexed form does not show ATPase or DNA helicase
CC       (PubMed:12207017). Required for S-phase checkpoint activation upon UV-
CC       induced damage (By similarity). {ECO:0000250|UniProtKB:P33993,
CC       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. Component of the CMG helicase complex, a hexameric ring of
CC       related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS
CC       complex. Interacts with the ATR-ATRIP complex and with RAD17. Interacts
CC       with TIPIN. Interacts with MCMBP. Interacts with ANKRD17. Component of
CC       the replisome complex composed of at least DONSON, MCM2, MCM7, PCNA and
CC       TICRR. {ECO:0000250|UniProtKB:P33993, 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 ECS(LRR1) E3 ubiquitin-protein ligase complex
CC       when forks converge following formation of DNA interstrand cross-links
CC       (PubMed:33590678). During mitosis, ubiquitinated by TRAIP when forks
CC       converge following formation of DNA interstrand cross-links
CC       (PubMed:33590678). Short ubiquitin chains on MCM7 promote recruitment
CC       of DNA glycosylase NEIL3 (By similarity). 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 (PubMed:33590678). {ECO:0000250|UniProtKB:Q91876,
CC       ECO:0000269|PubMed:33590678}.
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; 28.
DR   ComplexPortal; CPX-2941; MCM complex.
DR   CORUM; Q61881; -.
DR   DIP; DIP-45877N; -.
DR   IntAct; Q61881; 4.
DR   MINT; Q61881; -.
DR   STRING; 10090.ENSMUSP00000000505; -.
DR   GlyGen; Q61881; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q61881; -.
DR   PhosphoSitePlus; Q61881; -.
DR   SwissPalm; Q61881; -.
DR   EPD; Q61881; -.
DR   MaxQB; Q61881; -.
DR   PaxDb; 10090-ENSMUSP00000000505; -.
DR   ProteomicsDB; 295841; -.
DR   Pumba; Q61881; -.
DR   Antibodypedia; 1289; 1283 antibodies from 45 providers.
DR   DNASU; 17220; -.
DR   Ensembl; ENSMUST00000000505.16; ENSMUSP00000000505.10; ENSMUSG00000029730.17.
DR   GeneID; 17220; -.
DR   KEGG; mmu:17220; -.
DR   UCSC; uc009aeu.1; mouse.
DR   AGR; MGI:1298398; -.
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; AQHVTYV; -.
DR   OrthoDB; 5476523at2759; -.
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; 27 hits in 78 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 129 other cell types or tissues.
DR   ExpressionAtlas; Q61881; baseline and differential.
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:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:Ensembl.
DR   GO; GO:0003697; F:single-stranded DNA binding; IPI:MGI.
DR   GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR   GO; GO:0006974; P:DNA damage response; ISO: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:0006279; P:premeiotic DNA replication; NAS:ComplexPortal.
DR   GO; GO:0042325; P:regulation of phosphorylation; ISO:MGI.
DR   CDD; cd17758; MCM7; 1.
DR   Gene3D; 2.20.28.10; -; 1.
DR   Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR   PANTHER; PTHR11630:SF26; DNA REPLICATION LICENSING FACTOR MCM7; 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; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00847; MCM_1; 1.
DR   PROSITE; PS50051; MCM_2; 1.
DR   Genevisible; Q61881; MM.
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         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared with MCM3"
FT                   /evidence="ECO:0000250|UniProtKB:P33993"
FT   BINDING         384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared with MCM3"
FT                   /evidence="ECO:0000250|UniProtKB:P33993"
FT   BINDING         386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared with MCM3"
FT                   /evidence="ECO:0000250|UniProtKB:P33993"
FT   BINDING         387
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared with MCM3"
FT                   /evidence="ECO:0000250|UniProtKB:P33993"
FT   BINDING         388
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared with MCM3"
FT                   /evidence="ECO:0000250|UniProtKB:P33993"
FT   BINDING         489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /ligand_note="ligand shared with MCM3"
FT                   /evidence="ECO:0000250|UniProtKB:P33993"
FT   BINDING         514
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with MCM4"
FT                   /evidence="ECO:0000250|UniProtKB:P33993"
FT   BINDING         604
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /ligand_note="ligand shared with MCM4"
FT                   /evidence="ECO:0000250|UniProtKB:P33993"
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
//