MCM3_MOUSE
ID MCM3_MOUSE Reviewed; 812 AA.
AC P25206; Q61492;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=DNA replication licensing factor MCM3;
DE EC=3.6.4.12;
DE AltName: Full=DNA polymerase alpha holoenzyme-associated protein P1 {ECO:0000303|PubMed:7925275};
DE AltName: Full=P1-MCM3 {ECO:0000303|PubMed:7925275};
GN Name=Mcm3; Synonyms=Mcmd, Mcmd3;
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-812.
RX PubMed=1549468; DOI=10.1093/nar/20.5.1069;
RA Thoemmes P., Fett R., Schray B., Burkhart R., Barnes M., Kennedy C.,
RA Brown N.C., Knippers R.;
RT "Properties of the nuclear P1 protein, a mammalian homologue of the yeast
RT Mcm3 replication protein.";
RL Nucleic Acids Res. 20:1069-1074(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26, AND INTERACTION WITH DNA
RP POLYMERASE ALPHA.
RX PubMed=7925275; DOI=10.1002/j.1460-2075.1994.tb06751.x;
RA Kimura H., Nozaki N., Sugimoto K.;
RT "DNA polymerase alpha associated protein P1, a murine homolog of yeast
RT MCM3, changes its intranuclear distribution during the DNA synthetic
RT period.";
RL EMBO J. 13:4311-4320(1994).
RN [4]
RP INTERACTION WITH MCM3AP.
RX PubMed=10733502;
RA Kuwahara K., Yoshida M., Kondo E., Sakata A., Watanabe Y., Abe E.,
RA Kouno Y., Tomiyasu S., Fujimura S., Tokuhisa T., Kimura H., Ezaki T.,
RA Sakaguchi N.;
RT "A novel nuclear phosphoprotein, GANP, is up-regulated in centrocytes of
RT the germinal center and associated with MCM3, a protein essential for DNA
RT replication.";
RL Blood 95:2321-2328(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668 AND SER-672, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-668; SER-672;
RP SER-708; THR-719; THR-729; SER-732 AND SER-738, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-293 AND LYS-547, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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. Required for DNA
CC replication and cell proliferation. {ECO:0000250|UniProtKB:P49739}.
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 -!- SUBUNIT: Component of the MCM2-7 complex (By similarity). The complex
CC forms a toroidal hexameric ring with the proposed subunit order MCM2-
CC MCM6-MCM4-MCM7-MCM3-MCM5 (By similarity). Associated with the
CC replication-specific DNA polymerase alpha (PubMed:7925275). Interacts
CC with MCMBP (By similarity). Interacts with ANKRD17 (By similarity).
CC Interacts with MCM3AP; this interaction leads to MCM3 acetylation
CC (PubMed:10733502). Component of the CMG helicase complex, composed of
CC the MCM2-7 complex, the GINS complex and CDC45 (By similarity).
CC {ECO:0000250|UniProtKB:P25205, ECO:0000250|UniProtKB:P49739,
CC ECO:0000269|PubMed:10733502, ECO:0000269|PubMed:7925275}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49739}.
CC Chromosome {ECO:0000250|UniProtKB:P49739}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250|UniProtKB:P49739}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250|UniProtKB:P25205}.
CC -!- PTM: Acetylated by MCM3AP. {ECO:0000269|PubMed:10733502}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; BC031700; AAH31700.1; -; mRNA.
DR EMBL; X62154; CAA44079.1; -; mRNA.
DR EMBL; D26088; BAA05081.1; -; Genomic_DNA.
DR CCDS; CCDS14843.1; -.
DR PIR; S22804; S22804.
DR PIR; S51615; S51615.
DR RefSeq; NP_032589.1; NM_008563.2.
DR AlphaFoldDB; P25206; -.
DR SMR; P25206; -.
DR BioGRID; 201345; 44.
DR ComplexPortal; CPX-2941; MCM complex.
DR CORUM; P25206; -.
DR DIP; DIP-45878N; -.
DR ELM; P25206; -.
DR IntAct; P25206; 30.
DR STRING; 10090.ENSMUSP00000059192; -.
DR iPTMnet; P25206; -.
DR PhosphoSitePlus; P25206; -.
DR SwissPalm; P25206; -.
DR EPD; P25206; -.
DR jPOST; P25206; -.
DR PaxDb; P25206; -.
DR PeptideAtlas; P25206; -.
DR PRIDE; P25206; -.
DR ProteomicsDB; 295981; -.
DR Antibodypedia; 1433; 520 antibodies from 40 providers.
DR DNASU; 17215; -.
DR Ensembl; ENSMUST00000053266; ENSMUSP00000059192; ENSMUSG00000041859.
DR GeneID; 17215; -.
DR KEGG; mmu:17215; -.
DR UCSC; uc007alc.1; mouse.
DR CTD; 4172; -.
DR MGI; MGI:101845; Mcm3.
DR VEuPathDB; HostDB:ENSMUSG00000041859; -.
DR eggNOG; KOG0479; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_6_0_1; -.
DR InParanoid; P25206; -.
DR OMA; NVYPQED; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; P25206; -.
DR TreeFam; TF106459; -.
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; 17215; 27 hits in 77 CRISPR screens.
DR ChiTaRS; Mcm3; mouse.
DR PRO; PR:P25206; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P25206; protein.
DR Bgee; ENSMUSG00000041859; Expressed in somite and 238 other tissues.
DR ExpressionAtlas; P25206; baseline and differential.
DR Genevisible; P25206; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO: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; IEA:UniProtKB-EC.
DR GO; GO:0003697; F:single-stranded DNA binding; 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; ISO:MGI.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
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; IPR008046; Mcm3.
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 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; PR01659; MCMPROTEIN3.
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; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT CHAIN 2..812
FT /note="DNA replication licensing factor MCM3"
FT /id="PRO_0000194094"
FT DOMAIN 295..502
FT /note="MCM"
FT REGION 664..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 477..480
FT /note="Arginine finger"
FT COMPBIAS 682..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 345..352
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:P25205"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 293
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 547
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 705
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 719
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 722
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 729
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 18..22
FT /note="DYLDF -> RLLGL (in Ref. 2; CAA44079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 812 AA; 91546 MW; 3C8653CF13D0F140 CRC64;
MAGTVVLDDV ELREAQRDYL DFLDDEEDQG IYQNKVRELI SDNQYRLIVS VNDLRRKNEK
RANRLLNNAF EELVAFQRAL KDFVASIDAT YAKQYEEFYI GLEGSFGSKH VSPRTLTSCF
LSCVVCVEGI VTKCSLVRPK VVRSVHYCPA TKKTIERRYS DLTTLVAFPS SSVYPTKDEE
NNPLETEYGL SVYKDHQTIT IQEMPEKAPA GQLPRSVDVI LDDDLVDKVK PGDRIQVVGT
YRCLPGKKGC YTSGTFRTVL IACNVKQMSK DIQPAFSADD IAKIKKFSKT RSKDVFEQLA
RSLAPSIHGH DYVKKAILCL LLGGVERELE NGSHIRGDIN ILLIGDPSVA KSQLLRYVLC
TAPRAIPTTG RGSSGVGLTA AVTTDQETGE RRLEAGAMVL ADRGVVCIDE FDKMSDMDRT
AIHEVMEQGR VTIAKAGIHA RLNARCSVLA AANPVYGRYD QYKTPMENIG LQDSLLSRFD
LLFIMLDQMD PEQDREISDH VLRMHQYRAP GEQDGDALPL GSSVDILATD DPDFTQDDQQ
DTRIYEKHDS LLHGTKKKKE KMVSAAFMKK YIHVAKIIKP TLTQESAAYI AEEYSRLRSQ
DSMSSDTART SPVTARTLET LIRLATAHAK ARMSKTVDLQ DAEEAVELVQ YAYFKKVLEK
EKKRKKASED ESDLEDEEEK SQEDTEQKRK RRKTHAKDGE SYDPYDFSEA ETQMPQVHTP
KTDDSQEKTD DSQETQDSQK VELSEPRLKA FKAALLEVFQ EAHEQSVGML HLTESINRNR
EEPFSSEEIQ ACLSRMQDDN QVMVSEGIVF LI
