MCM3_ARATH
ID MCM3_ARATH Reviewed; 776 AA.
AC Q9FL33; O65400;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=DNA replication licensing factor MCM3;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance protein 3;
DE Short=AtMCM3;
GN Name=MCM3; OrderedLocusNames=At5g46280; ORFNames=MPL12.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Dodeman V.L., Phan T., Sabelli P., Bergounioux C.;
RT "Expression analysis of Arabidopsis thaliana MCM3 homolog during the cell
RT cycle.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12089153; DOI=10.1074/jbc.m205125200;
RA Stevens R., Mariconti L., Rossignol P., Perennes C., Cella R.,
RA Bergounioux C.;
RT "Two E2F sites in the Arabidopsis MCM3 promoter have different roles in
RT cell cycle activation and meristematic expression.";
RL J. Biol. Chem. 277:32978-32984(2002).
RN [5]
RP GENE FAMILY.
RX PubMed=17556508; DOI=10.1104/pp.107.101105;
RA Shultz R.W., Tatineni V.M., Hanley-Bowdoin L., Thompson W.F.;
RT "Genome-wide analysis of the core DNA replication machinery in the higher
RT plants Arabidopsis and rice.";
RL Plant Physiol. 144:1697-1714(2007).
RN [6]
RP SUBUNIT, AND INTERACTION WITH ETG1.
RX PubMed=18528439; DOI=10.1038/emboj.2008.107;
RA Takahashi N., Lammens T., Boudolf V., Maes S., Yoshizumi T., De Jaeger G.,
RA Witters E., Inze D., De Veylder L.;
RT "The DNA replication checkpoint aids survival of plants deficient in the
RT novel replisome factor ETG1.";
RL EMBO J. 27:1840-1851(2008).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=19357199; DOI=10.1104/pp.109.136614;
RA Shultz R.W., Lee T.J., Allen G.C., Thompson W.F., Hanley-Bowdoin L.;
RT "Dynamic localization of the DNA replication proteins MCM5 and MCM7 in
RT plants.";
RL Plant Physiol. 150:658-669(2009).
CC -!- FUNCTION: Probable component of the MCM2-7 complex (MCM complex) that
CC may function as a DNA helicase and which is essential to undergo a
CC single round of replication initiation and elongation per cell cycle in
CC eukaryotic cells. {ECO:0000269|PubMed:12089153}.
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 minichromosome maintenance (MCM) complex, a
CC heterotetramer composed of MCM2, MCM3, MCM4, MCM5, MCM6 and MCM7.
CC Interacts with ETG1. {ECO:0000269|PubMed:18528439}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in root meristem, shoot apex and flower
CC buds. {ECO:0000269|PubMed:12089153, ECO:0000269|PubMed:19357199}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; AJ000058; CAA03887.1; -; mRNA.
DR EMBL; AB010698; BAB11083.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95362.1; -; Genomic_DNA.
DR PIR; T52118; T52118.
DR RefSeq; NP_199440.1; NM_123997.3.
DR AlphaFoldDB; Q9FL33; -.
DR SMR; Q9FL33; -.
DR BioGRID; 19919; 13.
DR IntAct; Q9FL33; 1.
DR MINT; Q9FL33; -.
DR STRING; 3702.AT5G46280.1; -.
DR iPTMnet; Q9FL33; -.
DR PaxDb; Q9FL33; -.
DR PRIDE; Q9FL33; -.
DR ProteomicsDB; 238240; -.
DR EnsemblPlants; AT5G46280.1; AT5G46280.1; AT5G46280.
DR GeneID; 834670; -.
DR Gramene; AT5G46280.1; AT5G46280.1; AT5G46280.
DR KEGG; ath:AT5G46280; -.
DR Araport; AT5G46280; -.
DR TAIR; locus:2170418; AT5G46280.
DR eggNOG; KOG0479; Eukaryota.
DR HOGENOM; CLU_000995_6_0_1; -.
DR InParanoid; Q9FL33; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q9FL33; -.
DR BRENDA; 3.6.4.12; 399.
DR PRO; PR:Q9FL33; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FL33; baseline and differential.
DR Genevisible; Q9FL33; AT.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000347; C:THO complex; IDA:UniProtKB.
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; TAS:TAIR.
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 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 ATP-binding; Cell cycle; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..776
FT /note="DNA replication licensing factor MCM3"
FT /id="PRO_0000194097"
FT DOMAIN 285..491
FT /note="MCM"
FT REGION 643..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 467..470
FT /note="Arginine finger"
FT COMPBIAS 643..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 335..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 502
FT /note="G -> S (in Ref. 1; CAA03887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 776 AA; 86357 MW; 48EB068DC2AA8894 CRC64;
MDVPEETRLR HKRDFIQFLD SMYMEEIKAL VHQKRHRLII NISDIHHHFR EVASRILKNP
NEYMQSFCDA ATEATRAIDP KYLKEGELVL VGFEGYFVSR VVTPRELLSD FIGSMVCVEG
IVTKCSLVRP KVVKSVHFCP STGEFTNRDY RDITSHAGLP TGSVYPTRDD KGNLLVTEYG
LCKYKDHQTL SIQEVPENAA PGQLPRSVDV IAEDDLVDSC KPGDRVSVFG IYKALPGKSK
GSVNGVFRTI LIANNIALLN KEANAPIYTK QDLDNIKNIA RRDDAFDLLA RSLAPSIYGH
AWIKKAVVLL MLGGVEKNLK NGTHLRGDIN MMMVGDPSVA KSQLLRAIMN IAPLAISTTG
RGSSGVGLTA AVTSDQETGE RRLEAGAMVL ADKGIVCIDE FDKMNDQDRV AIHEVMEQQT
VTIAKAGIHA SLNARCSVVA AANPIYGTYD RSLTPTKNIG LPDSLLSRFD LLFIVLDQMD
AGIDSMISEH VLRMHRYKND RGEAGPDGSL PYAREDNAES EMFVKYNQTL HGKKKRGQTH
DKTLTIKFLK KYIHYAKHRI TPKLTDEASE RIAEAYADLR NAGSDTKTGG TLPITARTLE
TIIRLATAHA KMKLSSEVTK ADAEAALKLM NFAIYHQELT EMDDREQEER QREQAEQERT
PSGRRGNQRR NNEDGAENDT ANVDSETADP MEVDEPSVEQ FSGTVSAARI ETFERVFGQH
MRTHRLDDIS IADIETVVNN NGVGASRYSA DEIMALLEKL QDDNKVMISD GKVHII
