MCM2_ARATH
ID MCM2_ARATH Reviewed; 936 AA.
AC Q9LPD9; Q96275;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=DNA replication licensing factor MCM2;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance protein 2;
DE Short=AtMCM2;
GN Name=MCM2; OrderedLocusNames=At1g44900; ORFNames=T12C22.19;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 446-936.
RC STRAIN=cv. Columbia;
RA Callard P., Axelos M.;
RT "A.thaliana mRNA for MCM2-related protein.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19650778; DOI=10.1111/j.1469-8137.2009.02961.x;
RA Ni D.A., Sozzani R., Blanchet S., Domenichini S., Reuzeau C., Cella R.,
RA Bergounioux C., Raynaud C.;
RT "The Arabidopsis MCM2 gene is essential to embryo development and its over-
RT expression alters root meristem function.";
RL New Phytol. 184:311-322(2009).
RN [8]
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).
RN [9]
RP FUNCTION, AND INTERACTION WITH THE GEMINIVIRUS MUNGBEAN YELLOW MOSAIC VIRUS
RP (MYMV) REPLICATION INITIATOR PROTEIN.
RX PubMed=23242774; DOI=10.1007/s00705-012-1563-9;
RA Suyal G., Mukherjee S.K., Srivastava P.S., Choudhury N.R.;
RT "Arabidopsis thaliana MCM2 plays role(s) in mungbean yellow mosaic India
RT virus (MYMIV) DNA replication.";
RL Arch. Virol. 158:981-992(2013).
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. May play a crucial role in the control of de-
CC differentiation and cell proliferation processes required for lateral
CC root formation. Is essential for embryo development. Is involved in the
CC geminivirus mungbean yellow mosaic virus (MYMV) DNA replication,
CC presumably in conjunction with other host factors.
CC {ECO:0000269|PubMed:19650778, ECO:0000269|PubMed:23242774}.
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 and the replication-associated protein of the
CC geminivirus mungbean yellow mosaic virus (MYMV).
CC {ECO:0000269|PubMed:18528439, ECO:0000269|PubMed:23242774}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LPD9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in root apical meristem, lateral root
CC meristem primordia, leaf primordia, shoot apical meristem and flower
CC buds. {ECO:0000269|PubMed:19357199, ECO:0000269|PubMed:19650778}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:19650778}.
CC -!- MISCELLANEOUS: Over-expression of MCM2 strongly reduces plant and cell
CC sizes and inhibits endoreduplication. {ECO:0000305|PubMed:19650778}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK227536; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC020576; AAF78275.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32060.1; -; Genomic_DNA.
DR EMBL; AK227536; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Y08301; CAA69609.1; -; mRNA.
DR PIR; E96508; E96508.
DR RefSeq; NP_175112.2; NM_103572.5. [Q9LPD9-1]
DR AlphaFoldDB; Q9LPD9; -.
DR SMR; Q9LPD9; -.
DR BioGRID; 26281; 3.
DR IntAct; Q9LPD9; 2.
DR MINT; Q9LPD9; -.
DR STRING; 3702.AT1G44900.1; -.
DR iPTMnet; Q9LPD9; -.
DR PaxDb; Q9LPD9; -.
DR PRIDE; Q9LPD9; -.
DR ProteomicsDB; 238850; -. [Q9LPD9-1]
DR EnsemblPlants; AT1G44900.1; AT1G44900.1; AT1G44900. [Q9LPD9-1]
DR GeneID; 841056; -.
DR Gramene; AT1G44900.1; AT1G44900.1; AT1G44900. [Q9LPD9-1]
DR KEGG; ath:AT1G44900; -.
DR Araport; AT1G44900; -.
DR TAIR; locus:2028240; AT1G44900.
DR eggNOG; KOG0477; Eukaryota.
DR InParanoid; Q9LPD9; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q9LPD9; -.
DR PRO; PR:Q9LPD9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPD9; baseline and differential.
DR Genevisible; Q9LPD9; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR GO; GO:1905775; P:negative regulation of DNA helicase activity; IEA:InterPro.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:TAIR.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008045; MCM2.
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; PF12619; MCM2_N; 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; PR01658; MCMPROTEIN2.
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 Alternative splicing; ATP-binding; Cell cycle; DNA replication;
KW DNA-binding; Helicase; Host-virus interaction; Hydrolase; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..936
FT /note="DNA replication licensing factor MCM2"
FT /id="PRO_0000425986"
FT DOMAIN 499..705
FT /note="MCM"
FT ZN_FING 355..381
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 681..684
FT /note="Arginine finger"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 549..556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 936 AA; 105584 MW; EDED5161964DBC69 CRC64;
MAGENSDNEP SSPASPSSAG FNTDQLPIST SQNSENFSDE EEAAVDTQVI RDEPDEAEDE
EEEEGEDLFN DTFMNDYRKM DENDQYESNG IDDSVDDERD LGQAMLDRRA ADADLDAREN
RLANRKLPHL LHDNDSDDWN YRPSKRSRTT VPPRGNGGDP DGNPPSSPGV SQPDISMTDQ
TDDYQDEDDN DDEAEFEMYR IQGTLREWVM RDEVRRFIAK KFKDFLLTYV KPKNENGDIE
YVRLINEMVS ANKCSLEIDY KEFIHVHPNI AIWLADAPQP VLEVMEEVSE KVIFDLHPNY
KNIHTKIYVR VTNLPVNDQI RNIRQIHLNT MIRIGGVVTR RSGVFPQLQQ VKYDCNKCGA
VLGPFFQNSY SEVKVGSCSE CQSKGPFTVN VEQTIYRNYQ KLTIQESPGT VPAGRLPRHK
EVILLNDLID CARPGEEIEV TGIYTNNFDL SLNTKNGFPV FATVVEANYV TKKQDLFSAY
KLTQEDKTQI EELSKDPRIV ERIIKSIAPS IYGHEDIKTA LALAMFGGQE KNIKGKHRLR
GDINVLLLGD PGTAKSQFLK YVEKTGQRAV YTTGKGASAV GLTAAVHKDP VTREWTLEGG
ALVLADRGIC LIDEFDKMND QDRVSIHEAM EQQSISISKA GIVTSLQARC SVIAAANPVG
GRYDSSKSFA QNVELTDPIL SRFDILCVVK DVVDPVTDEM LAEFVVNSHF KSQPKGGKME
DSDPEDGIQG SSGSTDPEVL PQNLLKKYLT YSKLYVFPKL GELDAKKLET VYANLRRESM
NGQGVSIATR HLESMIRMSE AHARMHLRQY VTEEDVNMAI RVLLDSFIST QKFGVQRTLR
ESFKRYITYK KDFNSLLLVL LKELVKNALK FEEIISGSNS GLPTIEVKIE ELQTKAKEYD
IADLRPFFSS TDFSKAHFEL DHGRGMIKCP KRLITW
