MCM7_ARATH
ID MCM7_ARATH Reviewed; 716 AA.
AC P43299; O04721;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=DNA replication licensing factor MCM7;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance protein 7;
DE Short=AtMCM7;
DE AltName: Full=Protein PROLIFERA;
GN Name=MCM7; Synonyms=PRL; OrderedLocusNames=At4g02060;
GN ORFNames=AGAA.2, T10M13.7;
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. Landsberg erecta;
RX PubMed=7754372; DOI=10.1126/science.7754372;
RA Springer P.S., McCombie W.R., Sundaresan V., Martienssen R.A.;
RT "Gene trap tagging of PROLIFERA, an essential MCM2-3-5-like gene in
RT Arabidopsis.";
RL Science 268:877-880(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Till S., Granat S., Parnell L., Kaplan N., Hoffman J., Lodhi M.,
RA Johnson A.F., Dedhia N., Martienssen R., McCombie W.R.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP CHARACTERIZATION.
RX PubMed=10751170; DOI=10.1242/dev.127.9.1815;
RA Springer P.S., Holding D.R., Groover A., Yordan C., Martienssen R.A.;
RT "The essential Mcm7 protein PROLIFERA is localized to the nucleus of
RT dividing cells during the G(1) phase and is required maternally for early
RT Arabidopsis development.";
RL Development 127:1815-1822(2000).
RN [6]
RP INDUCTION.
RX PubMed=18944154; DOI=10.1094/phyto.2003.93.1.35;
RA Huang X., Springer P.S., Kaloshian I.;
RT "Expression of the Arabidopsis MCM gene PROLIFERA during root-knot and cyst
RT nematode infection.";
RL Phytopathology 93:35-41(2003).
RN [7]
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 [8]
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 [9]
RP SUBCELLULAR LOCATION, AND 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 (By similarity). Required for megagametophyte and
CC embryo development. {ECO:0000250}.
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:0000269|PubMed:19357199}. Cytoplasm
CC {ECO:0000269|PubMed:19357199}. Note=Localized in the nucleus during G1,
CC S and G2 phases of the cell cycle, and released into the cytoplasmic
CC compartment during mitosis.
CC -!- TISSUE SPECIFICITY: Expressed in shoot apex and flower buds.
CC {ECO:0000269|PubMed:19357199}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in nucleus during the G1 phase of the
CC cell cycle. During mitosis, the protein rapidly disappears, returning
CC to daughter nuclei during G1.
CC -!- INDUCTION: By both rootknot and cyst nematode infections.
CC {ECO:0000269|PubMed:18944154}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; L39954; AAC37429.1; -; mRNA.
DR EMBL; AF001535; AAB57797.1; -; Genomic_DNA.
DR EMBL; AF001308; AAC78698.1; -; Genomic_DNA.
DR EMBL; AL161493; CAB80699.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82117.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82118.1; -; Genomic_DNA.
DR PIR; T01507; T01507.
DR RefSeq; NP_001190655.1; NM_001203726.1.
DR RefSeq; NP_192115.1; NM_116437.3.
DR AlphaFoldDB; P43299; -.
DR SMR; P43299; -.
DR BioGRID; 13442; 9.
DR IntAct; P43299; 5.
DR MINT; P43299; -.
DR STRING; 3702.AT4G02060.2; -.
DR iPTMnet; P43299; -.
DR PaxDb; P43299; -.
DR PRIDE; P43299; -.
DR ProteomicsDB; 250828; -.
DR EnsemblPlants; AT4G02060.1; AT4G02060.1; AT4G02060.
DR EnsemblPlants; AT4G02060.2; AT4G02060.2; AT4G02060.
DR GeneID; 828153; -.
DR Gramene; AT4G02060.1; AT4G02060.1; AT4G02060.
DR Gramene; AT4G02060.2; AT4G02060.2; AT4G02060.
DR KEGG; ath:AT4G02060; -.
DR Araport; AT4G02060; -.
DR TAIR; locus:2132223; AT4G02060.
DR eggNOG; KOG0482; Eukaryota.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; P43299; -.
DR OMA; NAYTCDR; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; P43299; -.
DR PRO; PR:P43299; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P43299; baseline and differential.
DR Genevisible; P43299; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0090329; P:regulation of DNA-templated DNA replication; IPI:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; TAS:TAIR.
DR CDD; cd17758; MCM7; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; 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; Cytoplasm; DNA replication; DNA-binding; Helicase;
KW Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..716
FT /note="DNA replication licensing factor MCM7"
FT /id="PRO_0000194122"
FT DOMAIN 326..531
FT /note="MCM"
FT ZN_FING 178..205
FT /note="C4-type"
FT /evidence="ECO:0000250"
FT MOTIF 508..511
FT /note="Arginine finger"
FT BINDING 376..383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 707
FT /note="D -> E (in Ref. 1; AAC37429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 80333 MW; 102DE5445E0C32D5 CRC64;
MKDHDFDGDK GLAKGFLENF ADANGRSKYM EILQEVSNRK IRAIQVDLDD LFNYKDESEE
FLGRLTENTR RYVSIFSAAV DELLPEPTEA FPDDDHDILM TQRADDGTDN PDVSDPHQQI
PSEIKRYYEV YFKAPSKGRP STIREVKASH IGQLVRISGI VTRCSDVKPL MAVAVYTCED
CGHEIYQEVT SRVFMPLFKC PSSRCRLNSK AGNPILQLRA SKFLKFQEAK MQELAEHVPK
GHIPRSMTVH LRGELTRKVS PGDVVEFSGI FLPIPYTGFK ALRAGLVADT YLEATSVTHF
KKKYEEYEFQ KDEEEQIARL AEDGDIYNKL SRSLAPEIYG HEDIKKALLL LLVGAPHRQL
KDGMKIRGDV HICLMGDPGV AKSQLLKHII NVAPRGVYTT GKGSSGVGLT AAVMRDQVTN
EMVLEGGALV LADMGICAID EFDKMDESDR TAIHEVMEQQ TVSIAKAGIT TSLNARTAVL
AAANPAWGRY DLRRTPAENI NLPPALLSRF DLLWLILDRA DMDSDLELAK HVLHVHQTEE
SPALGFEPLE PNILRAYISA ARRLSPYVPA ELEEYIATAY SSIRQEEAKS NTPHSYTTVR
TLLSILRISA ALARLRFSES VAQSDVDEAL RLMQMSKISL YADDRQKAGL DAISDTYSII
RDEAARSKKT HVSYANALNW ISRKGYSEAQ LKECLEEYAA LNVWQIDPHT FDIRFI