MCM3_DROME
ID MCM3_DROME Reviewed; 819 AA.
AC Q9XYU1; P91675;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=DNA replication licensing factor Mcm3;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance 3 protein;
DE Short=DmMCM3;
GN Name=Mcm3; Synonyms=Mcm3-RA; ORFNames=CG4206;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9795205; DOI=10.1016/s0378-1119(98)00358-8;
RA Ohno K., Hirose F., Inoue Y.H., Takisawa H., Mimura S., Hashimoto Y.,
RA Kiyono T., Nishida Y., Matsukage A.;
RT "cDNA cloning and expression during development of Drosophila melanogaster
RT MCM3, MCM6 and MCM7.";
RL Gene 217:177-185(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10023044; DOI=10.1016/s0378-1119(98)00596-4;
RA Feger G.;
RT "Identification and complete cDNA sequence of the missing Drosophila MCMs:
RT DmMCM3, DmMCM6 and DmMCM7.";
RL Gene 227:149-155(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION IN THE MCM2-7 COMPLEX, AND FUNCTION OF THE MCM2-7 COMPLEX.
RX PubMed=16798881; DOI=10.1073/pnas.0602400103;
RA Moyer S.E., Lewis P.W., Botchan M.R.;
RT "Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the
RT eukaryotic DNA replication fork helicase.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10236-10241(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697; SER-735 AND SER-739, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; TYR-538; SER-664;
RP SER-666; SER-680; SER-682; THR-690; THR-692 AND SER-697, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [9]
RP RECONSTITUTION OF THE MCM2-7 COMPLEX, FUNCTION OF THE MCM2-7 COMPLEX, AND
RP MUTAGENESIS OF LYS-346.
RX PubMed=20122406; DOI=10.1016/j.molcel.2009.12.030;
RA Ilves I., Petojevic T., Pesavento J.J., Botchan M.R.;
RT "Activation of the MCM2-7 helicase by association with Cdc45 and GINS
RT proteins.";
RL Mol. Cell 37:247-258(2010).
CC -!- FUNCTION: Acts as component of the Mcm2-7 complex (Mcm complex) (Mcm
CC complex) which is the putative replicative helicase essential for 'once
CC per cell cycle' DNA replication initiation and elongation in eukaryotic
CC cells. 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.
CC {ECO:0000269|PubMed:16798881, ECO:0000269|PubMed:20122406}.
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. The complex forms a toroidal
CC hexameric ring with the proposed subunit order Mcm2-Mcm6-Mcm4-Mcm7-
CC Mcm3-Mcm5 (Probable). {ECO:0000269|PubMed:16798881, ECO:0000305}.
CC -!- INTERACTION:
CC Q9XYU1; Q9VGW6: Mcm5; NbExp=7; IntAct=EBI-103930, EBI-83298;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; AB010107; BAA34731.1; -; mRNA.
DR EMBL; AF124745; AAD32859.1; -; mRNA.
DR EMBL; AE014298; AAF46023.1; -; Genomic_DNA.
DR EMBL; BT046156; ACI46544.1; -; mRNA.
DR RefSeq; NP_511048.2; NM_078493.4.
DR PDB; 6RAW; EM; 3.70 A; 3=1-819.
DR PDB; 6RAX; EM; 3.99 A; 3=1-819.
DR PDB; 6RAY; EM; 4.28 A; 3=1-819.
DR PDB; 6RAZ; EM; 4.46 A; 3=1-819.
DR PDBsum; 6RAW; -.
DR PDBsum; 6RAX; -.
DR PDBsum; 6RAY; -.
DR PDBsum; 6RAZ; -.
DR AlphaFoldDB; Q9XYU1; -.
DR SMR; Q9XYU1; -.
DR BioGRID; 57959; 14.
DR ComplexPortal; CPX-2942; MCM complex.
DR IntAct; Q9XYU1; 11.
DR STRING; 7227.FBpp0070729; -.
DR iPTMnet; Q9XYU1; -.
DR PaxDb; Q9XYU1; -.
DR PRIDE; Q9XYU1; -.
DR EnsemblMetazoa; FBtr0070762; FBpp0070729; FBgn0284442.
DR GeneID; 31449; -.
DR KEGG; dme:Dmel_CG4206; -.
DR UCSC; CG4206-RA; d. melanogaster.
DR CTD; 4172; -.
DR FlyBase; FBgn0284442; Mcm3.
DR VEuPathDB; VectorBase:FBgn0284442; -.
DR eggNOG; KOG0479; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR InParanoid; Q9XYU1; -.
DR OMA; NVYPQED; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q9XYU1; -.
DR Reactome; R-DME-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DME-68867; Assembly of the pre-replicative complex.
DR Reactome; R-DME-68949; Orc1 removal from chromatin.
DR Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR Reactome; R-DME-69052; Switching of origins to a post-replicative state.
DR BioGRID-ORCS; 31449; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31449; -.
DR PRO; PR:Q9XYU1; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0284442; Expressed in secondary oocyte and 34 other tissues.
DR ExpressionAtlas; Q9XYU1; baseline and differential.
DR Genevisible; Q9XYU1; DM.
DR GO; GO:0071162; C:CMG complex; IDA:FlyBase.
DR GO; GO:0042555; C:MCM complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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 3D-structure; ATP-binding; Cell cycle; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..819
FT /note="DNA replication licensing factor Mcm3"
FT /id="PRO_0000406421"
FT DOMAIN 290..496
FT /note="MCM"
FT REGION 655..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 472..475
FT /note="Arginine finger"
FT COMPBIAS 655..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 340..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 538
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 692
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MUTAGEN 346
FT /note="K->A: Greatly reduces complex helicase activity."
FT /evidence="ECO:0000269|PubMed:20122406"
FT CONFLICT 141
FT /note="S -> C (in Ref. 1; BAA34731)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="H -> D (in Ref. 1; BAA34731)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="L -> Q (in Ref. 1; BAA34731)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="Q -> L (in Ref. 1; BAA34731)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="V -> D (in Ref. 1; BAA34731)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="S -> L (in Ref. 1; BAA34731)"
FT /evidence="ECO:0000305"
FT CONFLICT 795..796
FT /note="EI -> AL (in Ref. 1; BAA34731)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 819 AA; 90918 MW; CE4C14FE89BA8113 CRC64;
MAHEGEQFIK DIQREYVDFL DDEEDQGIYA GHVKDMIAEK SKRLIVNVND LKRKNPQRAL
GLLSNAADEQ LAFGRALKEY ASTVDPGYAK MHEDLFVGFE GCFGNRHVTP RSLTSIYLGN
MVCVEGIVTK VSLIRPKVVR SVHYCPNTRK VMERKYTDLT SFEAVPSGAA YPTKDEDGNL
LETEYGLSVY KDHQTLTIQE MPEKAPAGQL PRSVDIVCDD DLVDRCKPGD RVQIVGSYRC
LPGKRGGYTS GTFRTVLLAN NISLLSKESN LDISREDIML CKKLAKNNDI FELLSKSLAP
SIHGHAYVKQ AILCLLLGGV EKILPNGTRL RGDINVLLIG DPSVAKSQLL RYVLNTAPRA
IPTTGRGSSG VGLTAAVTTD QETGERRLEA GAMVLADRGV VCIDEFDKMS DIDRTAIHEV
MEQGRVTISK AGIHASLNAR CSVLAAANPV YGRYDQYKTP MENIGLQDSL LSRFDLLFVM
LDVIDSDVDQ MISDHVVRMH RYRNPKEADG EPLSMGSSYA DSLSFVSSSE EKKDTEVYEK
YDALLHGKSR QRHEKILSVE FMRKYIHIAK CMKPKLGEQA CEAIANEYSR LRSQEAVETD
VARTQPITAR TLETLIRLST AHARARMSKS VTIDDAHAAI ELVQFAYFKK VLDKDRPSKR
RRNSGSDAED DNGEASSQRS PSRRSKRTRT ATVGADSDEE DIEPPQPDAG DLTRRETRRS
LPARSVAMLM ASPSSEEQSV ATSTTEPAII SDARLGEFKN NLQRLFREAR EQSLALARIT
TAINVGSQEP FTAGEIEAAV HRMTEDNQIM VADDIVFLI
