MCM2_XENLA
ID MCM2_XENLA Reviewed; 886 AA.
AC P55861; O42588; Q7ZX05;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=DNA replication licensing factor mcm2;
DE AltName: Full=BM28-homolog;
DE AltName: Full=Minichromosome maintenance protein 2;
DE Short=xMCM2;
DE AltName: Full=p112;
GN Name=mcm2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION IN A COMPLEX WITH MCM5.
RC TISSUE=Oocyte;
RX PubMed=8917078; DOI=10.1016/0378-1119(96)00122-9;
RA Miyake S., Saito I., Kobayashi H., Yamashita S.;
RT "Identification of two Xenopus laevis genes, xMCM2 and xCDC46, with
RT sequence homology to MCM genes involved in DNA replication.";
RL Gene 175:71-75(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COMPLEX WITH
RP MMCM3; MCM4; MCM5; MMCM6 AND MCM7, AND SUBCELLULAR LOCATION.
RC TISSUE=Oocyte;
RX PubMed=9214647; DOI=10.1093/emboj/16.11.3320;
RA Kubota Y., Mimura S., Nishimoto S., Masuda T., Nojima H., Takisawa H.;
RT "Licensing of DNA replication by a multi-protein complex of MCM/P1 proteins
RT in Xenopus eggs.";
RL EMBO J. 16:3320-3331(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, IDENTIFICATION IN RLF-M COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=9214646; DOI=10.1093/emboj/16.11.3312;
RA Thommes P., Kubota Y., Takisawa H., Blow J.J.;
RT "The RLF-M component of the replication licensing system forms complexes
RT containing all six MCM/P1 polypeptides.";
RL EMBO J. 16:3312-3319(1997).
RN [5]
RP IDENTIFICATION IN MCM COMPLEXES.
RX PubMed=9851868; DOI=10.1006/excr.1998.4271;
RA Coue M., Amariglio F., Maiorano D., Bocquet S., Mechali M.;
RT "Evidence for different MCM subcomplexes with differential binding to
RT chromatin in Xenopus.";
RL Exp. Cell Res. 245:282-289(1998).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=10779356; DOI=10.1128/mcb.20.10.3667-3676.2000;
RA Pereverzeva I., Whitmire E., Khan B., Coue M.;
RT "Distinct phosphoisoforms of the Xenopus Mcm4 protein regulate the function
RT of the Mcm complex.";
RL Mol. Cell. Biol. 20:3667-3676(2000).
RN [7]
RP FUNCTION OF THE MCM2-7 COMPLEX, AND IDENTIFICATION IN A COMPLEX WITH MMCM3;
RP MCM4; MCM5; MMCM6 AND MCM7.
RX PubMed=16369567; DOI=10.1038/sj.emboj.7600892;
RA Ying C.Y., Gautier J.;
RT "The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is
RT required for DNA unwinding.";
RL EMBO J. 24:4334-4344(2005).
RN [8]
RP PHOSPHORYLATION.
RX PubMed=16204181; DOI=10.1101/gad.1339805;
RA Takahashi T.S., Walter J.C.;
RT "Cdc7-Drf1 is a developmentally regulated protein kinase required for the
RT initiation of vertebrate DNA replication.";
RL Genes Dev. 19:2295-2300(2005).
RN [9]
RP IDENTIFICATION IN THE CMG HELICASE COMPLEX.
RX PubMed=30979826; DOI=10.26508/lsa.201900390;
RA Priego Moreno S., Jones R.M., Poovathumkadavil D., Scaramuzza S.,
RA Gambus A.;
RT "Mitotic replisome disassembly depends on TRAIP ubiquitin ligase
RT activity.";
RL Life. Sci Alliance 2:0-0(2019).
RN [10]
RP IDENTIFICATION IN THE CMG HELICASE COMPLEX.
RX PubMed=30842657; DOI=10.1038/s41586-019-1002-0;
RA Wu R.A., Semlow D.R., Kamimae-Lanning A.N., Kochenova O.V., Chistol G.,
RA Hodskinson M.R., Amunugama R., Sparks J.L., Wang M., Deng L., Mimoso C.A.,
RA Low E., Patel K.J., Walter J.C.;
RT "TRAIP is a master regulator of DNA interstrand crosslink repair.";
RL Nature 567:267-272(2019).
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 the entry
CC in S phase and for cell division. {ECO:0000269|PubMed:16369567,
CC ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}.
CC -!- SUBUNIT: Component of the mcm2-7 complex (RLF-M) (PubMed:16369567,
CC PubMed:8917078, PubMed:9214646, PubMed:9214647, PubMed:9851868). The
CC complex forms a toroidal hexameric ring with the proposed subunit order
CC mcm2-mcm6-mcm4-mcm7-mcm3-mcm5 (PubMed:16369567, PubMed:8917078,
CC PubMed:9214646, PubMed:9214647, PubMed:9851868). Component of the
CC replisome complex (By similarity). Component of the CMG helicase
CC complex, composed of the mcm2-7 complex, the GINS complex and cdc45
CC (PubMed:30979826, PubMed:30842657). {ECO:0000250|UniProtKB:P49736,
CC ECO:0000269|PubMed:16369567, ECO:0000269|PubMed:30842657,
CC ECO:0000269|PubMed:30979826, ECO:0000269|PubMed:8917078,
CC ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647,
CC ECO:0000269|PubMed:9851868}.
CC -!- INTERACTION:
CC P55861; P49739: mmcm3; NbExp=9; IntAct=EBI-876864, EBI-491720;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9214646,
CC ECO:0000269|PubMed:9214647}. Chromosome {ECO:0000269|PubMed:9214646,
CC ECO:0000269|PubMed:9214647}. Note=Associated with chromatin before the
CC formation of nuclei and detaches from it as DNA replication progresses.
CC {ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}.
CC -!- PTM: May be in a phosphorylated state in the mitotic mcm complex.
CC Phosphorylated in the interphase mcm complex. Phosphorylated by the
CC cdc7-dbf4 and cdc7-dbf4b complexes. {ECO:0000269|PubMed:10779356,
CC ECO:0000269|PubMed:16204181}.
CC -!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins yielded a
CC variety of dimeric, trimeric and tetrameric complexes with unclear
CC biological significance. Specifically a MCM467 subcomplex is shown to
CC have in vitro helicase activity which is inhibited by the MCM2 subunit.
CC The MCM2-7 hexamer is the proposed physiological active complex.
CC {ECO:0000250|UniProtKB:P49736}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; D63919; BAA09948.1; -; mRNA.
DR EMBL; U44047; AAC60223.1; -; mRNA.
DR EMBL; BC046274; AAH46274.1; -; mRNA.
DR PIR; JC5085; JC5085.
DR RefSeq; NP_001080759.1; NM_001087290.2.
DR AlphaFoldDB; P55861; -.
DR SMR; P55861; -.
DR BioGRID; 98693; 11.
DR ComplexPortal; CPX-2943; MCM complex.
DR IntAct; P55861; 7.
DR MINT; P55861; -.
DR iPTMnet; P55861; -.
DR MaxQB; P55861; -.
DR PRIDE; P55861; -.
DR DNASU; 380451; -.
DR GeneID; 380451; -.
DR KEGG; xla:380451; -.
DR CTD; 380451; -.
DR Xenbase; XB-GENE-999979; mcm2.L.
DR OMA; KFARYTH; -.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 380451; Expressed in oocyte and 18 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0071162; C:CMG complex; IDA:UniProtKB.
DR GO; GO:0042555; C:MCM complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:UniProtKB.
DR GO; GO:1905775; P:negative regulation of DNA helicase activity; IEA:InterPro.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:UniProtKB.
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 PANTHER; PTHR11630:SF44; PTHR11630:SF44; 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 ATP-binding; Cell cycle; Chromosome; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..886
FT /note="DNA replication licensing factor mcm2"
FT /id="PRO_0000194089"
FT DOMAIN 458..665
FT /note="MCM"
FT ZN_FING 314..340
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 640..643
FT /note="Arginine finger"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..59
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 508..515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 169
FT /note="E -> K (in Ref. 2; AAC60223)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="G -> R (in Ref. 1; BAA09948)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="L -> F (in Ref. 1; BAA09948)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="M -> I (in Ref. 1; BAA09948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 886 AA; 100262 MW; 524C7B3673E2B2DD CRC64;
MADSSESFNI ATSPRAGSRR DALTSSPGRD LPPFEDESEG MFGDGVVPEE EEDGEELIGD
AMERDYRPIS ELDRYEVEGL DDEEDVEDLT ASQREAAEQS MRMRDREMGR ELGRMRRGLL
YDSDEEEEDR PARKRRMAER AAEGAPEEDE EMIESIENLE DMKGHTVREW VSMAATRLEI
YHRFKNFLRT HVDEHGHNVF KEKISDMCKE NKESLPVNYE DLAAREHVLA YFLPEAPAEM
LKIFDEAAKE VVLVMYPKYD RIAREIHVRI SHLPLVEELR SLRQLHLNQL IRTSGVVTCC
TGVLPQLSMV KYNCNKCNFI LGPFFQSQNQ EVRPGSCPEC QSFGPFEINM EETVYQNYQR
ITIQESPGKV AAGRLPRSKD AILLADLVDS CKPGDEIELT GIYHNNYDGS LNTANGFPVF
ATVILANHIT KKDDKVAVGE LTDEDVKAIV ALSKDERIGE RIFASIAPSI YGHEDIKRGL
ALALFGGEAK NPGGKHKVRG DINVLLCGDP GTAKSQFLKY VEKVASRAVF TTGQGASAVG
LTAYVQRHPV TKEWTLEAGA LVLADRGVCL IDEFDKMNDQ DRTSIHEAME QQSISISKAG
IVTSLQARCT VIAASNPIGG RYDPSLTFSE NVDLTEPIVS RFDILCVVRD TVDPVQDEML
ARFVVSSHIK HHPSSKDIAN GDAAEFALPN TFGVEALPQE VLKKYIMYAK EKIRPKLNQM
DQDKVAKMYS DLRKESMATG SIPITVRHIE SMIRMAEAHA RMHLRDYVVE DDVNMAIRVM
LESFIDTQKF SVMRSMRKTF ARYLAFRRDN NELLLFVLKQ LIAEQVTYQR NRYGAQQDTI
EVPEKDLVDK ARQINIHNLS AFYDSDLFKM NKFTHDVKKK LIIQQF
