MCM7A_XENLA
ID MCM7A_XENLA Reviewed; 720 AA.
AC Q91876; O42591; Q6GQ16;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=DNA replication licensing factor mcm7-A;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q61881};
DE AltName: Full=CDC47 homolog A;
DE AltName: Full=CDC47p;
DE AltName: Full=Minichromosome maintenance protein 7-A;
DE Short=xMCM7-A;
DE AltName: Full=p90;
GN Name=mcm7-a; Synonyms=cdc47;
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], FUNCTION, INTERACTION WITH MMCM3,
RP IDENTIFICATION IN A COMPLEX WITH MCM2; MMCM3; MCM4 AND MCM5, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Egg;
RX PubMed=8816774; DOI=10.1073/pnas.93.19.10189;
RA Romanowski P., Madine M.A., Laskey R.A.;
RT "XMCM7, a novel member of the Xenopus MCM family, interacts with XMCM3 and
RT colocalizes with it throughout replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10189-10194(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COMPLEX WITH
RP MCM2; MMCM3; MCM4; MCM5 AND MMCM6, 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 (JUN-2004) 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 A COMPLEX WITH ZMCM6, AND DEVELOPMENTAL STAGE.
RX PubMed=9512418; DOI=10.1016/s0960-9822(98)70136-8;
RA Sible J.C., Erikson E., Hendrickson M., Maller J.L., Gautier J.;
RT "Developmental regulation of MCM replication factors in Xenopus laevis.";
RL Curr. Biol. 8:347-350(1998).
RN [6]
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 [7]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH MCM2; MMCM3; MCM4; MCM5 AND
RP MMCM6, AND MUTAGENESIS OF LYS-386.
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 UBIQUITINATION, AND 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 [9]
RP UBIQUITINATION, AND 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. The existence of
CC maternal and zygotic forms of mcm3 and mcm6 suggests that specific
CC forms of mcm2-7 complexes may be used during different stages of
CC development. {ECO:0000269|PubMed:16369567, ECO:0000269|PubMed:8816774,
CC ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}.
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 Evidence={ECO:0000250|UniProtKB:Q61881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q61881};
CC -!- SUBUNIT: Component of the mcm2-7 complex (RLF-M) (PubMed:16369567,
CC PubMed:8816774, 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:8816774,
CC PubMed:9214646, PubMed:9214647, PubMed:9851868). The heterodimer of
CC mmcm3/mcm5 interacts with mcm4, mmcm6, mcm7 and weakly with mcm2
CC (PubMed:16369567, PubMed:8816774, PubMed:9214646, PubMed:9214647,
CC PubMed:9851868). The N-terminus is required for interaction with mmcm3,
CC though this interaction may not be direct, and remains in a complex
CC with mmcm3 throughout the cell cycle (PubMed:16369567, PubMed:8816774,
CC PubMed:9214646, PubMed:9214647, PubMed:9851868). Begins to associate
CC with zmcm6 at the neurula stage (PubMed:9512418). 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:P33993,
CC ECO:0000269|PubMed:16369567, ECO:0000269|PubMed:30842657,
CC ECO:0000269|PubMed:30979826, ECO:0000269|PubMed:8816774,
CC ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647,
CC ECO:0000269|PubMed:9512418, ECO:0000269|PubMed:9851868}.
CC -!- INTERACTION:
CC Q91876; P70032: plk1; NbExp=3; IntAct=EBI-876852, EBI-3511304;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8816774,
CC ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}. Chromosome
CC {ECO:0000269|PubMed:8816774, 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:8816774, ECO:0000269|PubMed:9214646,
CC ECO:0000269|PubMed:9214647}.
CC -!- DEVELOPMENTAL STAGE: Present at constant levels throughout development.
CC {ECO:0000269|PubMed:9512418}.
CC -!- PTM: Ubiquitinated by traip when forks converge following formation of
CC DNA interstrand cross-links (PubMed:30979826, PubMed:30842657).
CC Ubiquitinated via 'Lys-6'- and 'Lys-63'-linked polyubiquitination by
CC traip (PubMed:30979826). Short ubiquitin chains on mcm7 promote
CC recruitment of DNA glycosylase neil3 (PubMed:30979826,
CC PubMed:30842657). If the interstrand cross-link cannot be cleaved by
CC neil3, the ubiquitin chains continue to grow on mcm7, promoting the
CC unloading of the CMG helicase complex by the vcp/p97 ATPase
CC (PubMed:30979826, PubMed:30842657). {ECO:0000269|PubMed:30842657,
CC ECO:0000269|PubMed:30979826}.
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:Q61881}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; U51234; AAB17253.1; -; mRNA.
DR EMBL; U44051; AAC60227.1; -; mRNA.
DR EMBL; BC072932; AAH72932.1; -; mRNA.
DR PIR; T47221; T47221.
DR RefSeq; NP_001081466.1; NM_001087997.1.
DR AlphaFoldDB; Q91876; -.
DR SMR; Q91876; -.
DR ComplexPortal; CPX-2943; MCM complex.
DR IntAct; Q91876; 6.
DR MINT; Q91876; -.
DR DNASU; 397852; -.
DR GeneID; 397852; -.
DR KEGG; xla:397852; -.
DR CTD; 397852; -.
DR Xenbase; XB-GENE-5946952; mcm7.S.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 397852; Expressed in egg cell 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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: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:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:UniProtKB.
DR CDD; cd17758; MCM7; 1.
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; 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; 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; Chromosome; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..720
FT /note="DNA replication licensing factor mcm7-A"
FT /id="PRO_0000194121"
FT DOMAIN 331..537
FT /note="MCM"
FT ZN_FING 183..210
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT MOTIF 512..515
FT /note="Arginine finger"
FT BINDING 380..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 386
FT /note="K->A: Reduces ATPase activity of the mcm2-mcm7
FT complex and disrupts DNA replication. Does not disrupt
FT formation of the pre-replicative complex onto chromatin.
FT Abolishes ATPase activity of the mcm2-mcm7 complex; when
FT associated with A-404 in mmcm6."
FT /evidence="ECO:0000269|PubMed:16369567"
FT CONFLICT 162
FT /note="I -> V (in Ref. 1; AAB17253)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="G -> W (in Ref. 2; AAC60227)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="V -> L (in Ref. 2; AAC60227)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="S -> T (in Ref. 1; AAB17253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 81879 MW; AD623D73B501647E CRC64;
MPRDYQTEKE KCKTFLQEFY KDDEIGKKHF KYGVQLANIA HREQVALYID LDDLAEEDPE
LVDAICENTR RYTNLFADAV QELLPQYKER EVVHKDALDV YIEHRLMMEQ RGRDPNEMRD
SQNQYPPELM RRFELYFKAP SSSKARVVRD VKADSIGKLV NIRGIVTRVT EVKPMMVVAT
YTCDQCGAET YQPIQSPTFM PLIMCPSREC QTNRSGGRLY LQTRGSKFIK FQELKIQEHS
DQVPVGNIPR CMSVYVRGEN TRLAQPGDHV GITGVFLPML RTGFRQVVQG LLSETYLECH
RLVKMNKSED DELGTEELSE EELRQITEED FYEKLAASIA PEIYGHEDVK KALLLLLVGG
VDNSPRGMKI RGNINICLMG DPGVAKSQLL SYIDRLAPRS QYTTGRGSSG VGLTAAVMKD
PVTGEMTLEG GALVLADQGV CCIDEFDKMM DTDRTAIHEV MEQQTISIAK AGIMTTLNAR
CSILAAANPA YGRYNPKKTV EQNIQLPAAL LSRFDVLWLI QDKPDRDNDL RLAQHITYVH
QHSKQPPSQF QPLDMKLMRR YITMCKRKQP AIPEALADYL TAAYVEMRKE ARTNKDMTFT
SARTLLSVLR LSTALARLRL EDVVEKEDVN EAMRLMEMSK DSLLGDKGHT SRTQRPADVI
FSTIREMVPE KGARSVKYSE AEQRCVSKGF TPAQFEAALE EYEELNVWLV NQARTKITFV
