MCM3M_XENLA
ID MCM3M_XENLA Reviewed; 807 AA.
AC P49739; Q2NL58; Q91919;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Maternal DNA replication licensing factor mcm3;
DE EC=3.6.4.12;
DE AltName: Full=Maternal minichromosome maintenance protein 3;
DE Short=mMCM3;
DE Short=xMCM3;
DE AltName: Full=P1 homolog;
DE AltName: Full=XRLF subunit beta;
DE AltName: Full=p100;
GN Name=mmcm3;
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, IDENTIFICATION IN A COMPLEX WITH MCM2
RP AND MCM5, AND SUBCELLULAR LOCATION.
RC TISSUE=Egg;
RX PubMed=7760938; DOI=10.1038/375421a0;
RA Madine M.A., Khoo C.Y., Mills A.D., Laskey R.A.;
RT "MCM3 complex required for cell cycle regulation of DNA replication in
RT vertebrate cells.";
RL Nature 375:421-424(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-807, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Oocyte;
RX PubMed=7758114; DOI=10.1016/0092-8674(95)90081-0;
RA Kubota Y., Mimura S., Nishimoto S., Takisawa H., Nojima H.;
RT "Identification of the yeast MCM3-related protein as a component of Xenopus
RT DNA replication licensing factor.";
RL Cell 81:601-609(1995).
RN [4]
RP FUNCTION, IDENTIFICATION IN RLF-M COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=7760937; DOI=10.1038/375418a0;
RA Chong J.P., Mahbubani H.M., Khoo C.Y., Blow J.J.;
RT "Purification of an MCM-containing complex as a component of the DNA
RT replication licensing system.";
RL Nature 375:418-421(1995).
RN [5]
RP FUNCTION, INTERACTION WITH MCM7, IDENTIFICATION IN A COMPLEX WITH MCM2;
RP MCM4; MCM5 AND MCM7, AND SUBCELLULAR LOCATION.
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 [6]
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 [7]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH MCM2; MCM4; MCM5; MMCM6 AND
RP MCM7, AND SUBCELLULAR LOCATION.
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 [8]
RP 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 [9]
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 [10]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH MCM2; MCM4; MCM5; MMCM6 AND
RP 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 [11]
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 [12]
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. 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:7758114,
CC ECO:0000269|PubMed:7760937, ECO:0000269|PubMed:7760938,
CC ECO:0000269|PubMed:8816774, ECO:0000269|PubMed:9214646,
CC 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 -!- SUBUNIT: Component of the mcm2-7 complex (RLF-M) (PubMed:8816774,
CC PubMed:16369567, PubMed:7760937, PubMed:7760938, PubMed:9214646,
CC PubMed:9214647, PubMed:9851868). The complex forms a toroidal hexameric
CC ring with the proposed subunit order mcm2-mcm6-mcm4-mcm7-mcm3-mcm5
CC (PubMed:16369567, PubMed:7760937, PubMed:7760938, PubMed:9214646,
CC PubMed:9214647, PubMed:9851868). The heterodimer of mmcm3/mcm5
CC interacts with mcm4, mmcm6, mcm7 and weakly with mcm2 (PubMed:16369567,
CC PubMed:7760937, PubMed:7760938, PubMed:9214646, PubMed:9214647,
CC PubMed:9851868). Interacts with mcm7, though this interaction may not
CC be direct, and remains in a complex with mcm7 throughout the cell cycle
CC (PubMed:8816774). Component of the CMG helicase complex, composed of
CC the mcm2-7 complex, the GINS complex and cdc45 (PubMed:30979826,
CC PubMed:30842657). {ECO:0000269|PubMed:16369567,
CC ECO:0000269|PubMed:30842657, ECO:0000269|PubMed:30979826,
CC ECO:0000269|PubMed:7760937, ECO:0000269|PubMed:7760938,
CC ECO:0000269|PubMed:8816774, ECO:0000269|PubMed:9214646,
CC ECO:0000269|PubMed:9214647, ECO:0000269|PubMed:9851868}.
CC -!- INTERACTION:
CC P49739; P55861: mcm2; NbExp=9; IntAct=EBI-491720, EBI-876864;
CC P49739; P55862: mcm5-a; NbExp=5; IntAct=EBI-491720, EBI-876879;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7758114,
CC ECO:0000269|PubMed:7760937, ECO:0000269|PubMed:7760938,
CC ECO:0000269|PubMed:8816774, 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 -!- DEVELOPMENTAL STAGE: Expressed maternally. Expression decreases
CC suddenly at the gastrula stage. {ECO:0000269|PubMed:9512418}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; U26057; AAA80227.1; -; mRNA.
DR EMBL; D38074; BAA07268.1; -; mRNA.
DR EMBL; BC110950; AAI10951.1; -; mRNA.
DR PIR; I51685; I51685.
DR RefSeq; NP_001081412.1; NM_001087943.1.
DR AlphaFoldDB; P49739; -.
DR SMR; P49739; -.
DR BioGRID; 99160; 3.
DR ComplexPortal; CPX-2943; MCM complex.
DR IntAct; P49739; 10.
DR MINT; P49739; -.
DR MaxQB; P49739; -.
DR DNASU; 397821; -.
DR GeneID; 397821; -.
DR KEGG; xla:397821; -.
DR CTD; 397821; -.
DR Xenbase; XB-GENE-5857895; mcm3.L.
DR OMA; VHDINAD; -.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 397821; Expressed in blastula and 5 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: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 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 ATP-binding; Cell cycle; Chromosome; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..807
FT /note="Maternal DNA replication licensing factor mcm3"
FT /id="PRO_0000194095"
FT DOMAIN 295..502
FT /note="MCM"
FT REGION 664..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 477..480
FT /note="Arginine finger"
FT COMPBIAS 683..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 345..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 206
FT /note="E -> D (in Ref. 2; BAA07268)"
FT /evidence="ECO:0000305"
FT CONFLICT 606
FT /note="D -> G (in Ref. 1; AAA80227)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="S -> P (in Ref. 1; AAA80227)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="D -> G (in Ref. 2; BAA07268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 807 AA; 90405 MW; 70B08E9BE0F3A81F CRC64;
MDYGGGFEDH ELREAQREYL DFLDDDQDQG LYHGKVRDMI GSNEHRLIVN LNDVRRKNDK
RANLMLNDAF AETIAFQRAL KDLVASIDAT YAKQFEEFSV GFEGSFGSKH VSPRTLTASL
LGSLVCVEGI VTKCSLVRPK VMRSVHYCPA TKKTLERKYS DLTSLEAFPS SSIYPTKDEE
NNPLETEYGL STYKDHQTLS IQEMPEKAPA GQLPRSVDII ADDDLVDKCK PGDRVQIVGI
YRCLPSKQGG FTSGTFRTIL LANNIKLMSK EIAPTFSADD VAKIKKFCKA HSKDIFEHLS
KSLAPSIHGH EYIKKAILCM LLGGNEKVLE NGTRIRGDIN VLLIGDPSVA KSQLLRYVLH
TAPRAIPTTG RGSSGVGLTA AVTTDQETGE RRLEAGAMVL ADRGVVCIDE FDKMSDMDRT
AIHEVMEQGR VTIAKAGIQA RLNARCSVLA AANPVYGRYD QYRTPMENIG LQDSLLSRFD
LLFIVLDKMD ADNDQEIADH VLRMHRYRTP GEQDGYALPL GCSVEIFATD DPNASDVTDQ
ELQIYEKHDN LLHGPRKNKS KIVSMQFIRK YIHVAKLIKP VLTSEAADYI SQEYAKIRNH
DQINNDSART MPVTARALET MIRLSTAHAK VRMSKTIERQ DAETALELVQ FAYFKKVLAK
EKKKTDKDLH DENLSQDTLS QESVRKSSRR AGKIADSQDD SMDPYSFSEQ DSSLNENLSQ
SLRPQRKKAE SQDGKRSLSQ NRTKEFKAAL LKAFKSSRSQ SVAVSQLLEL INKGNPEPFE
RSEVKEALDN MQNDNQVMVS EDVVFLI
