MCM4_XENTR
ID MCM4_XENTR Reviewed; 863 AA.
AC Q6GL41;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA replication licensing factor mcm4;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P49717};
DE AltName: Full=Minichromosome maintenance protein 4;
GN Name=mcm4 {ECO:0000312|EMBL:AAH74670.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH74670.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000250|UniProtKB:P30664}.
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:P49717};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P49717};
CC -!- SUBUNIT: Component of the mcm2-7 complex (RLF-M). The complex forms a
CC toroidal hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-
CC mcm7-mcm3-mcm5. The heterodimer of mmcm3/mcm5 interacts with mcm4,
CC mmcm6, mcm7 and weakly with mcm2. Component of the CMG helicase
CC complex, composed of the mcm2-7 complex, the GINS complex and cdc45.
CC {ECO:0000250|UniProtKB:P30664}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P30664}.
CC Chromosome {ECO:0000250|UniProtKB:P30664}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250|UniProtKB:P30664}.
CC -!- PTM: Hyperphosphorylated during mitosis in a mechanism requiring cdc2-
CC cyclin B and other kinases. Undergoes dephosphorylation after exiting
CC mitosis, existing in a partially phosphorylated state in the cytosolic
CC interphase mcm complex which associates with the pre-replication
CC complexes (pre-Rcs). Complete dephosphorylation inactivates the mcm
CC complex, preventing its binding to chromatin. Becomes actively
CC phosphorylated during S phase once the mcm complex is assembled on the
CC chromatin. This chromatin-associated phosphorylation occurs during the
CC activation of the pre-Rcs and is independent of cdks. Phosphorylated by
CC the cdc7-dbf4b complex (By similarity). {ECO:0000250}.
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:P49717}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000255}.
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DR EMBL; BC074670; AAH74670.1; -; mRNA.
DR RefSeq; NP_001005655.1; NM_001005655.1.
DR RefSeq; XP_012819970.1; XM_012964516.2.
DR AlphaFoldDB; Q6GL41; -.
DR SMR; Q6GL41; -.
DR STRING; 8364.ENSXETP00000010537; -.
DR PaxDb; Q6GL41; -.
DR DNASU; 448137; -.
DR GeneID; 448137; -.
DR KEGG; xtr:448137; -.
DR CTD; 4173; -.
DR Xenbase; XB-GENE-1011481; mcm4.
DR eggNOG; KOG0478; Eukaryota.
DR InParanoid; Q6GL41; -.
DR OrthoDB; 266497at2759; -.
DR Reactome; R-XTR-176187; Activation of ATR in response to replication stress.
DR Reactome; R-XTR-68867; Assembly of the pre-replicative complex.
DR Reactome; R-XTR-68962; Activation of the pre-replicative complex.
DR Reactome; R-XTR-69052; Switching of origins to a post-replicative state.
DR Proteomes; UP000008143; Chromosome 6.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000004854; Expressed in ovary and 15 other tissues.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
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:0003682; F:chromatin binding; IEA:Ensembl.
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:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0001878; P:response to yeast; IEA:Ensembl.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
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:SF66; PTHR11630:SF66; 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; PR01660; MCMPROTEIN4.
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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Chromosome; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..863
FT /note="DNA replication licensing factor mcm4"
FT /id="PRO_0000240595"
FT DOMAIN 458..667
FT /note="MCM"
FT /evidence="ECO:0000255"
FT ZN_FING 306..331
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 642..645
FT /note="Arginine finger"
FT COMPBIAS 46..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 510..517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 863 AA; 97196 MW; 2AAFF32FE85BE97B CRC64;
MSSPTSTPSR RRNKRGRGSN PPTPHGEEVQ SPPSQRRRTE DSTSIGELLP MPTSPSGDLQ
SPSGQELMFS SPAPSRHSAL QSELDLSSPL TYGTPSSRVE GTPRSGIRGT PARQRPDLGS
ARKVKQVDLH SDQPAAEELV TSEQSLGQKL VIWGTDVNVA TCKEKFQRFV QRFIDPLAKE
EENVGLDLNE PIYMQRLEEI NVVGEPFLNV DCDHLRSFDQ DLYRQLVCYP QEVIPTFDMA
ANEIFFERYP DSILEHQIQV RPYNALKTRN MRSLNPEDID QLITISGMVI RTSQIIPEMQ
EAFFKCQVCA FTTRVEIDRG RISEPSVCKH CNTTHSMALI HNRSMFSDKQ MIKLQESPED
MPAGQTPHTT ILYGHNDLVD KVQPGDRVNV TGIYRAVPIR VNPRVRNVKS VYKTHIDVIH
YRKTDAKRLH GIDEDTEQKM FTEERVAMLK ELAAKPDIYE RLASALAPSI YEHEDIKKGI
LLQLFGGTRK DFSHTGRGKF RAEVNILLCG DPGTSKSQLL QYVYNLVPRG QYTSGKGSSA
VGLTAYVMKD PETRQLVLQT GALVLSDNGI CCIDEFDKMN ESTRSVLHEV MEQQTLSIAK
AGIICQLNAR TSVLAAANPV ESQWNPKKTT IENIQLPHTL LSRFDLIFLM LDPQDETYDR
RLAHHLVALY YQSEEQMKEE HLDMAVLKDY IAYARTYVNP RLGEEASQAL IEAYVDMRKI
GSGRGMVSAY PRQLESLIRL SEAHAKVRFS SKVETIDVEE AKRLHREALK QSATDPRTGI
VDISILTTGM SATARKRKEE LAQVLKKLIQ SKGKTPALKY QQLFEDLRGQ SDAAVTKDMF
DEALHALADE DYLTVTGKTV RLL
