MCM6_RAT
ID MCM6_RAT Reviewed; 507 AA.
AC Q62724;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=DNA replication licensing factor MCM6;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P97311};
DE AltName: Full=Intestinal DNA replication protein;
DE Flags: Fragment;
GN Name=Mcm6; Synonyms=Mcmd6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holtzman; TISSUE=Intestine;
RX PubMed=7590274; DOI=10.1016/0378-1119(95)00297-j;
RA Sykes D.E., Weiser M.M.;
RT "Rat intestinal crypt-cell replication factor with homology to early S-
RT phase proteins required for cell division.";
RL Gene 163:243-247(1995).
RN [2]
RP SEQUENCE REVISION.
RA Sykes D.E.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:Q14566}.
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:P97311};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P97311};
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. May interact with MCM10. Interacts with TIPIN. Interacts
CC with CDT1. Interacts with MCMBP. Interacts with DDI2 (By similarity).
CC Component of the CMG helicase complex, composed of the MCM2-7 complex,
CC the GINS complex and CDC45 (By similarity).
CC {ECO:0000250|UniProtKB:Q14566, ECO:0000250|UniProtKB:Q5FWY4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14566}.
CC Chromosome {ECO:0000250|UniProtKB:Q14566}. Note=Binds to chromatin
CC during G1 and detach from it during S phase.
CC {ECO:0000250|UniProtKB:Q14566}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250|UniProtKB:Q14566}.
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:P97311}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U17565; AAC18424.1; -; mRNA.
DR PIR; T10753; T10753.
DR AlphaFoldDB; Q62724; -.
DR SMR; Q62724; -.
DR STRING; 10116.ENSRNOP00000004969; -.
DR iPTMnet; Q62724; -.
DR jPOST; Q62724; -.
DR PaxDb; Q62724; -.
DR PeptideAtlas; Q62724; -.
DR UCSC; RGD:61967; rat.
DR RGD; 61967; Mcm6.
DR eggNOG; KOG0480; Eukaryota.
DR InParanoid; Q62724; -.
DR PhylomeDB; Q62724; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:RGD.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISO:RGD.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902969; P:mitotic DNA replication; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR041024; Mcm6_C.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; PTHR11630; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF18263; MCM6_C; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00350; MCM; 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 Acetylation; ATP-binding; Cell cycle; Chromosome; DNA replication;
KW DNA-binding; Glycoprotein; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN <1..507
FT /note="DNA replication licensing factor MCM6"
FT /id="PRO_0000194115"
FT DOMAIN 32..239
FT /note="MCM"
FT REGION 365..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 214..217
FT /note="Arginine finger"
FT BINDING 82..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 329
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97311"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97311"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97311"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 477
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT NON_TER 1
SQ SEQUENCE 507 AA; 57370 MW; 03CE569FFFCDC654 CRC64;
LRDEEQTAES IKNQMTVKEW EKVFEMSQDQ NLYHNLCTSL FPTIHGNDEV KRGVLLMLFG
GVPKTTGEGT SLRGDINVCI VGDPSTAKSQ FLKHVDEFSP RAVYTSGKAS SASGLTAAVV
RDEESHEFVI EAGALMLADN GVCCIDEFDK MDMRDQVAIH EAMEQQTISI TKAGVKATLN
ARTSILAAAN PVSGHYDRSK SLKQNINLSA PIMSRFDLFF ILVDECNEVT DYAIARRIVD
LHSRIEESID RVYSLDDIRR YLLFARQFKP KISKESEDFI VEQYKRLRQR DGSGITKSSW
RITVRQLESM IRLSESMARM HCCDEVQPKH VKEAFRLLNK SIIRVETPDV NLDQEEEIQM
ETDEGPGGIN GHADSPAPVN GFNGSGEDAS QETVPKPSLR LAFAEYCRIS NLIVLHLRKM
EEEEDESALK RSELVNWYLK EIESEIDSEE ELINKKRIIE KVVHRLTHYD HVLIELTQAG
LKGSSEGSES YEEDPYLVVN PNYLLED
