MCM7_BOVIN
ID MCM7_BOVIN Reviewed; 719 AA.
AC Q3ZBH9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=DNA replication licensing factor MCM7;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q61881};
GN Name=MCM7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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. Required for S-phase
CC checkpoint activation upon UV-induced damage.
CC {ECO:0000250|UniProtKB:P33993}.
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. The complex forms a toroidal
CC hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-
CC MCM3-MCM5. Interacts with the ATR-ATRIP complex and with RAD17.
CC Interacts with TIPIN. Interacts with MCMBP. Interacts with ANKRD17.
CC Component of the replisome complex composed of at least DONSON, MCM2,
CC MCM7, PCNA and TICRR (By similarity). Component of the CMG helicase
CC complex, composed of the MCM2-7 complex, the GINS complex and CDC45 (By
CC similarity). {ECO:0000250|UniProtKB:P33993,
CC ECO:0000250|UniProtKB:Q91876}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91876}.
CC Chromosome {ECO:0000250|UniProtKB:Q91876}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250|UniProtKB:Q91876}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250|UniProtKB:P33993}.
CC -!- PTM: Ubiquitinated by traip when forks converge following formation of
CC DNA interstrand cross-links. Short ubiquitin chains on MCM7 promote
CC recruitment of DNA glycosylase NEIL3. If the interstrand cross-link
CC cannot be cleaved by NEIL3, the ubiquitin chains continue to grow on
CC MCM7, promoting the unloading of the CMG helicase complex by the
CC VCP/p97 ATPase. {ECO:0000250|UniProtKB:Q91876}.
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; BC103287; AAI03288.1; -; mRNA.
DR RefSeq; NP_001020516.2; NM_001025345.2.
DR AlphaFoldDB; Q3ZBH9; -.
DR SMR; Q3ZBH9; -.
DR IntAct; Q3ZBH9; 1.
DR STRING; 9913.ENSBTAP00000003728; -.
DR PaxDb; Q3ZBH9; -.
DR PeptideAtlas; Q3ZBH9; -.
DR PRIDE; Q3ZBH9; -.
DR Ensembl; ENSBTAT00000003728; ENSBTAP00000003728; ENSBTAG00000030965.
DR GeneID; 539924; -.
DR KEGG; bta:539924; -.
DR CTD; 4176; -.
DR VEuPathDB; HostDB:ENSBTAG00000030965; -.
DR VGNC; VGNC:31313; MCM7.
DR eggNOG; KOG0482; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; Q3ZBH9; -.
DR OMA; NAYTCDR; -.
DR OrthoDB; 266497at2759; -.
DR TreeFam; TF300400; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000030965; Expressed in nasopharynx and 111 other tissues.
DR ExpressionAtlas; Q3ZBH9; baseline.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
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; ISS:AgBase.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:AgBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; ISS:AgBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:AgBase.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0006270; P:DNA replication initiation; 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:AgBase.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0042325; P:regulation of phosphorylation; ISS:AgBase.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cell cycle; Chromosome; DNA replication;
KW DNA-binding; Glycoprotein; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT CHAIN 2..719
FT /note="DNA replication licensing factor MCM7"
FT /id="PRO_0000238630"
FT DOMAIN 332..538
FT /note="MCM"
FT REGION 521..564
FT /note="Interaction with RAD17"
FT /evidence="ECO:0000250"
FT REGION 577..719
FT /note="Interaction with ATRIP"
FT /evidence="ECO:0000250"
FT MOTIF 513..516
FT /note="Arginine finger"
FT BINDING 381..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P33993"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P33993"
SQ SEQUENCE 719 AA; 81315 MW; B1EC2501A196B2AE CRC64;
MALKDYVLEK DKVKKFLQEF YQDDESGKKQ FKYGNQLVQL AHREQVAMYV DLDDIAEDDP
ELVDSICENT KRYARLFADA VQELLPQYKE REVVNKDVLD VYIEHRLMME QRSRDPGAAR
SPQNQYPPEL MRRFELYFQG PSSNKPRVIR EVRADSVGKL VTVRGIVTRV SEVKPRMVVA
TYTCDQCGAE TYQPIQSPTF MPLIMCPSQE CQTNRSGGRL YLQTRGSKFI KFQEMKMQEH
SDQVPVGNIP RSITVLVEGE NTRIAQPGDH VSVTGIFLPI LRTGFRQMVQ GLLSETYLEA
HRIVKMSKSE EDESGAGELT REELRQITEE DFYEKLAASI APEIYGHEDV KKALLLLLVG
GVDQSPRGMK IRGNINICLM GDPGVAKSQL LSYIDRLAPR SQYTTGRGSS GVGLTAAVLR
DSVSGELTLE GGALVLADQG VCCIDEFDKM AEADRTAIHE VMEQQTISIA KAGILTTLNA
RCSILAAANP AYGRYNPRRS LEQNIQLPAA LLSRFDLLWL IQDRPDRDND LRLAQHITYV
HQHSRQPPAQ FEPLDMKLMR RYIAMCREKQ PAVPESLADY ITAAYVEMRR EAWASKDATY
TSARTLLAIL RLSTALARLR MVDTVEKEDV NEAIRLMEMS KDSLLGDKGQ TARTQRPADV
IFATVRELVS EGQSVRFSEA EQRCISRGFT PAQFQAALDE YEELNVWQVN TARTRITFV
