MCM3_BOVIN
ID MCM3_BOVIN Reviewed; 808 AA.
AC A4FUD9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA replication licensing factor MCM3;
DE EC=3.6.4.12;
GN Name=MCM3;
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 (APR-2006) 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 DNA
CC replication and cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:P49739}.
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. The complex forms a toroidal
CC hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-
CC MCM3-MCM5 (By similarity). Associated with the replication-specific DNA
CC polymerase alpha (By similarity). Interacts with MCMBP. Interacts with
CC ANKRD17 (By similarity). Interacts with MCM3AP; this interaction leads
CC to MCM3 acetylation (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:P25205,
CC ECO:0000250|UniProtKB:P25206, ECO:0000250|UniProtKB:P49739}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49739}.
CC Chromosome {ECO:0000250|UniProtKB:P49739}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250|UniProtKB:P49739}.
CC -!- PTM: Acetylated by MCM3AP. {ECO:0000250|UniProtKB:P25205}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; BC114737; AAI14738.1; -; mRNA.
DR RefSeq; NP_001013604.2; NM_001013586.2.
DR AlphaFoldDB; A4FUD9; -.
DR SMR; A4FUD9; -.
DR STRING; 9913.ENSBTAP00000014194; -.
DR PaxDb; A4FUD9; -.
DR PRIDE; A4FUD9; -.
DR Ensembl; ENSBTAT00000014194; ENSBTAP00000014194; ENSBTAG00000010721.
DR GeneID; 281302; -.
DR KEGG; bta:281302; -.
DR CTD; 4172; -.
DR VEuPathDB; HostDB:ENSBTAG00000010721; -.
DR VGNC; VGNC:31309; MCM3.
DR eggNOG; KOG0479; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR InParanoid; A4FUD9; -.
DR OMA; NVYPQED; -.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000010721; Expressed in nasopharynx and 108 other tissues.
DR ExpressionAtlas; A4FUD9; baseline and differential.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
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:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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: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; IEA:Ensembl.
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 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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cell cycle; Chromosome; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT CHAIN 2..808
FT /note="DNA replication licensing factor MCM3"
FT /id="PRO_0000318902"
FT DOMAIN 295..502
FT /note="MCM"
FT REGION 662..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 477..480
FT /note="Arginine finger"
FT COMPBIAS 681..707
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 293
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25206"
FT MOD_RES 535
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 547
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25206"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 708
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 713
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 722
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25206"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25206"
SQ SEQUENCE 808 AA; 90858 MW; 4344BE9A95678C9C CRC64;
MAGTVVLDDV ELREAQRDYL DFLDDEEDQG IYQSKVRELI SDNQYRLIVN VNDLRRKNEK
RANRLLSNAF EELVAFQRAL KDFVASIDAT YAKQYEEFYI GLEGSFGSKH VSPRTLTSCF
LSCVVCVEGI VTKCSLVRPK VVRSVHYCPA TKKTIERRYS DLTSLVAFPS SSVYPTKDEE
NNPLETEYGL SVYKDHQIIT IQEMPEKAPA GQLPRSVDVI LDDDLVDRVK PGDRVQVVGT
YRCLPGKKGG YTSGTFRTVL IACNVKQMSK DVQPSFSAED IAKIKKFSKT RSKDIFDQLA
RSLAPSIHGH DYVKKAILCL LLGGVERDLE NGSHIRGDIN ILLIGDPSVA KSQLLRYVLC
TAPRAIPTTG RGSSGVGLTA AVTTDQETGE RRLEAGAMVL ADRGVVCIDE FDKMSDMDRT
AIHEVMEQGR VTIAKAGIHA RLNARCSVLA AANPVYGRYD QYKTPMENIG LQDSLLSRFD
LLFIMLDQMD PEQDREISDH VLRMHRYRAP GEQDGDAMPL GSAVDILATD DPNFSPDDQQ
DTQIYEKHDN LLHGIKKKKE KMVSAAFMRK YIHVAKIIKP VLTQESAAYI AEEYSRLRSQ
DSMSSDTART SPVTARTLET LIRLATAHAK ARMSKTVDLQ DAEEAVELVQ YAYFKKVLEK
EKKRKKRSED ESDAEDEVEK SQEDQEQKTK RRRICPSDAK EGDSYDPYDF TNTEEEMPQV
HTPKATDSQE TKESQKVELS ESRLKAFKAA LLEVFREAHA QSVGMNRLTE SVNRDNEEPF
SSAEIQAALS RMQDDNQVMV SEGIVFLI
