MCM3_PONAB
ID MCM3_PONAB Reviewed; 808 AA.
AC Q5R8G6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, 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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-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. 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: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250|UniProtKB:P25205}.
CC -!- PTM: Acetylated by MCM3AP. {ECO:0000250|UniProtKB:P25205}.
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; CR859786; CAH91944.1; -; mRNA.
DR RefSeq; NP_001126128.1; NM_001132656.1.
DR AlphaFoldDB; Q5R8G6; -.
DR SMR; Q5R8G6; -.
DR STRING; 9601.ENSPPYP00000018688; -.
DR GeneID; 100173085; -.
DR KEGG; pon:100173085; -.
DR CTD; 4172; -.
DR eggNOG; KOG0479; Eukaryota.
DR InParanoid; Q5R8G6; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0042555; C:MCM complex; ISS: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 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; Glycoprotein; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; 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_0000318903"
FT DOMAIN 295..502
FT /note="MCM"
FT REGION 662..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 477..480
FT /note="Arginine finger"
FT COMPBIAS 682..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..738
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 674
FT /note="Phosphothreonine"
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 711
FT /note="Phosphoserine"
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 725
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; 90999 MW; 50411B0117A921CB CRC64;
MAGTVVLDDV ELREAQRDYL DFLDDEEDQG IYQSKVRELI SDNQYRLIVN VNDLRRKNEK
RANRLLNNAF EELVAFQRAL KDFVASIDAT YAKQYEEFYV GLEGSFGSKH VSPRTLTSCF
LSCVVCVEGI VTKCSLVRPK VVRSVHYCPA TKKTIERRYS DLTTLVAFPS SSVYPTKDEE
NNPLETEYGL SVYKDHQTIT IQEMPEKAPA GQLPRSVDVI LDDDLVDKAK PGDRVQVVGT
YRCLPGKKGG YTSGTFRTVL IACNVKQMSK DAQPSFSAED 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 DPNFSQEDQQ
DTQIYEKHDN LLHGTKKKKE KMVSAAFMKK YIHVAKIIKP VLTQESATYI AEEYSRLRSQ
DSMSSDTART SPVTARTLET LIRLATAHAK ARMSKTVDLQ DAEEAVELVQ YAYFKKVLEK
EKKRKKRSED ESETEDEEEK SQEDQEQKRK RRKTRQSDAK DGDSYDPYDF SDTEEEMPQV
HTPKTADSQE TKESQKVELS ESRLKAFKVA LLDVFREAHA QSIGMNRLTE SINRDSEEPF
SSVEIQAALS KMQDDNQVMV SEGIIFLI
