MCM5_MOUSE
ID MCM5_MOUSE Reviewed; 734 AA.
AC P49718; Q52KC3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DNA replication licensing factor MCM5 {ECO:0000250|UniProtKB:P33992};
DE EC=3.6.4.12;
DE AltName: Full=CDC46 homolog {ECO:0000303|PubMed:7610039};
DE AltName: Full=P1-CDC46 {ECO:0000250|UniProtKB:P33992};
GN Name=Mcm5 {ECO:0000312|MGI:MGI:103197}; Synonyms=Cdc46, Mcmd5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7610039; DOI=10.1093/nar/23.12.2097;
RA Kimura H., Takizawa N., Nozaki N., Sugimoto K.;
RT "Molecular cloning of cDNA encoding mouse Cdc21 and CDC46 homologs and
RT characterization of the products: physical interaction between P1(MCM3) and
RT CDC46 proteins.";
RL Nucleic Acids Res. 23:2097-2104(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:P33992}.
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. Interacts with ANKRD17. Interacts with MCMBP (By
CC similarity). Component of the CMG helicase complex, composed of the
CC MCM2-7 complex, the GINS complex and CDC45 (By similarity). Interacts
CC with TONSL; the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P33992, ECO:0000250|UniProtKB:P55862}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P33992}.
CC Chromosome {ECO:0000250|UniProtKB:P55862}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P33992}. Note=Associated with chromatin before
CC the formation of nuclei and detaches from it as DNA replication
CC progresses. {ECO:0000250|UniProtKB:P55862}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05083.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D26090; BAA05083.1; ALT_FRAME; mRNA.
DR EMBL; AK133826; BAE21865.1; -; mRNA.
DR EMBL; AC084823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL10828.1; -; Genomic_DNA.
DR EMBL; CH466525; EDL10827.1; -; Genomic_DNA.
DR EMBL; CH466525; EDL10829.1; -; Genomic_DNA.
DR EMBL; BC094416; AAH94416.1; -; mRNA.
DR CCDS; CCDS22424.1; -.
DR PIR; S56767; S56767.
DR RefSeq; NP_001289469.1; NM_001302540.1.
DR RefSeq; NP_032592.2; NM_008566.3.
DR AlphaFoldDB; P49718; -.
DR SMR; P49718; -.
DR ComplexPortal; CPX-2941; MCM complex.
DR CORUM; P49718; -.
DR DIP; DIP-45875N; -.
DR IntAct; P49718; 5.
DR STRING; 10090.ENSMUSP00000126135; -.
DR iPTMnet; P49718; -.
DR PhosphoSitePlus; P49718; -.
DR SwissPalm; P49718; -.
DR EPD; P49718; -.
DR jPOST; P49718; -.
DR MaxQB; P49718; -.
DR PaxDb; P49718; -.
DR PeptideAtlas; P49718; -.
DR PRIDE; P49718; -.
DR ProteomicsDB; 295710; -.
DR ProteomicsDB; 342918; -.
DR Antibodypedia; 244; 923 antibodies from 38 providers.
DR DNASU; 17218; -.
DR Ensembl; ENSMUST00000164309; ENSMUSP00000126135; ENSMUSG00000005410.
DR Ensembl; ENSMUST00000212426; ENSMUSP00000148648; ENSMUSG00000005410.
DR Ensembl; ENSMUST00000212811; ENSMUSP00000148525; ENSMUSG00000005410.
DR GeneID; 17218; -.
DR KEGG; mmu:17218; -.
DR UCSC; uc009mhd.2; mouse.
DR CTD; 4174; -.
DR MGI; MGI:103197; Mcm5.
DR VEuPathDB; HostDB:ENSMUSG00000005410; -.
DR eggNOG; KOG0481; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; P49718; -.
DR OMA; ITYCKTR; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; P49718; -.
DR TreeFam; TF105653; -.
DR Reactome; R-MMU-176187; Activation of ATR in response to replication stress.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-68962; Activation of the pre-replicative complex.
DR Reactome; R-MMU-69052; Switching of origins to a post-replicative state.
DR BioGRID-ORCS; 17218; 23 hits in 72 CRISPR screens.
DR ChiTaRS; Mcm5; mouse.
DR PRO; PR:P49718; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P49718; protein.
DR Bgee; ENSMUSG00000005410; Expressed in urogenital fold and 251 other tissues.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISO:MGI.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008048; MCM5.
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; PR01661; MCMPROTEIN5.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell cycle; Chromosome; Cytoplasm;
KW DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P33992"
FT CHAIN 2..734
FT /note="DNA replication licensing factor MCM5"
FT /id="PRO_0000194108"
FT DOMAIN 331..537
FT /note="MCM"
FT MOTIF 512..515
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-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P33992"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33992"
FT MOD_RES 392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P33992"
FT MOD_RES 396
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P33992"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33992"
SQ SEQUENCE 734 AA; 82407 MW; 06B4DCABCECDD5D2 CRC64;
MSGFDDPGIF YSDSFGGDPG AEEGQARKSQ LQRRFKEFLR QYRVGTDRTG FTFKYRDELK
RHYNLGEYWI EVEMEDLASF DEELADHLHK QPAEHLQLLE EAAKEVADEV TRPRPAGDEL
LQDIQVMLKS DASPSSIRIL KSDMMSHLVK IPGIIISASA VRAKATRISI QCRSCHNTLT
NIAMRPGLEG YALPRKCNMD QAGRPKCPLD PYFIMPDKCK CVDFQTLKLQ ELPDAVPHGE
MPRHMQLYCD RYLCDKVVPG NRVTIMGIYS IKKFGLNPSK GRDRVGVGIR SSYIRVLGIQ
VDTDGSGRSF AGSVSPQEEE EFRRLAALPN IYELISKSIS PSIFGGMDMK KAIACLLFGG
SRKRLPDGLT RRGDINLLML GDPGTAKSQL LKFVEKCSPI GVYTSGKGSS AAGLTASVIR
DPSSRNFIME GGAMVLADGG VVCIDEFDKM REDDRVAIHE AMEQQTISIA KAGITTTLNS
RCSVLAAANS VFGRWDETKG EDNIDFMPTI LSRFDMIFIV KDEHNEERDM MLAKHVMTLH
VSALTQTQAV EGEIDLAKMK KFIAYCRARC GPRLSAEAAE KLKNRYIIMR SGARQHERDS
DRRSSIPITV RQLEAIVRIA EALSKMKLQP FATEADVEEA LRLFQVSTLD AALSGNLSGV
EGFTTQEDQE MLSRIEKQLK RRFAIGSQVS EHSIVQDFTK QKYPEHAIRK VLQLMLRRGE
IQHRMQRKVL YRLK
