MCM8_RAT
ID MCM8_RAT Reviewed; 830 AA.
AC D3ZVK1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=DNA helicase MCM8;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9UJA3};
DE AltName: Full=Minichromosome maintenance 8;
GN Name=Mcm8;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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.
CC -!- FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in the
CC repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-
CC links (ICLs) by homologous recombination (HR). Required for DNA
CC resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the
CC MRN complex to the repair site and by promoting the complex nuclease
CC activity. Probably by regulating the localization of the MNR complex,
CC indirectly regulates the recruitment of downstream effector RAD51 to
CC DNA damage sites including DBSs and ICLs. The MCM8-MCM9 complex is
CC dispensable for DNA replication and S phase progression. However, may
CC play a non-essential for DNA replication: may be involved in the
CC activation of the prereplicative complex (pre-RC) during G(1) phase by
CC recruiting CDC6 to the origin recognition complex (ORC). Probably by
CC regulating HR, plays a key role during gametogenesis. Stabilizes MCM9
CC protein. {ECO:0000250|UniProtKB:Q9CWV1, ECO:0000250|UniProtKB:Q9UJA3}.
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:Q9UJA3};
CC -!- SUBUNIT: Component of the MCM8-MCM9 complex, which forms a hexamer
CC composed of MCM8 and MCM9. Interacts with the DNA mismatch repair (MMR)
CC complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1. Interacts
CC with RAD51; the interaction recruits RAD51 to DNA damage sites.
CC Interacts with the MRN complex composed of MRE11, RAD50 and NBN/NBS1.
CC Interacts with CDC6 and ORC2. Interacts with HROB; the interaction
CC recruits the MCM8-MCM9 complex to DNA damage sites (By similarity).
CC {ECO:0000250|UniProtKB:Q9UJA3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJA3}.
CC Chromosome {ECO:0000250|UniProtKB:Q9UJA3}. Note=Localizes to nuclear
CC foci. Localizes to double-stranded DNA breaks. Binds chromatin
CC throughout the cell cycle. {ECO:0000250|UniProtKB:Q9UJA3}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; CH473949; EDL80275.1; -; Genomic_DNA.
DR RefSeq; NP_001099984.1; NM_001106514.1.
DR RefSeq; XP_006235136.1; XM_006235074.3.
DR RefSeq; XP_008760385.1; XM_008762163.2.
DR AlphaFoldDB; D3ZVK1; -.
DR SMR; D3ZVK1; -.
DR STRING; 10116.ENSRNOP00000028898; -.
DR PaxDb; D3ZVK1; -.
DR PRIDE; D3ZVK1; -.
DR Ensembl; ENSRNOT00000028898; ENSRNOP00000028898; ENSRNOG00000021272.
DR GeneID; 296178; -.
DR KEGG; rno:296178; -.
DR CTD; 84515; -.
DR RGD; 1305218; Mcm8.
DR eggNOG; KOG0480; Eukaryota.
DR GeneTree; ENSGT01050000244972; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; D3ZVK1; -.
DR OMA; THTVDWQ; -.
DR OrthoDB; 266497at2759; -.
DR TreeFam; TF323155; -.
DR Reactome; R-RNO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-RNO-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-RNO-68949; Orc1 removal from chromatin.
DR Reactome; R-RNO-68962; Activation of the pre-replicative complex.
DR PRO; PR:D3ZVK1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000021272; Expressed in testis and 19 other tissues.
DR Genevisible; D3ZVK1; RN.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0097362; C:MCM8-MCM9 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:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0032406; F:MutLbeta complex binding; ISO:RGD.
DR GO; GO:0032407; F:MutSalpha complex binding; ISO:RGD.
DR GO; GO:0032408; F:MutSbeta complex binding; ISO:RGD.
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:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0007292; P:female gamete generation; ISS:UniProtKB.
DR GO; GO:0048232; P:male gamete generation; ISS:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0036298; P:recombinational interstrand cross-link repair; ISO:RGD.
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; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
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; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Chromosome; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..830
FT /note="DNA helicase MCM8"
FT /id="PRO_0000419471"
FT DOMAIN 392..599
FT /note="MCM"
FT BINDING 444..451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA3"
SQ SEQUENCE 830 AA; 91977 MW; 0A131A878F0204C9 CRC64;
MSGAYRGRGF GRGRFQNWKR GRGGGNFSGR WRDRTDLSKA AGNHASEQAS QPLLQQSTLD
QFIPYKGWKL YFSEVYSNNS PLTEKIQAFE KFFTRHIDLY DKDEIERKGS ILVDFKELTK
DNEITNLIPD IENALRDAPE KTLACMGLAI HQVLTKDLER HAAELQAQEG LCNGGGTMVN
VPHIYARVYN YEPLTHLKNI RATCYGKYIS IRGTVVRVSN IKPLCTKMAF QCAACGEIQS
FPLPDGKYNL PTKCPVPACR GRSFTPLRSS PLTVTMDWQL IKIQELMSDA QREAGRIPRT
IECELVHDLV DSCVPGDTVT VTGIVKVSNS EEGSRSKNDK CMFLLYIEAN SVSNSKGQKA
QTAEDGCKHG TLMEFSLKDL YAIQEIQAEE NLLKLIVNSL CPVIFGHELV KAGLMLALFG
GSQKYADDKN RIPIRGDPHV LIVGDPGLGK SQMLQAACNV APRGVYVCGN TATSSGLTVT
LSKDSSSGDF ALEAGALVLG DQGICGIDEF DKMGNQHQAL LEAMEQQSIS LAKAGVVCSL
PARTSIIAAA NPVGGHYNKA RTVSENLKMG SALLSRFDLV FILLDTPNEQ HDHLLSEHVI
AIRAGKQRAV SSATVSRVLS QDSNTSVLEV VSEKPLSERL KVAPGEKTDP IPHQLLRKYI
GYARQYVHPR LSTEAAQALQ DFYLELRKQS QRVGSSPITT RQLESLIRLT EARARLELRE
EATKEDAEDI IEIMKHSMLG TYSDEFGNLD FERSQHGSGM SNRSTAKRFI SALNSIAERT
YNNIFQFHQL RQIAKELNIQ VADFENFIGS LNDQGYLLKK GPKIYQLQTM
