MCM9_RAT
ID MCM9_RAT Reviewed; 1124 AA.
AC F1M5F3;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=DNA helicase MCM9;
DE EC=3.6.4.12;
DE AltName: Full=Mini-chromosome maintenance deficient domain-containing protein 1;
DE AltName: Full=Minichromosome maintenance 9;
GN Name=Mcm9; Synonyms=Mcmdc1;
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).
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 MRN complex,
CC indirectly regulates the recruitment of downstream effector RAD51 to
CC DNA damage sites including DBSs and ICLs. Acts as a helicase in DNA
CC mismatch repair (MMR) following DNA replication errors to unwind the
CC mismatch containing DNA strand. In addition, recruits MLH1, a component
CC of the MMR complex, to chromatin. The MCM8-MCM9 complex is dispensable
CC for DNA replication and S phase progression. Probably by regulating HR,
CC plays a key role during gametogenesis. {ECO:0000250|UniProtKB:Q2KHI9,
CC ECO:0000250|UniProtKB:Q9NXL9}.
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:Q9NXL9};
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 MLH1; the interaction recruits MLH1 to chromatin. Interacts with
CC MSH2; the interaction recruits MCM9 to chromatin. Interacts with MSH6.
CC Interacts with the MRN complex composed of MRE11, RAD50 and NBN/NBS1;
CC the interaction recruits the MRN complex to DNA damage sites. Interacts
CC with RAD51; the interaction recruits RAD51 to DNA damage sites.
CC {ECO:0000250|UniProtKB:Q9NXL9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NXL9}.
CC Chromosome {ECO:0000250|UniProtKB:Q9NXL9}. Note=Colocalizes to nuclear
CC foci with RPA1 following DNA damage. Localizes to double-stranded DNA
CC breaks. Recruited to chromatin by MSH2. {ECO:0000250|UniProtKB:Q9NXL9}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR AlphaFoldDB; F1M5F3; -.
DR SMR; F1M5F3; -.
DR STRING; 10116.ENSRNOP00000004499; -.
DR PaxDb; F1M5F3; -.
DR RGD; 1305582; Mcmdc1.
DR eggNOG; KOG0477; Eukaryota.
DR InParanoid; F1M5F3; -.
DR PRO; PR:F1M5F3; -.
DR Proteomes; UP000002494; Unplaced.
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; 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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
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:0007276; P:gamete generation; ISS:UniProtKB.
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; Chromosome; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1124
FT /note="DNA helicase MCM9"
FT /id="PRO_0000419476"
FT DOMAIN 300..505
FT /note="MCM"
FT REGION 657..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXL9"
SQ SEQUENCE 1124 AA; 124125 MW; AA7130F096924CB3 CRC64;
MNSEQVTLVG QVFESYVSEY HKNDILLILK ERDEDAHYPL VVNAMTLFET NMEIGDYFTV
FPNEVLTVFD SALRRSALAV LQSLPEPEGL SMKQNLHARI SGLPVCPELV REHIPKTKDV
GHFLSVTGTV IRTSLVKVLE FERDYMCNKC KYVFTVKADF EQYYTFSRPS SCPSSDTCDS
SKFTCLSDLS ASPARCRDYQ EIKIQEQVQR LSVGSIPRSM KVILEDDLVD SCKSGDDLTI
YGVVMQRWKP FQRDMRCEVE IVLKANYVQV NNEQSSGMVM DEDARKEFED FWEHYKSDPF
AGRNEILASL CPQVFGMYLV KLAVAMVLAG GIQRTDAAGT RVRGESHLLL VGDPGTGKSQ
FLKYAAKITP RSVLTTGIGS TSAGLTVTAV KDSGEWNLEA GALVLADAGL CCIDEFNSLK
EHDRTSIHEA MEQQTISVAK AGLVCKLNTR TTILAATNPK GQYDPQESVS VNIALGSPLL
SRFDLILVLL DTRNEDWDRI ISSFILENKG YPSKSENLWS MEKMKTYFCL IRNLHPTLSD
VSNQVLLRYY QMQRQSDSRN AARTTIRLLE SLIRLAEAHA RLMFRSTVTL EDAITVVSVM
ESSMQGGALL GGVNALHTSF PESPRAQYRR QCELILEKLE LQSLLQEELR RLERLQNESD
QCQPHSPEVE AAPGSCRNDP RDRPGLRTPT QQEQSCSWSP AESSGGDSPT GPGLSRPTSC
NHKAEDGGGR GDCLAWADPT ASPEIAQEST IVSPGLKTME EKEDLKISNN GAQGKGKHGL
QKRSQLLKPG RLPASGATDT SLRSRGSEST RARQAAVVSE AGRDDDQESG PRRLPRLLKE
GSQSVCTTRV RTLPPTVPFP LSISPPGPGK KTGTPKRKRQ KSAQVEAPGP EGTETMSAPV
VKLAKFTFKQ KSKLTHSPEG QGPMPPSASK VAVDSSKIPR QRTRREAGVP AAGPGQSTST
SGDRCSEQLQ GQTKALSRQP PESHRPREEK EQGPERRVIQ SELELGSQAG HSHPACKKDR
KEGASCSNKS KVHAGTMARL ANFSFTSPPE SKSESLPPER KESRDRSHNP PATTAPVLGQ
QRQSFQLQQP PERVNLSTLS LFTLSELDDE ALDFDWDEEM RKKP
