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DNA helicase MCM9 (EC 3.6.4.12) (Mini-chromosome maintenance deficient domain-containing protein 1) (Minichromosome maintenance 9)

 MCM9_MOUSE              Reviewed;        1134 AA.
Q2KHI9; Q3V370; Q6P6J6; Q9D344;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 2.
20-JUN-2018, entry version 100.
RecName: Full=DNA helicase MCM9;
EC=3.6.4.12;
AltName: Full=Mini-chromosome maintenance deficient domain-containing protein 1;
AltName: Full=Minichromosome maintenance 9;
Name=Mcm9; Synonyms=Mcmdc1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-1134 (ISOFORMS 1/2).
TISSUE=Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Colon;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
IDENTIFICATION.
PubMed=16226853; DOI=10.1016/j.gene.2005.07.031;
Lutzmann M., Maiorano D., Mechali M.;
"Identification of full genes and proteins of MCM9, a novel,
vertebrate-specific member of the MCM2-8 protein family.";
Gene 362:51-56(2005).
[5]
IDENTIFICATION, AND INDUCTION.
PubMed=15850810; DOI=10.1016/j.bbrc.2005.03.222;
Yoshida K.;
"Identification of a novel cell-cycle-induced MCM family protein
MCM9.";
Biochem. Biophys. Res. Commun. 331:669-674(2005).
[6]
FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 3) DISRUPTION
PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=21987787; DOI=10.1073/pnas.1113524108;
Hartford S.A., Luo Y., Southard T.L., Min I.M., Lis J.T.,
Schimenti J.C.;
"Minichromosome maintenance helicase paralog MCM9 is dispensible for
DNA replication but functions in germ-line stem cells and tumor
suppression.";
Proc. Natl. Acad. Sci. U.S.A. 108:17702-17707(2011).
[7]
FUNCTION, IDENTIFICATION IN THE MCM8-MCM9 COMPLEX, AND DISRUPTION
PHENOTYPE.
PubMed=22771120; DOI=10.1016/j.molcel.2012.05.048;
Lutzmann M., Grey C., Traver S., Ganier O., Maya-Mendoza A.,
Ranisavljevic N., Bernex F., Nishiyama A., Montel N., Gavois E.,
Forichon L., de Massy B., Mechali M.;
"MCM8- and MCM9-deficient mice reveal gametogenesis defects and genome
instability due to impaired homologous recombination.";
Mol. Cell 47:523-534(2012).
-!- FUNCTION: Component of the MCM8-MCM9 complex, a complex involved
in homologous recombination repair following DNA interstrand
cross-links and plays a key role during gametogenesis. The MCM8-
MCM9 complex probably acts as a hexameric helicase downstream of
the Fanconi anemia proteins BRCA2 and RAD51 and is required to
process aberrant forks into homologous recombination substrates
and to orchestrate homologous recombination with resection, fork
stabilization and fork restart. {ECO:0000269|PubMed:21987787,
ECO:0000269|PubMed:22771120}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Component of the MCM8-MCM9 complex, which forms a hexamer
composed of MCM8 and MCM9. {ECO:0000269|PubMed:22771120}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to
nuclear foci and colocalizes with RAD51. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Mcm9(L);
IsoId=Q2KHI9-1; Sequence=Displayed;
Name=2;
IsoId=Q2KHI9-2; Sequence=VSP_028015;
Name=3; Synonyms=Mcm9(S);
IsoId=Q2KHI9-3; Sequence=VSP_028016, VSP_028017;
Note=Incomplete sequence.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:21987787}.
-!- INDUCTION: By E2F1 and serum stimulation.
{ECO:0000269|PubMed:15850810}.
-!- DISRUPTION PHENOTYPE: Females are viable but are sterile due to
defects in double-strand break repair during gametogenesis. Males
are not sterile and produce spermatozoa, but in much reduced
quantity. Female ovaries are completely devoid of oocytes, and
testes show a severe early proliferation defect of germ cells,
causing a retarded development of only a fraction of seminiferous
tubules that produce then apparently normal spermatozoa.
{ECO:0000269|PubMed:22771120}.
-!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC153949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC155941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC062185; AAH62185.2; -; mRNA.
EMBL; AK018494; BAB31238.1; -; mRNA.
EMBL; AK046636; BAE20656.1; -; mRNA.
EMBL; BN000883; CAJ70649.1; -; mRNA.
CCDS; CCDS23846.1; -. [Q2KHI9-2]
RefSeq; NP_082106.2; NM_027830.2. [Q2KHI9-2]
RefSeq; XP_017169586.1; XM_017314097.1. [Q2KHI9-1]
UniGene; Mm.278221; -.
ProteinModelPortal; Q2KHI9; -.
SMR; Q2KHI9; -.
STRING; 10090.ENSMUSP00000074978; -.
iPTMnet; Q2KHI9; -.
PhosphoSitePlus; Q2KHI9; -.
MaxQB; Q2KHI9; -.
PaxDb; Q2KHI9; -.
PeptideAtlas; Q2KHI9; -.
PRIDE; Q2KHI9; -.
Ensembl; ENSMUST00000075540; ENSMUSP00000074978; ENSMUSG00000058298. [Q2KHI9-2]
GeneID; 71567; -.
KEGG; mmu:71567; -.
UCSC; uc007fbq.1; mouse. [Q2KHI9-2]
UCSC; uc007fbs.1; mouse. [Q2KHI9-3]
CTD; 254394; -.
MGI; MGI:1918817; Mcm9.
eggNOG; KOG0477; Eukaryota.
eggNOG; COG1241; LUCA.
GeneTree; ENSGT00920000149094; -.
HOGENOM; HOG000169812; -.
HOVERGEN; HBG108122; -.
InParanoid; Q2KHI9; -.
KO; K10738; -.
OMA; VMCAPEK; -.
OrthoDB; EOG091G01CK; -.
PhylomeDB; Q2KHI9; -.
TreeFam; TF329421; -.
ChiTaRS; Mcm9; mouse.
PRO; PR:Q2KHI9; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000058298; -.
CleanEx; MM_MCM9; -.
ExpressionAtlas; Q2KHI9; baseline and differential.
Genevisible; Q2KHI9; MM.
GO; GO:0097362; C:MCM8-MCM9 complex; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
GO; GO:0007292; P:female gamete generation; IMP:UniProtKB.
GO; GO:0007276; P:gamete generation; IMP:UniProtKB.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR031327; MCM.
InterPro; IPR001208; MCM_dom.
InterPro; IPR033762; MCM_OB.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11630; PTHR11630; 1.
Pfam; PF00493; MCM; 1.
Pfam; PF17207; MCM_OB; 1.
PRINTS; PR01657; MCMFAMILY.
SMART; SM00382; AAA; 1.
SMART; SM00350; MCM; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50051; MCM_2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; DNA damage;
DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 1134 DNA helicase MCM9.
/FTId=PRO_0000304144.
DOMAIN 300 505 MCM.
NP_BIND 352 359 ATP. {ECO:0000255}.
MOD_RES 754 754 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NXL9}.
MOD_RES 795 795 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NXL9}.
VAR_SEQ 1 1 M -> MDQRTTRNGKYCDVEPVSRSNPAPCLRDPPLRRLVR
PKPRLQLPESRLSPCSRLPLADSSVRPGARPPASAPGRSPS
GRKVEAVRGSGSAGSSSPSEAEREQREEACAPPRKAAPSSG
RAHAPPPPTPRGSGWGDHGRSAVPATKTVRVEPYPPFKM
(in isoform 2). {ECO:0000305}.
/FTId=VSP_028015.
VAR_SEQ 385 386 LT -> TV (in isoform 3). {ECO:0000305}.
/FTId=VSP_028016.
VAR_SEQ 387 1134 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_028017.
CONFLICT 137 137 K -> R (in Ref. 3; BAB31238).
{ECO:0000305}.
CONFLICT 875 875 S -> T (in Ref. 2; AAH62185).
{ECO:0000305}.
CONFLICT 1050 1050 S -> P (in Ref. 2; AAH62185).
{ECO:0000305}.
CONFLICT 1063 1065 Missing (in Ref. 2; AAH62185).
{ECO:0000305}.
SEQUENCE 1134 AA; 125814 MW; 92E748317EB14832 CRC64;
MNSEQVTLVG QVFESYVSEY HKNDILLILK ERDEDAHYPV VVNAMSLFET NMEIGDYFTV
FPNEVLTVFD SALRRSALAI LQSLPETEGL SMKQNLHARI SGLPVCPELV REHIPKTKDV
GHFLSVTGTV IRTSLVKVLE FERDYMCNKC KHVFMVEADF EQYYTFSRPS SCPSLASCDS
SKFSCLSDLS SSPARCRDYQ EIKIQEQVQR LSVGSIPRSM KVILEDDLVD SCKSGDDLTI
YGVVMQRWKP FQRDVRCEVE IVLKANYVQV NNEQSSGMVM DEDTRKEFED FWEHYKSDPF
AGRNEILASL CPQVFGMYLV KLAVAMVLAG GIQRTDAAGT RVRGESHLLL VGDPGTGKSQ
FLKYAAKITP RSVLTTGIGS TSAGLTVTAV KDSGEWNLEA GALVLADAGL CCIDEFNSLK
EHDRTSIHEA MEQQTISVAK AGLVCKLNTR TTILAATNPK GQYDPKESVS VNIALGSPLL
SRFDLVLVLL DTRNEDWDRI ISSFILENKG YPSKSENLWS MEKMKTYFCL IRNLHPTLSE
VSNQVLLRYY QMQRQSDSRN AARTTIRLLE SLIRLAEAHA RLMFRSAVTL EDAVTAVSVM
ESSMQGGALL GGVNALHTSF PENPRAQYQR QCELILEKLE LQGLLQEELR RLERLQNESV
HQCQSHSLEE EVAPGSCRND PRDKPRLRTS TQQEQSCSWS STERSGADSP PGPGLNRPTS
CNNSAENRDG RGDGLDWLDP TSSPEIAPES TIVSPNVKTT EKNVNLKISN NKSQGKEKHG
PQQRSKLLEA GHLPSSGAMN APLRSHGVKR TKASQAVVVS EAGRGDEEDS VPRRLPKLLK
EGSQNVCRST TRVRPLPPTV PLSLSIPSPG SGKRSGTPKR KRRKSAQVEE PEPEGMETPT
VKLAKFTFKQ KTKLTHSPEG QGPIPPSASE IAVDSSKIPQ QRTRREAAVP VVAPGKSTST
SGDRCSDQLH GKTKELSRQP PDSNPPREER EQGPKRRVIQ PKPELGNQAG HSHLACEKDR
KEGVSCGNKS SKVHAGTIAR LASFSFTSPS ESKSESLPPE RKDSRDSRDS RDSRDRCHSP
PATTAPVLGQ QRQTFQLQQP TERANLSTLS LFTLSELDDE ALDFDWEEEM RKKP


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