MCM8_CHICK
ID MCM8_CHICK Reviewed; 830 AA.
AC I0IUP3; E1BWN1; F1NEZ3; Q5F3V9;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=DNA helicase MCM8;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance 8;
GN Name=MCM8; ORFNames=RCJMB04_5o15;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN THE
RP MCM8-MCM9 COMPLEX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-452 AND
RP ARG-578.
RX PubMed=22771115; DOI=10.1016/j.molcel.2012.05.047;
RA Nishimura K., Ishiai M., Horikawa K., Fukagawa T., Takata M., Takisawa H.,
RA Kanemaki M.T.;
RT "Mcm8 and Mcm9 form a complex that functions in homologous recombination
RT repair induced by DNA interstrand crosslinks.";
RL Mol. Cell 47:511-522(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in
CC homologous recombination repair following DNA interstrand cross-links
CC and plays a key role during gametogenesis. The MCM8-MCM9 complex
CC probably acts as a hexameric helicase required to process aberrant
CC forks into homologous recombination substrates and to orchestrate
CC homologous recombination with resection, fork stabilization and fork
CC restart. {ECO:0000269|PubMed:22771115}.
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 MCM8-MCM9 complex, which forms a hexamer
CC composed of MCM8 and MCM9. {ECO:0000269|PubMed:22771115}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22771115}.
CC Note=Localizes to nuclear foci and colocalizes with RAD51.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=I0IUP3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=I0IUP3-2; Sequence=VSP_044192, VSP_044193, VSP_044194;
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; AB689140; BAM08992.1; -; mRNA.
DR EMBL; AJ851541; CAH65175.1; -; mRNA.
DR EMBL; AADN02012184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02012185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001280098.1; NM_001293169.1. [I0IUP3-1]
DR AlphaFoldDB; I0IUP3; -.
DR SMR; I0IUP3; -.
DR STRING; 9031.ENSGALP00000014959; -.
DR PaxDb; I0IUP3; -.
DR Ensembl; ENSGALT00000014975; ENSGALP00000014959; ENSGALG00000009195. [I0IUP3-1]
DR Ensembl; ENSGALT00000088103; ENSGALP00000059238; ENSGALG00000009195. [I0IUP3-2]
DR GeneID; 421314; -.
DR KEGG; gga:421314; -.
DR CTD; 84515; -.
DR VEuPathDB; HostDB:geneid_421314; -.
DR eggNOG; KOG0480; Eukaryota.
DR GeneTree; ENSGT01050000244972; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; I0IUP3; -.
DR OMA; THTVDWQ; -.
DR OrthoDB; 266497at2759; -.
DR Reactome; R-GGA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-GGA-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-GGA-68949; Orc1 removal from chromatin.
DR Reactome; R-GGA-68962; Activation of the pre-replicative complex.
DR PRO; PR:I0IUP3; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000009195; Expressed in spermatid and 13 other tissues.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0097362; C:MCM8-MCM9 complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA: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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; DNA damage; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..830
FT /note="DNA helicase MCM8"
FT /id="PRO_0000419472"
FT DOMAIN 394..601
FT /note="MCM"
FT BINDING 446..453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15642098"
FT /id="VSP_044192"
FT VAR_SEQ 505..548
FT /note="GICGIDEFDKMGSQHQALLEAMEQQSISLAKAGIVCSLPARTSI -> ESLF
FT CHWRNQDTASASQASCSNMKWKWTLLKGQLGPTSPAVSRI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15642098"
FT /id="VSP_044193"
FT VAR_SEQ 549..830
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15642098"
FT /id="VSP_044194"
FT MUTAGEN 452
FT /note="K->A: Loss of function; when associated with A-578."
FT /evidence="ECO:0000269|PubMed:22771115"
FT MUTAGEN 578
FT /note="R->A: Loss of function; when associated with A-452."
FT /evidence="ECO:0000269|PubMed:22771115"
FT CONFLICT I0IUP3-2:417
FT /note="W -> R (in Ref. 2; CAH65175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 92809 MW; 9E0B3F498832B541 CRC64;
MSRDLRGRGC PRGRGFQGWR GGWRGGWRGG WRGGWRGRTQ KVEWKRAPEP ASSRLVQSTL
DQFIPYKGWK LYFSEAYADK SPFVQKTQAF EKFFMQRIEL YDKDEIERKG SILVDYKELI
EDRELTKSIP NISTELRDMP QKILQCMGLA IHQVLTKDLE RHAAELQVQE GLPLDGEPII
NVPLIHARLY NYEPLTQLKN VRANCYGKYI ALRGTVVRVS NIKPLCTKLA FVCGTCGDVQ
SVPLPDGKYT LPTKCLVPEC RGRSFTPDRS SPLTATVDWQ SVKVQELMSD DQREAGRIPR
TIECELVQDL VDSCVPGDVV TITGVVKVSS TEEGASKNKN DKCVFLLYIE ANSVSNSKGQ
KTKNFEEETF QRSFMEFSLK DLYAVQEIQA EENLFRIIVN SLCPAIYGHE IVKAGLALAL
FGGCQKFVDD KNRIPVRGDP HVLIVGDPGL GKSQMLQAVC NVAPRGVYVC GNTSTSSGLT
VTLSRDGASG DFALEAGALV LGDQGICGID EFDKMGSQHQ ALLEAMEQQS ISLAKAGIVC
SLPARTSIVA AANPVGGHYN KAKTVSENLK MGSALLSRFD LVFILLDTPN EDHDHLLSEH
VMAIRAGKQA VCSSAVVSRT NVQDRSVLEV VSDRPLLERL KISPGENFDA IPHQLLRKYV
GYARQYVHPH LSPEAAQVLQ EFYLELRKQN QGASSTPITT RQLESLIRLT EARSRLELRE
KCTKEDAEDV IEIMKYSMLG TYSDEFGKLD FERSQHGSGM SNRSQAKRFV SALSSIAERT
YSNLFDLQQL RQVAKELQIR VFDFESFIES LNDQGYLLKK GSRLYQLQTM
