MUS81_MOUSE
ID MUS81_MOUSE Reviewed; 551 AA.
AC Q91ZJ0; Q8R356;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Crossover junction endonuclease MUS81;
DE EC=3.1.22.-;
GN Name=Mus81;
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].
RC STRAIN=BALB/cJ;
RX PubMed=11741546; DOI=10.1016/s1097-2765(01)00375-6;
RA Chen X.-B., Melchionna R., Denis C.-M., Gaillard P.-H.L., Blasina A.,
RA Van de Weyer I., Boddy M.N., Russell P., Vialard J., McGowan C.H.;
RT "Human Mus81-associated endonuclease cleaves Holliday junctions in vitro.";
RL Mol. Cell 8:1117-1127(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [3]
RP FUNCTION, AND INTERACTION WITH EME1.
RX PubMed=14609959; DOI=10.1093/emboj/cdg580;
RA Abraham J., Lemmers B., Hande M.P., Moynahan M.E., Chahwan C., Ciccia A.,
RA Essers J., Hanada K., Chahwan R., Khaw A.K., McPherson P., Shehabeldin A.,
RA Laister R., Arrowsmith C., Kanaar R., West S.C., Jasin M., Hakem R.;
RT "Eme1 is involved in DNA damage processing and maintenance of genomic
RT stability in mammalian cells.";
RL EMBO J. 22:6137-6147(2003).
RN [4]
RP FUNCTION.
RX PubMed=15205536; DOI=10.1126/science.1094557;
RA McPherson J.P., Lemmers B., Chahwan R., Pamidi A., Migon E.,
RA Matysiak-Zablocki E., Moynahan M.E., Essers J., Hanada K., Poonepalli A.,
RA Sanchez-Sweatman O., Khokha R., Kanaar R., Jasin M., Hande M.P., Hakem R.;
RT "Involvement of mammalian Mus81 in genome integrity and tumor
RT suppression.";
RL Science 304:1822-1826(2004).
RN [5]
RP FUNCTION.
RX PubMed=16107704; DOI=10.1128/mcb.25.17.7569-7579.2005;
RA Dendouga N., Gao H., Moechars D., Janicot M., Vialard J., McGowan C.H.;
RT "Disruption of murine Mus81 increases genomic instability and DNA damage
RT sensitivity but does not promote tumorigenesis.";
RL Mol. Cell. Biol. 25:7569-7579(2005).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=27010503; DOI=10.1371/journal.pone.0152278;
RA Braun J., Meixner A., Brachner A., Foisner R.;
RT "The GIY-YIG type endonuclease ankyrin repeat and LEM domain-containing
RT protein 1 (ANKLE1) is dispensable for mouse hematopoiesis.";
RL PLoS ONE 11:E0152278-E0152278(2016).
CC -!- FUNCTION: Interacts with EME1 and EME2 to form a DNA structure-specific
CC endonuclease with substrate preference for branched DNA structures with
CC a 5'-end at the branch nick. Typical substrates include 3'-flap
CC structures, replication forks and nicked Holliday junctions. May be
CC required in mitosis for the processing of stalled or collapsed
CC replication forks. {ECO:0000269|PubMed:14609959,
CC ECO:0000269|PubMed:15205536, ECO:0000269|PubMed:16107704}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: May self-associate. Interacts with CHEK2. Interacts with BLM,
CC and this interaction may stimulate the endonuclease activity of MUS81.
CC Interacts with EME2. Interacts with SLX4/BTBD12; this interaction is
CC direct and links the MUS81-EME1 complex to SLX4, which may coordinate
CC the action of the structure-specific endonuclease during DNA repair.
CC Interacts with DCLRE1B/Apollo (By similarity). Interacts with EME1.
CC Interacts with RECQL5; this interaction stimulates mitotic DNA
CC synthesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:14609959}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Recruited to foci of DNA
CC damage in S-phase cells. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed highly in testis. Expressed also in bone
CC marrow, brain, thymus and to a lesser extent in heart and skeletal
CC muscle, colon, kidney and spleen. {ECO:0000269|PubMed:27010503}.
CC -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
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DR EMBL; AF425647; AAL28066.1; -; mRNA.
DR EMBL; BC026560; AAH26560.1; -; mRNA.
DR CCDS; CCDS29467.1; -.
DR RefSeq; NP_082153.3; NM_027877.3.
DR PDB; 2KP7; NMR; -; A=11-90.
DR PDBsum; 2KP7; -.
DR AlphaFoldDB; Q91ZJ0; -.
DR BMRB; Q91ZJ0; -.
DR SMR; Q91ZJ0; -.
DR BioGRID; 214873; 18.
DR ComplexPortal; CPX-585; Deoxyribonuclease complex MUS81-EME1.
DR ComplexPortal; CPX-587; Deoxyribonuclease complex MUS81-EME2.
DR IntAct; Q91ZJ0; 15.
DR STRING; 10090.ENSMUSP00000114895; -.
DR PhosphoSitePlus; Q91ZJ0; -.
DR EPD; Q91ZJ0; -.
DR MaxQB; Q91ZJ0; -.
DR PaxDb; Q91ZJ0; -.
DR PeptideAtlas; Q91ZJ0; -.
DR PRIDE; Q91ZJ0; -.
DR ProteomicsDB; 287332; -.
DR Antibodypedia; 16020; 198 antibodies from 25 providers.
DR Ensembl; ENSMUST00000124334; ENSMUSP00000114895; ENSMUSG00000024906.
DR GeneID; 71711; -.
DR KEGG; mmu:71711; -.
DR UCSC; uc008gdn.2; mouse.
DR CTD; 80198; -.
DR MGI; MGI:1918961; Mus81.
DR VEuPathDB; HostDB:ENSMUSG00000024906; -.
DR eggNOG; KOG2379; Eukaryota.
DR GeneTree; ENSGT00390000005498; -.
DR HOGENOM; CLU_014329_3_0_1; -.
DR InParanoid; Q91ZJ0; -.
DR OMA; WIKEWLD; -.
DR OrthoDB; 738810at2759; -.
DR PhylomeDB; Q91ZJ0; -.
DR TreeFam; TF315113; -.
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 71711; 25 hits in 107 CRISPR screens.
DR ChiTaRS; Mus81; mouse.
DR EvolutionaryTrace; Q91ZJ0; -.
DR PRO; PR:Q91ZJ0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91ZJ0; protein.
DR Bgee; ENSMUSG00000024906; Expressed in hindlimb stylopod muscle and 203 other tissues.
DR ExpressionAtlas; Q91ZJ0; baseline and differential.
DR Genevisible; Q91ZJ0; MM.
DR GO; GO:1905347; C:endodeoxyribonuclease complex; ISO:MGI.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central.
DR GO; GO:0043596; C:nuclear replication fork; IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048257; F:3'-flap endonuclease activity; ISO:MGI.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; ISO:MGI.
DR GO; GO:0006302; P:double-strand break repair; ISO:MGI.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0033687; P:osteoblast proliferation; ISO:MGI.
DR GO; GO:0031297; P:replication fork processing; ISO:MGI.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0072429; P:response to intra-S DNA damage checkpoint signaling; ISO:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 1.10.150.670; -; 1.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR042530; EME1/EME2_C.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR033309; Mus81.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR13451; PTHR13451; 2.
DR Pfam; PF02732; ERCC4; 1.
DR SMART; SM00891; ERCC4; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..551
FT /note="Crossover junction endonuclease MUS81"
FT /id="PRO_0000198859"
FT DOMAIN 270..372
FT /note="ERCC4"
FT REGION 84..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..244
FT /note="Interaction with BLM"
FT /evidence="ECO:0000250"
FT REGION 229..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96NY9"
FT CONFLICT 4
FT /note="P -> R (in Ref. 2; AAH26560)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="A -> D (in Ref. 2; AAH26560)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="P -> L (in Ref. 1; AAL28066)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="A -> V (in Ref. 1; AAL28066)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="A -> T (in Ref. 2; AAH26560)"
FT /evidence="ECO:0000305"
FT HELIX 20..35
FT /evidence="ECO:0007829|PDB:2KP7"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:2KP7"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:2KP7"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:2KP7"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:2KP7"
SQ SEQUENCE 551 AA; 61531 MW; 98A5EE72E656C684 CRC64;
MAEPVRLGRK RPLPVCPNPL FVRWLTEWRD EAASRGRHTR FVFQKALRSL QRYPLPLRSG
KEAKILQHFG DRLCRMLDEK LKQHLASGGD HAPSSPSGKK GASKGPPEQV QDSSMPVPTQ
PQAGSTSVGY WPAQNSGARE ILLQLYREHL NSDGHSFLTK EELLQKCAQK TPRVVPGSSK
PWPALRSLLH RNLILGTHRP ARYALTPEGL ELAQKLAEAE GLSTRHAGFR PEEHHGEDSA
VPEALSEPGT TEGAVQQRPL ELRPSEYRVL LCVDIGETRG AGHRPEMLRE LQRLRVPHTV
RKLHVGDFVW VAQETRPRDP ERPGELVLDH IVERKRLDDL CSSIIDGRFR EQKFRLKRCG
LGHRVYLVEE HGSVHNLSLP ESTLLQAVTN TQVIDGFFVK RTMDIKESAG YLALLTKGLE
RLYQGHTLRS RPWGAPGAAE SEAKPSTNPL CSLLTFSDFN AEAVKNKAQS VREVFARQLM
QVRGLSGEKA AAVVDRYSTP ASLLAAYDAC ATAKEQEMLL STIKCGRLQR NLGPALSRTL
YQLYCSHSPL S
