位置:首页 > 蛋白库 > MUS81_RAT
MUS81_RAT
ID   MUS81_RAT               Reviewed;         551 AA.
AC   Q4KM32;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Crossover junction endonuclease MUS81;
DE            EC=3.1.22.-;
GN   Name=Mus81;
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 MRNA].
RC   TISSUE=Thymus;
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).
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:0000250|UniProtKB:Q96NY9}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: May self-associate. Interacts with EME1, EME2 and CHEK2.
CC       Interacts with BLM, and this interaction may stimulate the endonuclease
CC       activity of MUS81. 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. Interacts with RECQL5; this interaction
CC       stimulates mitotic DNA synthesis (By similarity).
CC       {ECO:0000250|UniProtKB:Q96NY9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Note=Recruited to foci of DNA
CC       damage in S-phase cells. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC098853; AAH98853.1; -; mRNA.
DR   RefSeq; NP_001020816.1; NM_001025645.1.
DR   AlphaFoldDB; Q4KM32; -.
DR   SMR; Q4KM32; -.
DR   STRING; 10116.ENSRNOP00000028015; -.
DR   PaxDb; Q4KM32; -.
DR   PRIDE; Q4KM32; -.
DR   GeneID; 293678; -.
DR   KEGG; rno:293678; -.
DR   UCSC; RGD:1311957; rat.
DR   CTD; 80198; -.
DR   RGD; 1311957; Mus81.
DR   VEuPathDB; HostDB:ENSRNOG00000020617; -.
DR   eggNOG; KOG2379; Eukaryota.
DR   HOGENOM; CLU_014329_3_0_1; -.
DR   InParanoid; Q4KM32; -.
DR   OMA; WIKEWLD; -.
DR   OrthoDB; 738810at2759; -.
DR   PhylomeDB; Q4KM32; -.
DR   TreeFam; TF315113; -.
DR   Reactome; R-RNO-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR   Reactome; R-RNO-6783310; Fanconi Anemia Pathway.
DR   PRO; PR:Q4KM32; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020617; Expressed in testis and 19 other tissues.
DR   Genevisible; Q4KM32; RN.
DR   GO; GO:1905347; C:endodeoxyribonuclease complex; ISO:RGD.
DR   GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048257; F:3'-flap endonuclease activity; ISO:RGD.
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:RGD.
DR   GO; GO:0006281; P:DNA repair; ISO:RGD.
DR   GO; GO:0006302; P:double-strand break repair; ISO:RGD.
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:RGD.
DR   GO; GO:0031297; P:replication fork processing; ISO:RGD.
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:RGD.
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   2: Evidence at transcript level;
KW   DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW   Magnesium; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..551
FT                   /note="Crossover junction endonuclease MUS81"
FT                   /id="PRO_0000223636"
FT   DOMAIN          270..372
FT                   /note="ERCC4"
FT   REGION          85..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          231..255
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"
SQ   SEQUENCE   551 AA;  61903 MW;  3F42CC6A4E6559C1 CRC64;
     MAEPVRLGRK RPLPVCPNPL FVRWLTEWRD EAASRGRHTR FVFQKALRSL QRYPLPLRNG
     KEAKILQHFG DRLCRMLDER LKEHLASGGD HAPSSPSGKK RASKGPPAQV QGSSMPVPTQ
     PQAGSTNAGY WPAQNSGARE ILLQLYREHL NSDGHSFLTK EELLQKCAQK TPRVVPESSR
     PWPALRGLLH RNLVLRTHRP ARYALTPEGL ELAQKLAEAE GLSTLNTAFQ PEEHHEESPV
     PEAILSEPGT TEVGVQQRPL ELRPSEYRVL LCVDIGETRG AGHRPEMLRE LQRLRVPHTV
     RKLHVGDFVW VAQETRPRDP ERPGELVLDH IVERKRLDDL CSSIIDGRFR EQKFRLKRCG
     LGHRIYLVEE HGSVQNLSLP ESTLLQAVTN TQVIDGFFVK RTMDIKESAG YLALLTKGLE
     RLYQGHTLHS RPWGTPGDAE SEAKPSTNPL CSLLTFSDFN AEAVKNKAQS VREVFARQLM
     QVRGLSGEKA AALVDRYSTP ASLLAAYDAC ATTKEQEMLL STVKCGRLQR NLGPALSRTL
     YQLYCSHSPL T
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024