RMI1_MOUSE
ID RMI1_MOUSE Reviewed; 616 AA.
AC Q9D4G9; Q8C560; Q8CI20;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=RecQ-mediated genome instability protein 1;
GN Name=Rmi1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, Testis, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; 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).
CC -!- FUNCTION: Essential component of the RMI complex, a complex that plays
CC an important role in the processing of homologous recombination
CC intermediates to limit DNA crossover formation in cells. Promotes TOP3A
CC binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-
CC mediated dissolution. Required for BLM phosphorylation during mitosis.
CC Within the BLM complex, required for BLM and TOP3A stability (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the RMI complex, containing at least TOP3A, RMI1
CC and RMI2. The RMI complex interacts with BLM. Directly interacts with
CC RMI2 and TOP3A. May bind DHJ. Interacts (via N-terminal region) with
CC BLM; the interaction is direct (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Forms foci in
CC response to DNA damage. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RMI1 family. {ECO:0000305}.
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DR EMBL; AK016542; BAB30292.1; -; mRNA.
DR EMBL; AK032229; BAC27772.1; -; mRNA.
DR EMBL; AK079457; BAC37651.1; -; mRNA.
DR EMBL; BC037694; AAH37694.1; -; mRNA.
DR CCDS; CCDS26571.1; -.
DR RefSeq; NP_001161720.1; NM_001168248.1.
DR RefSeq; NP_083180.3; NM_028904.3.
DR RefSeq; XP_006517483.1; XM_006517420.3.
DR AlphaFoldDB; Q9D4G9; -.
DR SMR; Q9D4G9; -.
DR BioGRID; 216710; 9.
DR ComplexPortal; CPX-3303; BTR double Holliday Junction dissolution complex.
DR IntAct; Q9D4G9; 6.
DR STRING; 10090.ENSMUSP00000041035; -.
DR iPTMnet; Q9D4G9; -.
DR PhosphoSitePlus; Q9D4G9; -.
DR EPD; Q9D4G9; -.
DR jPOST; Q9D4G9; -.
DR MaxQB; Q9D4G9; -.
DR PaxDb; Q9D4G9; -.
DR PeptideAtlas; Q9D4G9; -.
DR PRIDE; Q9D4G9; -.
DR ProteomicsDB; 299913; -.
DR Antibodypedia; 27643; 171 antibodies from 23 providers.
DR Ensembl; ENSMUST00000042450; ENSMUSP00000041035; ENSMUSG00000035367.
DR Ensembl; ENSMUST00000224479; ENSMUSP00000153050; ENSMUSG00000035367.
DR Ensembl; ENSMUST00000225815; ENSMUSP00000153621; ENSMUSG00000035367.
DR Ensembl; ENSMUST00000225828; ENSMUSP00000153675; ENSMUSG00000035367.
DR GeneID; 74386; -.
DR KEGG; mmu:74386; -.
DR UCSC; uc007qua.2; mouse.
DR CTD; 80010; -.
DR MGI; MGI:1921636; Rmi1.
DR VEuPathDB; HostDB:ENSMUSG00000035367; -.
DR eggNOG; KOG3683; Eukaryota.
DR GeneTree; ENSGT00940000161055; -.
DR HOGENOM; CLU_030961_0_0_1; -.
DR InParanoid; Q9D4G9; -.
DR OMA; STWHVKV; -.
DR OrthoDB; 531291at2759; -.
DR PhylomeDB; Q9D4G9; -.
DR TreeFam; TF316491; -.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 74386; 9 hits in 71 CRISPR screens.
DR ChiTaRS; Rmi1; mouse.
DR PRO; PR:Q9D4G9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9D4G9; protein.
DR Bgee; ENSMUSG00000035367; Expressed in animal zygote and 224 other tissues.
DR Genevisible; Q9D4G9; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0002023; P:reduction of food intake in response to dietary excess; IMP:MGI.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0071139; P:resolution of recombination intermediates; ISO:MGI.
DR GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR GO; GO:0009749; P:response to glucose; IMP:MGI.
DR Gene3D; 1.10.8.1020; -; 1.
DR Gene3D; 2.40.50.770; -; 1.
DR InterPro; IPR033472; DUF1767.
DR InterPro; IPR032199; RMI1_C.
DR InterPro; IPR013894; RMI1_N.
DR InterPro; IPR042470; RMI1_N_C_sf.
DR InterPro; IPR044881; RMI1_N_N_sf.
DR Pfam; PF16099; RMI1_C; 1.
DR Pfam; PF08585; RMI1_N; 1.
DR SMART; SM01161; DUF1767; 1.
PE 2: Evidence at transcript level;
KW Acetylation; DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..616
FT /note="RecQ-mediated genome instability protein 1"
FT /id="PRO_0000227547"
FT REGION 269..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9A7"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9A7"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9A7"
FT CROSSLNK 335
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9A7"
FT CROSSLNK 387
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9A7"
FT CONFLICT 73
FT /note="I -> V (in Ref. 2; AAH37694)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="L -> S (in Ref. 1; BAC37651)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="R -> H (in Ref. 2; AAH37694)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="D -> G (in Ref. 2; AAH37694)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="K -> E (in Ref. 2; AAH37694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 616 AA; 68465 MW; 2C70E918FD911803 CRC64;
MSVASAVLRV ETWLLATWHV KVPPMWLEAC VNWIQEENNN ATLSQAQINK QVLEQWLLTD
LRDLEHPLLP DDILELPKGE LNGFYALQIN SLVDVSQPAY SQIQKLRGKN TTNDLVSAET
QSTPKPWEVR PSRMLMLQLT DGVTHIQGME YQSIPALHSG LPPGTKILVR GCILFRLGVL
LLKPENVKVL GGEVDGLSEE NAQEKVLARL IGELDPTVPV IPNNSIHNVP KVSGGLDAVL
GPSDEELLAS LDESEESAAN NDVAMERSCF STGTSSNTTP TNPSGFEPGC NISSRPKEKP
PNQPTHFTDG EFDDFSLEEA LLLEETVQKE QMETKASQPL TLKENTGKCM EIFSHKPSSL
NHTALIHKQG NSNFDEKTSE QMIHEDKFFD CASTRNHHKR FSAHDFTNDS KISEVDDAAQ
QTLSSSNVHC LRNKILNRKL DLSEKSSQIS KENGHPFQAC SSRSFENNTY LSIGMDLHSP
PFIYLSVLMA RKPKEVTTVT VKAFIVTLTG NLSSSGGFWG VTAKVSDGTA YLDVDFIDEI
LTSMIGYSVP EMKQLRKDPL KYKTFLEGLQ KCQRDLIDLC CLMTISYDPS SCKGVVLELQ
DVGMEHVENL KKRLNK
