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   27-MAR-2024, entry version 149.
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.ENSMUSP00000153050; -.
DR   iPTMnet; Q9D4G9; -.
DR   PhosphoSitePlus; Q9D4G9; -.
DR   EPD; Q9D4G9; -.
DR   jPOST; Q9D4G9; -.
DR   MaxQB; Q9D4G9; -.
DR   PaxDb; 10090-ENSMUSP00000041035; -.
DR   PeptideAtlas; Q9D4G9; -.
DR   ProteomicsDB; 299913; -.
DR   Pumba; Q9D4G9; -.
DR   Antibodypedia; 27643; 184 antibodies from 24 providers.
DR   Ensembl; ENSMUST00000042450.10; ENSMUSP00000041035.9; ENSMUSG00000035367.10.
DR   Ensembl; ENSMUST00000224479.2; ENSMUSP00000153050.2; ENSMUSG00000035367.10.
DR   Ensembl; ENSMUST00000225815.2; ENSMUSP00000153621.2; ENSMUSG00000035367.10.
DR   Ensembl; ENSMUST00000225828.2; ENSMUSP00000153675.2; ENSMUSG00000035367.10.
DR   GeneID; 74386; -.
DR   KEGG; mmu:74386; -.
DR   UCSC; uc007qua.2; mouse.
DR   AGR; MGI:1921636; -.
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; SATWHVK; -.
DR   OrthoDB; 68841at2759; -.
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; 10 hits in 77 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 227 other cell types or tissues.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; NAS: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:0071139; P:resolution of DNA recombination intermediates; ISO:MGI.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR   GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR   GO; GO:0009749; P:response to glucose; IMP:MGI.
DR   Gene3D; 2.40.50.510; -; 1.
DR   Gene3D; 1.10.8.1020; RecQ-mediated genome instability protein 1, N-terminal domain; 1.
DR   Gene3D; 2.40.50.770; RecQ-mediated genome instability protein Rmi1, C-terminal domain; 1.
DR   InterPro; IPR032199; RMI1_C.
DR   InterPro; IPR049363; RMI1_N.
DR   InterPro; IPR042470; RMI1_N_C_sf.
DR   InterPro; IPR044881; RMI1_N_N_sf.
DR   InterPro; IPR013894; RMI1_OB.
DR   PANTHER; PTHR14790:SF15; RECQ-MEDIATED GENOME INSTABILITY PROTEIN 1; 1.
DR   PANTHER; PTHR14790; RECQ-MEDIATED GENOME INSTABILITY PROTEIN 1 RMI1; 1.
DR   Pfam; PF16099; RMI1_C; 1.
DR   Pfam; PF08585; RMI1_N_C; 1.
DR   Pfam; PF21000; RMI1_N_N; 1.
DR   SMART; SM01161; DUF1767; 1.
DR   Genevisible; Q9D4G9; MM.
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
//