RMI1_CAEEL
ID RMI1_CAEEL Reviewed; 926 AA.
AC P91399;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=RecQ-mediated genome instability protein 1 homolog {ECO:0000305};
GN Name=rmh-1 {ECO:0000312|WormBase:M01E11.3};
GN ORFNames=M01E11.3 {ECO:0000312|WormBase:M01E11.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH HIM-6 AND TOP-3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=27011106; DOI=10.1371/journal.pbio.1002412;
RA Jagut M., Hamminger P., Woglar A., Millonigg S., Paulin L., Mikl M.,
RA Dello Stritto M.R., Tang L., Habacher C., Tam A., Gallach M.,
RA von Haeseler A., Villeneuve A.M., Jantsch V.;
RT "Separable roles for a Caenorhabditis elegans RMI1 homolog in promoting and
RT antagonizing meiotic crossovers ensure faithful chromosome inheritance.";
RL PLoS Biol. 14:E1002412-E1002412(2016).
RN [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN BTR COMPLEX, INTERACTION WITH RMIF-2,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=34252074; DOI=10.1371/journal.pgen.1009663;
RA Velkova M., Silva N., Dello Stritto M.R., Schleiffer A., Barraud P.,
RA Hartl M., Jantsch V.;
RT "Caenorhabditis elegans RMI2 functional homolog-2 (RMIF-2) and RMI1 (RMH-1)
RT have both overlapping and distinct meiotic functions within the BTR
RT complex.";
RL PLoS Genet. 17:e1009663-e1009663(2021).
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 (By
CC similarity). Component of the BTR double Holliday Junction dissolution
CC complex, which is involved in homologous recombination during meiotic
CC double strand break repair in the germline (Probable). Promotes top-3
CC binding to double Holliday junctions (DHJ) and hence stimulates top-3-
CC mediated dissolution (By similarity). Stabilizes and positively
CC regulates the localization of the BTR double Holliday Junction
CC dissolution complex components rmif-2 and him-6 at nuclear foci during
CC meiotic recombination (PubMed:27011106, PubMed:34252074). Plays a role
CC in double strand break repair by regulating the accumulation of rad-51
CC at double strand breaks during meiosis (PubMed:27011106). Positively
CC regulates chiasma formation and DNA crossover designation, formation
CC and positioning on chromosome arms (away from the chromosome center)
CC during meiotic homologous recombination (PubMed:27011106,
CC PubMed:34252074). Specifically localizes him-6 to DNA crossover sites
CC along chromosome arms (PubMed:27011106). Also plays a role in the
CC repair of non-crossover homologous recombination intermediates during
CC meiosis (PubMed:27011106). Not required for chromosome pairing and
CC synapsis (PubMed:27011106). Together with rmh-2, positively regulates
CC larval development (PubMed:27011106). {ECO:0000250|UniProtKB:Q9H9A7,
CC ECO:0000269|PubMed:27011106, ECO:0000269|PubMed:34252074,
CC ECO:0000305|PubMed:34252074}.
CC -!- SUBUNIT: Component of the RMI complex, containing at least top-3, rmh-1
CC and rmh-2 (By similarity). Component of the BTR double Holliday
CC Junction dissolution complex composed of at least him-6, top-3, rmh-1
CC and rmif-2, which is involved in double strand break repair in the
CC germline (Probable). Interacts with rmif-2; the interaction is direct
CC and is required for mutual stability and localization at nuclear foci
CC (PubMed:34252074). May interact with him-6; the interaction is required
CC for mutual stability and localization at nuclear foci
CC (PubMed:27011106). May interact with top-3 (PubMed:27011106).
CC {ECO:0000250|UniProtKB:Q9H9A7, ECO:0000269|PubMed:27011106,
CC ECO:0000269|PubMed:34252074, ECO:0000305|PubMed:34252074}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27011106,
CC ECO:0000269|PubMed:34252074}. Chromosome {ECO:0000269|PubMed:27011106}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:27011106}. Note=In early
CC development, first localizes to the nucleoplasm then as development
CC proceeds progressively accumulates on foci on chromosomes
CC (PubMed:27011106). Co-localizes with rmif-2 in nuclei foci during
CC pachytene in meiotic prophase I (PubMed:34252074). Localization at
CC nuclear foci is dependent on rmif-2 during meiotic recombination
CC (PubMed:34252074). Accumulates at nuclei foci as pachytene progresses,
CC peaking at mid-pachytene (PubMed:27011106). Co-localizes with him-6 at
CC mid-pachytene and late-pachytene in meiotic prophase I
CC (PubMed:27011106). Does not localize to nuclei foci during diplotene
CC (PubMed:27011106). Localizes to nuclei foci at crossover sites and non-
CC crossover sites on DNA homologous recombination intermediates
CC (PubMed:27011106). Co-localizes with cosa-1 and msh-5 at DNA crossover
CC sites during meiotic homologous recombination (PubMed:27011106).
CC {ECO:0000269|PubMed:27011106, ECO:0000269|PubMed:34252074}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline (at protein level).
CC {ECO:0000269|PubMed:27011106, ECO:0000269|PubMed:34252074}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the germline throughout early
CC pachynema in meiotic prophase I (at protein level) (PubMed:27011106,
CC PubMed:34252074). Expression progressively increases during pachytene
CC in meiotic prophase I, peaking during mid-pachytene and reducing at
CC late pachytene (at protein level) (PubMed:27011106).
CC {ECO:0000269|PubMed:27011106, ECO:0000269|PubMed:34252074}.
CC -!- SIMILARITY: Belongs to the RMI1 family. {ECO:0000305}.
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DR EMBL; BX284601; CCD71341.1; -; Genomic_DNA.
DR PIR; T29323; T29323.
DR RefSeq; NP_491632.1; NM_059231.5.
DR AlphaFoldDB; P91399; -.
DR SMR; P91399; -.
DR STRING; 6239.M01E11.3; -.
DR EPD; P91399; -.
DR PaxDb; P91399; -.
DR EnsemblMetazoa; M01E11.3.1; M01E11.3.1; WBGene00019712.
DR GeneID; 172212; -.
DR KEGG; cel:CELE_M01E11.3; -.
DR UCSC; M01E11.3; c. elegans.
DR CTD; 172212; -.
DR WormBase; M01E11.3; CE12292; WBGene00019712; rmh-1.
DR eggNOG; KOG3683; Eukaryota.
DR GeneTree; ENSGT00940000161055; -.
DR HOGENOM; CLU_354981_0_0_1; -.
DR InParanoid; P91399; -.
DR OMA; DDLSWFH; -.
DR OrthoDB; 977321at2759; -.
DR Reactome; R-CEL-5693607; Processing of DNA double-strand break ends.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00019712; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0051026; P:chiasma assembly; IMP:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0002164; P:larval development; IMP:UniProtKB.
DR GO; GO:0090727; P:positive regulation of brood size; IMP:UniProtKB.
DR GO; GO:0045911; P:positive regulation of DNA recombination; IMP:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; IMP:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR Gene3D; 2.40.50.770; -; 1.
DR InterPro; IPR033472; DUF1767.
DR InterPro; IPR039215; RMI1.
DR InterPro; IPR013894; RMI1_N.
DR InterPro; IPR042470; RMI1_N_C_sf.
DR PANTHER; PTHR14790; PTHR14790; 1.
DR Pfam; PF08585; RMI1_N; 1.
DR SMART; SM01161; DUF1767; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Isopeptide bond; Meiosis; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..926
FT /note="RecQ-mediated genome instability protein 1 homolog"
FT /id="PRO_0000455613"
FT REGION 734..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 428
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9A7"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9A7"
SQ SEQUENCE 926 AA; 105874 MW; 2A4DDB220BFF9609 CRC64;
MKETELDRLF SWLARKHYPF KREWLRICVQ YIEGSLGQRI KTVDVKQIGE LVIQQFLNSK
ISEALDPTMK IPTSAVKVVI VKRMIFQVIS STNISTSLYE QLSECTRHNE DLAWFHGGSK
ADHEEENRDK EKDVASDRMN HTQTKNAIKK RGMLKIELTD GVNTLKAIEL DEVFDEKIML
PGAKIILTGK VKCRRGNLLL DKSNCAFLGG RVESLSFDKV AQLSNALKVD LDAEKKRRKA
SLENAAASVS RNNKKQIDKK NLSLNQSSLS PFLVKTSRIT GEVTVPVKQS LVPTASRILP
SSVAVIPSIQ IEKPTDPIEN WDFSIEEVPQ EPTPEPPSHH VRGLVEHYPL RSKPQDPLPP
PPTKRLSSLI IDKNSISKVS QNISNQVEKG LLQNKTIEDW TFNSTNSFDK SKKVMSIDNS
KDQKMKIKEL PGQLIRPTPI EKPIIGDPRM NSEKRKDVSV WVWEDRKGSE EEDIAAKRIK
KIDSVMEIPL CFVKETTRQA NRSNEESRHK LNTFAQTIHG PRSKIDDFRV KSNNVPVFKQ
ITDHFITVKS NPNSFTSSTR HTPPQMPKVV DFGNFEDYDE DYEDEVLPTS SFRDQLKQRK
SLDNHGEDVV LEEEMDHVDH DESIIECTMD HEGRLECERW GLRGRESNII EDDKRNVYNG
YNMNNNIERD NKYDSSMNGM PQPNLQHPLS ILPPPPVIPP SQNWNYTGYY QAPPLRNVIK
SETVDSVVPE DQKMVGAQGK KRPNVRQEND NMKNKQSANV QVYRTPFAER LNSGDSSSKL
SPQLFQRMAD LQIVPFGDAL FNRKFWMMSK IVVIMPSICS QIHELQSDGI DWLLQIRVTD
TSVKNVICRV STSLLNRIFG FDVQQCKNLF NKNQVEELRA KKCEAERKLL GFKRLDLLLW
VEVSPERNQI PLILDVKTIS DALNIL
