RMI2_BOVIN
ID RMI2_BOVIN Reviewed; 157 AA.
AC A5PJU7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=RecQ-mediated genome instability protein 2;
GN Name=RMI2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential component of the RMI complex, a complex that plays
CC an important role in the processing of homologous recombination
CC intermediates. It is required to regulate sister chromatid segregation
CC and to limit DNA crossover. Essential for the stability, localization,
CC and function of BLM, TOP3A, and complexes containing BLM. In the RMI
CC complex, it is required to target BLM to chromatin and stress-induced
CC nuclear foci and mitotic phosphorylation of BLM.
CC {ECO:0000250|UniProtKB:Q96E14}.
CC -!- SUBUNIT: Component of the RMI complex, containing at least TOP3A, RMI1
CC and RMI2. The RMI complex interacts with BLM (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with BLM
CC at nuclear DNA repair foci. {ECO:0000250}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RMI2 family. {ECO:0000305}.
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DR EMBL; BC142245; AAI42246.1; -; mRNA.
DR RefSeq; NP_001093190.1; NM_001099720.1.
DR AlphaFoldDB; A5PJU7; -.
DR SMR; A5PJU7; -.
DR STRING; 9913.ENSBTAP00000037296; -.
DR PaxDb; A5PJU7; -.
DR PRIDE; A5PJU7; -.
DR GeneID; 615553; -.
DR KEGG; bta:615553; -.
DR CTD; 116028; -.
DR eggNOG; ENOG502S4AN; Eukaryota.
DR InParanoid; A5PJU7; -.
DR OrthoDB; 1604165at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0043007; P:maintenance of rDNA; IBA:GO_Central.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0033045; P:regulation of sister chromatid segregation; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR032245; RMI2.
DR PANTHER; PTHR33962; PTHR33962; 1.
DR Pfam; PF16100; RMI2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; DNA replication; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96E14"
FT CHAIN 2..157
FT /note="RecQ-mediated genome instability protein 2"
FT /id="PRO_0000297576"
FT DNA_BIND 45..115
FT /note="OB"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96E14"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96E14"
SQ SEQUENCE 157 AA; 16948 MW; 8A8378D67EAE7423 CRC64;
MAAPTDSLSV SGPTAVRLPR SPPIKVLAEQ LRRDAEGGPG SWRLSRAAVG REPLELRAVW
MQGTVVEAGG GVARLRDPSG SFSVRGLERV PRGRPCLVPG KYVMVMGVIQ ACSPEPCLQA
VKMTDLSDNP LHESLWELEV EDLHRHIYSL DDVGTGD