HMG5_CAEEL
ID HMG5_CAEEL Reviewed; 204 AA.
AC Q94234;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=HMG box-containing protein 5 {ECO:0000312|WormBase:F45E4.9};
DE Flags: Precursor;
GN Name=hmg-5 {ECO:0000312|WormBase:F45E4.9};
GN ORFNames=F45E4.9 {ECO:0000312|WormBase:F45E4.9};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=14623111; DOI=10.1016/s0014-5793(03)01191-8;
RA Im S.H., Lee J.;
RT "Identification of HMG-5 as a double-stranded telomeric DNA-binding protein
RT in the nematode Caenorhabditis elegans.";
RL FEBS Lett. 554:455-461(2003).
RN [3] {ECO:0000305}
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21258070; DOI=10.1093/jb/mvr008;
RA Sumitani M., Kasashima K., Matsugi J., Endo H.;
RT "Biochemical properties of Caenorhabditis elegans HMG-5, a regulator of
RT mitochondrial DNA.";
RL J. Biochem. 149:581-589(2011).
CC -!- FUNCTION: Binds to mitochondrial DNA (mtDNA) and plays a role in the
CC maintenance of mtDNA levels (PubMed:21258070). May also associate with
CC telomeric DNA, binding to at least two telomeric repeats of the
CC sequence 5'-TTTAGGG-3' (Probable). {ECO:0000269|PubMed:21258070,
CC ECO:0000305|PubMed:14623111}.
CC -!- SUBUNIT: Self-associates. {ECO:0000269|PubMed:21258070}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. Mitochondrion
CC matrix, mitochondrion nucleoid {ECO:0000305|PubMed:21258070}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:14623111}.
CC Chromosome, telomere {ECO:0000269|PubMed:14623111}. Note=Mainly
CC localizes to telomeres in mature oocytes and embryonic cells.
CC {ECO:0000269|PubMed:14623111}.
CC -!- TISSUE SPECIFICITY: Highly expressed in oocytes (at protein level).
CC {ECO:0000269|PubMed:14623111}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all cells of early and late embryos
CC (at protein level) (PubMed:14623111). Expression diminishes at the time
CC of hatching, and there is very little expression in larvae and adults
CC (at protein level) (PubMed:14623111). {ECO:0000269|PubMed:14623111}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC mitochondrial DNA (mtDNA) copy number. {ECO:0000269|PubMed:21258070}.
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DR EMBL; BX284604; CCD63785.1; -; Genomic_DNA.
DR PIR; T25760; T25760.
DR RefSeq; NP_501245.1; NM_068844.3.
DR AlphaFoldDB; Q94234; -.
DR SMR; Q94234; -.
DR IntAct; Q94234; 1.
DR STRING; 6239.F45E4.9; -.
DR EPD; Q94234; -.
DR PaxDb; Q94234; -.
DR PeptideAtlas; Q94234; -.
DR EnsemblMetazoa; F45E4.9.1; F45E4.9.1; WBGene00001975.
DR GeneID; 177543; -.
DR KEGG; cel:CELE_F45E4.9; -.
DR UCSC; F45E4.9; c. elegans.
DR CTD; 177543; -.
DR WormBase; F45E4.9; CE10508; WBGene00001975; hmg-5.
DR eggNOG; KOG0381; Eukaryota.
DR HOGENOM; CLU_1379240_0_0_1; -.
DR InParanoid; Q94234; -.
DR OMA; AMYIKEN; -.
DR OrthoDB; 1553029at2759; -.
DR PhylomeDB; Q94234; -.
DR Reactome; R-CEL-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-CEL-163282; Mitochondrial transcription initiation.
DR PRO; PR:Q94234; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001975; Expressed in adult organism and 4 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:WormBase.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:WormBase.
DR GO; GO:0008301; F:DNA binding, bending; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:WormBase.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:WormBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0032042; P:mitochondrial DNA metabolic process; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 2.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF09011; HMG_box_2; 1.
DR SMART; SM00398; HMG; 2.
DR SUPFAM; SSF47095; SSF47095; 2.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; Mitochondrion; Mitochondrion nucleoid; Nucleus;
KW Reference proteome; Telomere; Transit peptide.
FT TRANSIT 1..10
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 11..204
FT /note="HMG box-containing protein 5"
FT /id="PRO_0000450268"
FT DNA_BIND 30..95
FT /note="HMG box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 132..195
FT /note="HMG box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 102..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 204 AA; 23422 MW; ACD5A5003556A396 CRC64;
MLGTISMRFF ATKVVAPRAS VAASTPQVPL GMNINPYAMF IKENFKANTS DMKRTDLMKE
LSGKWKALSI SEKDKYTELS KNYNAQKLDD FMKLSTEEQK KLVDSAKEKK AERASRRHAK
ERREKRKQSG RPSVPPSAYA LFIKEKLSGA GMESKEKMKE AVAQWKAFTD SQKKKYTDEA
KKLKDEYHVV LQKWEAEQKE NADQ
