ID ABF2_YEAST Reviewed; 183 AA.
AC Q02486; D6VZP6; Q712M5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 27-MAR-2024, entry version 196.
DE RecName: Full=ARS-binding factor 2, mitochondrial;
DE Flags: Precursor;
GN Name=ABF2; Synonyms=HIM1; OrderedLocusNames=YMR072W; ORFNames=YM9916.11;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-56.
RX PubMed=1881919; DOI=10.1073/pnas.88.17.7864;
RA Diffley J.F.X., Stillman B.;
RT "A close relative of the nuclear, chromosomal high-mobility group protein
RT HMG1 in yeast mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7864-7868(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sun C.L., Lee F.J., Lin-Chao S., Chao C.K.;
RT "Molecular cloning and characterization of yeast CDRP1: an HMG protein
RT which recognizes cisplatin-damaged DNA and confers drug sensitivity.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=9742088; DOI=10.1128/mcb.18.10.5712;
RA Cho J.H., Ha S.J., Kao L.R., Megraw T.L., Chae C.-B.;
RT "A novel DNA-binding protein bound to the mitochondrial inner membrane
RT restores the null mutation of mitochondrial histone Abf2p in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 18:5712-5723(1998).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Specific binding to the autonomously replicating sequence 1
CC (ARS1). Interaction with regulatory regions: probably involved in
CC compacting the mitochondrial genome. It might play a positive role in
CC gene expression and replication.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Has a temperature-sensitive growth defect in
CC glucose-rich medium, with slower growth and smaller colonies at 37
CC degrees Celsius but not 30 degrees Celsius; the phenotype is suppressed
CC by overexpression of YHM2. {ECO:0000269|PubMed:9742088}.
CC -!- MISCELLANEOUS: Present with 3810 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M73753; AAA73079.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ223169; CAA11146.1; -; mRNA.
DR EMBL; Z48952; CAA88797.1; -; Genomic_DNA.
DR EMBL; AY557967; AAS56293.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09970.1; -; Genomic_DNA.
DR PIR; A41302; A41302.
DR RefSeq; NP_013788.1; NM_001182570.1.
DR PDB; 5JGH; X-ray; 2.60 A; A/D/G/J=27-183.
DR PDB; 5JH0; X-ray; 2.18 A; A/D=27-183.
DR PDBsum; 5JGH; -.
DR PDBsum; 5JH0; -.
DR AlphaFoldDB; Q02486; -.
DR SMR; Q02486; -.
DR BioGRID; 35247; 197.
DR DIP; DIP-5492N; -.
DR IntAct; Q02486; 30.
DR MINT; Q02486; -.
DR STRING; 4932.YMR072W; -.
DR MaxQB; Q02486; -.
DR PaxDb; 4932-YMR072W; -.
DR PeptideAtlas; Q02486; -.
DR EnsemblFungi; YMR072W_mRNA; YMR072W; YMR072W.
DR GeneID; 855094; -.
DR KEGG; sce:YMR072W; -.
DR AGR; SGD:S000004676; -.
DR SGD; S000004676; ABF2.
DR VEuPathDB; FungiDB:YMR072W; -.
DR eggNOG; KOG0381; Eukaryota.
DR HOGENOM; CLU_082854_2_0_1; -.
DR InParanoid; Q02486; -.
DR OMA; PHSANEV; -.
DR OrthoDB; 1540759at2759; -.
DR BioCyc; YEAST:G3O-32774-MONOMER; -.
DR BioGRID-ORCS; 855094; 0 hits in 10 CRISPR screens.
DR ChiTaRS; ABF2; yeast.
DR PRO; PR:Q02486; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q02486; Protein.
DR GO; GO:0000262; C:mitochondrial chromosome; IDA:SGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR GO; GO:0090139; P:mitochondrial chromosome packaging; IMP:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR CDD; cd22010; HMG-box_ABF2-like_rpt1; 1.
DR CDD; cd22012; HMG-box_ABF2_IXR1-like_rpt2; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 2.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR PANTHER; PTHR48112; HIGH MOBILITY GROUP PROTEIN DSP1; 1.
DR PANTHER; PTHR48112:SF32; HIGH MOBILITY GROUP PROTEIN DSP1; 1.
DR Pfam; PF00505; HMG_box; 2.
DR SMART; SM00398; HMG; 2.
DR SUPFAM; SSF47095; HMG-box; 2.
DR PROSITE; PS50118; HMG_BOX_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Mitochondrion;
KW Nucleus; Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1881919"
FT CHAIN 27..183
FT /note="ARS-binding factor 2, mitochondrial"
FT /id="PRO_0000013477"
FT DNA_BIND 43..111
FT /note="HMG box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 116..183
FT /note="HMG box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:5JH0"
FT HELIX 49..64
FT /evidence="ECO:0007829|PDB:5JH0"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:5JH0"
FT HELIX 86..113
FT /evidence="ECO:0007829|PDB:5JH0"
FT HELIX 122..137
FT /evidence="ECO:0007829|PDB:5JH0"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:5JH0"
FT HELIX 159..179
FT /evidence="ECO:0007829|PDB:5JH0"
SQ SEQUENCE 183 AA; 21562 MW; D280A7D2B675B5B1 CRC64;
MNSYSLLTRS FHESSKPLFN LASTLLKASK RTQLRNELIK QGPKRPTSAY FLYLQDHRSQ
FVKENPTLRP AEISKIAGEK WQNLEADIKE KYISERKKLY SEYQKAKKEF DEKLPPKKPA
GPFIKYANEV RSQVFAQHPD KSQLDLMKII GDKWQSLDQS IKDKYIQEYK KAIQEYNARY
PLN
//
