YME2_YEAST
ID YME2_YEAST Reviewed; 850 AA.
AC P32843; D6W0C9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Mitochondrial escape protein 2;
DE AltName: Full=Protein RNA12;
DE Flags: Precursor;
GN Name=YME2; Synonyms=PRP12, RNA12; OrderedLocusNames=YMR302C;
GN ORFNames=YM9952.04C;
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 MUTAGENESIS OF ASN-502.
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=1557037; DOI=10.1007/bf00280010;
RA Liang S., Alksne L., Warner J.R., Lacroute F.;
RT "RNA12+, a gene of Saccharomyces cerevisiae involved in pre-rRNA
RT maturation. Characterization of a temperature-sensitive mutant, cloning and
RT sequencing of the gene.";
RL Mol. Gen. Genet. 232:304-312(1992).
RN [2]
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 [3]
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 [4]
RP FUNCTION.
RX PubMed=8514129; DOI=10.1093/genetics/134.1.21;
RA Thorsness P.E., Fox T.D.;
RT "Nuclear mutations in Saccharomyces cerevisiae that affect the escape of
RT DNA from mitochondria to the nucleus.";
RL Genetics 134:21-28(1993).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF ASN-502.
RX PubMed=8649384; DOI=10.1128/mcb.16.6.2764;
RA Hanekamp T., Thorsness P.E.;
RT "Inactivation of YME2/RNA12, which encodes an integral inner mitochondrial
RT membrane protein, causes increased escape of DNA from mitochondria to the
RT nucleus in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:2764-2771(1996).
RN [6]
RP FUNCTION.
RX PubMed=9933355; DOI=10.1007/s002940050418;
RA Hanekamp T., Thorsness P.E.;
RT "YNT20, a bypass suppressor of yme1 yme2, encodes a putative 3'-5'
RT exonuclease localized in mitochondria of Saccharomyces cerevisiae.";
RL Curr. Genet. 34:438-448(1999).
RN [7]
RP FUNCTION.
RX PubMed=11737636; DOI=10.1046/j.1365-2958.2001.02686.x;
RA Mollapour M., Piper P.W.;
RT "The ZbYME2 gene from the food spoilage yeast Zygosaccharomyces bailii
RT confers not only YME2 functions in Saccharomyces cerevisiae, but also the
RT capacity for catabolism of sorbate and benzoate, two major weak organic
RT acid preservatives.";
RL Mol. Microbiol. 42:919-930(2001).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
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 [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF ASN-502.
RX PubMed=16850347; DOI=10.1007/s00294-006-0087-9;
RA Park S., Hanekamp T., Thorsness M.K., Thorsness P.E.;
RT "Yme2p is a mediator of nucleoid structure and number in mitochondria of
RT the yeast Saccharomyces cerevisiae.";
RL Curr. Genet. 50:173-182(2006).
CC -!- FUNCTION: Plays a role in maintaining the mitochondrial genome and in
CC controlling the mtDNA escape. Involved in the regulation of mtDNA
CC nucleotide structure and number. May have a dispensable role in early
CC maturation of pre-rRNA. {ECO:0000269|PubMed:11737636,
CC ECO:0000269|PubMed:16850347, ECO:0000269|PubMed:8514129,
CC ECO:0000269|PubMed:8649384, ECO:0000269|PubMed:9933355}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:8649384}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:8649384}.
CC -!- MISCELLANEOUS: Present with 5260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the YME2 family. {ECO:0000305}.
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DR EMBL; S92205; AAB21991.1; -; Genomic_DNA.
DR EMBL; Z49212; CAA89135.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10203.1; -; Genomic_DNA.
DR PIR; S20462; S20462.
DR RefSeq; NP_014031.1; NM_001182811.1.
DR AlphaFoldDB; P32843; -.
DR BioGRID; 35482; 141.
DR DIP; DIP-678N; -.
DR IntAct; P32843; 37.
DR STRING; 4932.YMR302C; -.
DR MaxQB; P32843; -.
DR PaxDb; P32843; -.
DR PRIDE; P32843; -.
DR EnsemblFungi; YMR302C_mRNA; YMR302C; YMR302C.
DR GeneID; 855348; -.
DR KEGG; sce:YMR302C; -.
DR SGD; S000004917; YME2.
DR VEuPathDB; FungiDB:YMR302C; -.
DR eggNOG; ENOG502QS0P; Eukaryota.
DR HOGENOM; CLU_007861_1_0_1; -.
DR InParanoid; P32843; -.
DR OMA; FQFFRPY; -.
DR BioCyc; YEAST:G3O-32968-MON; -.
DR PRO; PR:P32843; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P32843; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd12433; RRM_Yme2p_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR018850; Mt_escape_2_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR039627; Yme2_C.
DR InterPro; IPR034260; Yme2_RRM.
DR PANTHER; PTHR32198; PTHR32198; 1.
DR Pfam; PF10443; RNA12; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; mRNA processing;
KW Reference proteome; RNA-binding; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 45..850
FT /note="Mitochondrial escape protein 2"
FT /id="PRO_0000081806"
FT TOPO_DOM 45..287
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..850
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 198..272
FT /note="RRM"
FT REGION 44..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 502
FT /note="N->Y: In YME2-4; prevents mtDNA escape, growth on
FT nonfermentable carbon sources and growth at 37 degrees
FT Celsius on glucose."
FT /evidence="ECO:0000269|PubMed:1557037,
FT ECO:0000269|PubMed:16850347, ECO:0000269|PubMed:8649384"
SQ SEQUENCE 850 AA; 96689 MW; 3BEFD730AAD376C7 CRC64;
MLLVRTTSLN VSRMPVPCLA RGIGILKGKY RLANLMNAQP SVRHVSSEIQ QKDQQAGESN
TATDTGVIHK SDEETLIYFD NVYARTTSVW NPTLWYNLLL RNQSRDAVRE KIRNLASPPN
NPIYGLELKS TIPVKRDGGV FATFVVPPKY TKAQVNSLIQ QNTARESSKN LLSYFTRASA
FPVKGSPWIE DLRRLPSTTI VIKFQGPALT EEEIYSLFRR YGTIIDIFPP TAANNNVAKV
RYRSFRGAIS AKNCVSGIEI HNTVLHIQYE NIRRGHLVSN FFTNHTRIAI PVLFALLSIF
AVLVFDPIRE FSIEQKITHK YSLSWDNKFW KQLKTLTSST MTSIKYYWGG PDDNHQRKHL
WEERIEKVND LKMWLEENNN TFVVIRGPRG SGKHDLVMQH TLQNRANVLY LDCDKLIKSR
TDPMFLKNAA SQLGYFPIFP WIDSVTGVLD LTVQGLTGQK TGLSETKESR FRNMLTTSLM
SIRRIALKNY KAFVSTGDGT VNVKEEDYLQ QHPEAKPVIV IDRFEGKSEI NGFVYKELSD
WAAMLVQMNI AHVIFLTETV ASNQRLSESL PNQVFKNLIL SDASKENSRN YVLSQLEDYL
YYNKKSKGEN VKEPESEKET AENNDSDSEA DTSVKKAEVI LNEKELQEID ASLEPLGGRM
LDLQAFVRRV KSGEEPSEAV DKMIEQASEQ ITQMFLSDKI DSNKSAQAWE LIELLSANPV
IPFHEIVNKP LFKAAPETGI MELENNGLIT VSRDRGVLQE IRPAKPLYRA AFTYLINDPE
LAKVLKTRYL LKVVGFETGR IKKWEEELKP LGKVPDQKLF KTRLDYLSGK INASNAVITK
CEEEIKNLSK
