MRS3_YEAST
ID MRS3_YEAST Reviewed; 314 AA.
AC P10566; D6VW52;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 4.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Mitochondrial RNA-splicing protein MRS3;
GN Name=MRS3; OrderedLocusNames=YJL133W; ORFNames=J0675;
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].
RC STRAIN=IC8/R101;
RX PubMed=2448588; DOI=10.1007/bf00337771;
RA Schmidt C., Soellner T., Schweyen R.J.;
RT "Nuclear suppression of a mitochondrial RNA splice defect: nucleotide
RT sequence and disruption of the MRS3 gene.";
RL Mol. Gen. Genet. 210:145-152(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=M1301;
RX PubMed=1703236; DOI=10.1016/0022-2836(91)90608-9;
RA Wiesenberger G., Link T.A., von Ahsen U., Waldherr M., Schweyen R.J.;
RT "MRS3 and MRS4, two suppressors of mtRNA splicing defects in yeast, are new
RT members of the mitochondrial carrier family.";
RL J. Mol. Biol. 217:23-37(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8813765;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT chromosome X reveals 14 known genes and 13 new open reading frames
RT including homologues of genes clustered on the right arm of chromosome
RT XI.";
RL Yeast 12:787-797(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [5]
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 [6]
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).
CC -!- FUNCTION: MRS3 suppresses a mitochondrial splice defect in the first
CC intron of the COB gene. It may act as a carrier, exerting its
CC suppressor activity via modulation of solute concentrations in the
CC mitochondrion (possibly of cations).
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- MISCELLANEOUS: Present with 1360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA39830.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X56445; CAA39829.1; -; Genomic_DNA.
DR EMBL; X56445; CAA39830.1; ALT_INIT; Genomic_DNA.
DR EMBL; X06239; CAA29582.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X87371; CAA60822.1; -; Genomic_DNA.
DR EMBL; Z49408; CAA89428.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08668.1; -; Genomic_DNA.
DR PIR; S55179; S55179.
DR RefSeq; NP_012402.1; NM_001181566.1.
DR AlphaFoldDB; P10566; -.
DR SMR; P10566; -.
DR BioGRID; 33623; 48.
DR DIP; DIP-8202N; -.
DR IntAct; P10566; 4.
DR MINT; P10566; -.
DR STRING; 4932.YJL133W; -.
DR TCDB; 2.A.29.5.1; the mitochondrial carrier (mc) family.
DR MaxQB; P10566; -.
DR PaxDb; P10566; -.
DR PRIDE; P10566; -.
DR EnsemblFungi; YJL133W_mRNA; YJL133W; YJL133W.
DR GeneID; 853308; -.
DR KEGG; sce:YJL133W; -.
DR SGD; S000003669; MRS3.
DR VEuPathDB; FungiDB:YJL133W; -.
DR eggNOG; KOG0760; Eukaryota.
DR GeneTree; ENSGT00940000169345; -.
DR HOGENOM; CLU_015166_3_1_1; -.
DR InParanoid; P10566; -.
DR OMA; FTTQLTM; -.
DR BioCyc; YEAST:G3O-31582-MON; -.
DR PRO; PR:P10566; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P10566; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; EXP:Reactome.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IMP:SGD.
DR GO; GO:0048250; P:iron import into the mitochondrion; IDA:SGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.50.40.10; -; 2.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR Pfam; PF00153; Mito_carr; 3.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; mRNA processing;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..314
FT /note="Mitochondrial RNA-splicing protein MRS3"
FT /id="PRO_0000090691"
FT TRANSMEM 33..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..204
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..238
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..298
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT REPEAT 31..118
FT /note="Solcar 1"
FT REPEAT 128..210
FT /note="Solcar 2"
FT REPEAT 217..310
FT /note="Solcar 3"
SQ SEQUENCE 314 AA; 34502 MW; 861145CE6E4EF321 CRC64;
MVENSSSNNS TRPIPAIPMD LPDYEALPTH APLYHQLIAG AFAGIMEHSV MFPIDALKTR
IQSANAKSLS AKNMLSQISH ISTSEGTLAL WKGVQSVILG AGPAHAVYFG TYEFCKKNLI
DSSDTQTHHP FKTAISGACA TTASDALMNP FDTIKQRIQL NTSASVWQTT KQIYQSEGLA
AFYYSYPTTL VMNIPFAAFN FVIYESSTKF LNPSNEYNPL IHCLCGSISG STCAAITTPL
DCIKTVLQIR GSQTVSLEIM RKADTFSKAA SAIYQVYGWK GFWRGWKPRI VANMPATAIS
WTAYECAKHF LMTY
