RCF1_YEAST
ID RCF1_YEAST Reviewed; 159 AA.
AC Q03713; D6VZE4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Respiratory supercomplex factor 1, mitochondrial;
DE AltName: Full=Altered inheritance of mitochondria protein 31;
GN Name=RCF1; Synonyms=AIM31; OrderedLocusNames=YML030W;
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 [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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=19300474; DOI=10.1371/journal.pgen.1000407;
RA Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J.,
RA Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M.,
RA Troyanskaya O.G., Caudy A.A.;
RT "Computationally driven, quantitative experiments discover genes required
RT for mitochondrial biogenesis.";
RL PLoS Genet. 5:E1000407-E1000407(2009).
RN [8]
RP ASSOCIATION WITH THE RESPIRATORY CHAIN COMPLEX IV.
RX PubMed=19750512; DOI=10.1002/pmic.200800951;
RA Helbig A.O., de Groot M.J., van Gestel R.A., Mohammed S., de Hulster E.A.,
RA Luttik M.A., Daran-Lapujade P., Pronk J.T., Heck A.J., Slijper M.;
RT "A three-way proteomics strategy allows differential analysis of yeast
RT mitochondrial membrane protein complexes under anaerobic and aerobic
RT conditions.";
RL Proteomics 9:4787-4798(2009).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND ASSOCIATION WITH THE RESPIRATORY CHAIN
RP COMPLEX III/COMPLEX IV SUPERCOMPLEX.
RX PubMed=22342701; DOI=10.1016/j.cmet.2012.01.016;
RA Vukotic M., Oeljeklaus S., Wiese S., Vogtle F.N., Meisinger C., Meyer H.E.,
RA Zieseniss A., Katschinski D.M., Jans D.C., Jakobs S., Warscheid B.,
RA Rehling P., Deckers M.;
RT "Rcf1 mediates cytochrome oxidase assembly and respirasome formation,
RT revealing heterogeneity of the enzyme complex.";
RL Cell Metab. 15:336-347(2012).
RN [10]
RP FUNCTION, AND ASSOCIATION WITH THE RESPIRATORY CHAIN COMPLEX III/COMPLEX IV
RP SUPERCOMPLEX.
RX PubMed=22405070; DOI=10.1016/j.cmet.2012.02.006;
RA Chen Y.C., Taylor E.B., Dephoure N., Heo J.M., Tonhato A., Papandreou I.,
RA Nath N., Denko N.C., Gygi S.P., Rutter J.;
RT "Identification of a protein mediating respiratory supercomplex
RT stability.";
RL Cell Metab. 15:348-360(2012).
RN [11]
RP FUNCTION, INTERACTION WITH COX3, AND ASSOCIATION WITH THE RESPIRATORY CHAIN
RP COMPLEX III/COMPLEX IV SUPERCOMPLEX.
RX PubMed=22310663; DOI=10.1128/mcb.06369-11;
RA Strogolova V., Furness A., Robb-McGrath M., Garlich J., Stuart R.A.;
RT "Rcf1 and Rcf2, members of the hypoxia-induced gene 1 protein family, are
RT critical components of the mitochondrial cytochrome bc1-cytochrome c
RT oxidase supercomplex.";
RL Mol. Cell. Biol. 32:1363-1373(2012).
RN [12]
RP FUNCTION.
RX PubMed=30683696; DOI=10.1074/jbc.ra118.006888;
RA Strogolova V., Hoang N.H., Hosler J., Stuart R.A.;
RT "The yeast mitochondrial proteins Rcf1 and Rcf2 support the enzymology of
RT the cytochrome c oxidase complex and generation of the proton motive
RT force.";
RL J. Biol. Chem. 294:4867-4877(2019).
RN [13]
RP FUNCTION.
RX PubMed=31591265; DOI=10.1074/jbc.ra119.010317;
RA Hoang N.H., Strogolova V., Mosley J.J., Stuart R.A., Hosler J.;
RT "Hypoxia-inducible gene domain 1 proteins in yeast mitochondria protect
RT against proton leak through complex IV.";
RL J. Biol. Chem. 294:17669-17677(2019).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=30598554; DOI=10.1038/s41594-018-0172-z;
RA Hartley A.M., Lukoyanova N., Zhang Y., Cabrera-Orefice A., Arnold S.,
RA Meunier B., Pinotsis N., Marechal A.;
RT "Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome
RT bc1.";
RL Nat. Struct. Mol. Biol. 26:78-83(2019).
RN [15]
RP STRUCTURE BY NMR, AND TOPOLOGY.
RX PubMed=29507228; DOI=10.1073/pnas.1712061115;
RA Zhou S., Pettersson P., Huang J., Sjoeholm J., Sjoestrand D., Pomes R.,
RA Hoegbom M., Brzezinski P., Maeler L., Aedelroth P.;
RT "Solution NMR structure of yeast Rcf1, a protein involved in respiratory
RT supercomplex formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:3048-3053(2018).
CC -!- FUNCTION: Assembly factor that plays a role in the assembly of the
CC respiratory chain supercomplexes (SCs) composed of ubiquinol-cytochrome
CC c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and
CC cytochrome c oxidase (complex IV, CIV). Involved in the recruitment of
CC COX13 and RCF2 into cytochrome c oxidase. May also be required for
CC late-stage assembly of the COX12 and COX13 subunits (PubMed:22342701,
CC PubMed:22405070, PubMed:22310663). Required for the generation and
CC maintenance of a normal proton motive force (PMF) across the inner
CC mitochondrial membrane (IMM) by preventing proton leakage through an
CC inactive population of CIV that accumulates when RCF1 and/or RCF2
CC proteins are absent (PubMed:30683696, PubMed:31591265).
CC {ECO:0000269|PubMed:22310663, ECO:0000269|PubMed:22342701,
CC ECO:0000269|PubMed:22405070, ECO:0000269|PubMed:30683696,
CC ECO:0000269|PubMed:31591265}.
CC -!- SUBUNIT: Associates with a subpopulation of the cytochrome bc1-
CC cytochrome c oxidase supercomplexes (PubMed:19750512, PubMed:22342701,
CC PubMed:22405070, PubMed:22310663). Associates in substoichiometric
CC amounts with complex IV (PubMed:22310663). Interacts with COX3
CC (PubMed:22310663). {ECO:0000269|PubMed:19750512,
CC ECO:0000269|PubMed:22310663, ECO:0000269|PubMed:22342701,
CC ECO:0000269|PubMed:22405070}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00836, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00836, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}.
CC -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss.
CC Promotes reactive oxygen species (ROS) generation.
CC {ECO:0000269|PubMed:19300474, ECO:0000269|PubMed:22342701}.
CC -!- MISCELLANEOUS: Present with 1210 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AIM31 family. {ECO:0000305}.
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DR EMBL; Z46659; CAA86625.1; -; Genomic_DNA.
DR EMBL; AY558234; AAS56560.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09868.1; -; Genomic_DNA.
DR PIR; S49749; S49749.
DR RefSeq; NP_013682.1; NM_001182388.1.
DR PDB; 5NF8; NMR; -; A/B=1-159.
DR PDBsum; 5NF8; -.
DR AlphaFoldDB; Q03713; -.
DR SMR; Q03713; -.
DR BioGRID; 35139; 328.
DR DIP; DIP-6835N; -.
DR IntAct; Q03713; 2.
DR STRING; 4932.YML030W; -.
DR TCDB; 8.A.112.1.1; the respiratory supercomplex factor (rcf) family.
DR MaxQB; Q03713; -.
DR PaxDb; Q03713; -.
DR PRIDE; Q03713; -.
DR EnsemblFungi; YML030W_mRNA; YML030W; YML030W.
DR GeneID; 854978; -.
DR KEGG; sce:YML030W; -.
DR SGD; S000004492; RCF1.
DR VEuPathDB; FungiDB:YML030W; -.
DR eggNOG; KOG4431; Eukaryota.
DR GeneTree; ENSGT00940000171730; -.
DR HOGENOM; CLU_087356_1_0_1; -.
DR InParanoid; Q03713; -.
DR OMA; REQLWIE; -.
DR BioCyc; YEAST:G3O-32631-MON; -.
DR PRO; PR:Q03713; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03713; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005746; C:mitochondrial respirasome; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IGI:SGD.
DR GO; GO:0097250; P:mitochondrial respirasome assembly; IMP:SGD.
DR GO; GO:0010155; P:regulation of proton transport; IMP:SGD.
DR InterPro; IPR007667; Hypoxia_induced_domain.
DR Pfam; PF04588; HIG_1_N; 1.
DR PROSITE; PS51503; HIG1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; Mitochondrion; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..159
FT /note="Respiratory supercomplex factor 1, mitochondrial"
FT /id="PRO_0000215779"
FT TOPO_DOM 1..13
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:29507228"
FT TRANSMEM 14..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:29507228"
FT TOPO_DOM 31..35
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:29507228"
FT TRANSMEM 36..57
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:29507228"
FT TOPO_DOM 58..63
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:29507228"
FT TRANSMEM 64..85
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:29507228"
FT TOPO_DOM 86..88
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:29507228"
FT TRANSMEM 89..106
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:29507228"
FT TOPO_DOM 107..133
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:29507228"
FT TRANSMEM 134..156
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:29507228"
FT TOPO_DOM 157..159
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:29507228"
FT DOMAIN 5..96
FT /note="HIG1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT COILED 88..159
FT /evidence="ECO:0000255"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:5NF8"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:5NF8"
FT HELIX 34..57
FT /evidence="ECO:0007829|PDB:5NF8"
FT HELIX 65..85
FT /evidence="ECO:0007829|PDB:5NF8"
FT HELIX 89..106
FT /evidence="ECO:0007829|PDB:5NF8"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5NF8"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:5NF8"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:5NF8"
FT HELIX 141..156
FT /evidence="ECO:0007829|PDB:5NF8"
SQ SEQUENCE 159 AA; 18477 MW; 86E57ABA0152402B CRC64;
MSRMPSSFDV TERDLDDMTF GERIIYHCKK QPLVPIGCLL TTGAVILAAQ NVRLGNKWKA
QYYFRWRVGL QAATLVALVA GSFIYGTSGK ELKAKEEQLK EKAKMREKLW IQELERREEE
TEARRKRAEL ARMKTLENEE EIKNLEKELS DLENKLGKK
