SHH3_YEAST
ID SHH3_YEAST Reviewed; 196 AA.
AC Q04487; D6VZU1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Mitochondrial inner membrane protein SHH3 {ECO:0000305};
DE AltName: Full=SDH3 homolog {ECO:0000303|PubMed:22152483};
DE Flags: Precursor;
GN Name=SHH3 {ECO:0000303|PubMed:22152483};
GN OrderedLocusNames=YMR118C {ECO:0000312|SGD:S000004724};
GN ORFNames=YM9718.17C;
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 DISRUPTION PHENOTYPE.
RX PubMed=22152483; DOI=10.1016/j.molcel.2011.09.025;
RA Gebert N., Gebert M., Oeljeklaus S., von der Malsburg K., Stroud D.A.,
RA Kulawiak B., Wirth C., Zahedi R.P., Dolezal P., Wiese S., Simon O.,
RA Schulze-Specking A., Truscott K.N., Sickmann A., Rehling P., Guiard B.,
RA Hunte C., Warscheid B., van der Laan M., Pfanner N., Wiedemann N.;
RT "Dual function of Sdh3 in the respiratory chain and TIM22 protein
RT translocase of the mitochondrial inner membrane.";
RL Mol. Cell 44:811-818(2011).
CC -!- FUNCTION: Homolog of SDH3, but seems not to be a stoichiometric subunit
CC of either the succinate dehydrogenase (SDH) complex or the
CC mitochondrial inner membrane translocase TIM22 complex.
CC {ECO:0000303|PubMed:22152483}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P33421}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Does not affect SDH or TIM22 complex formation.
CC {ECO:0000269|PubMed:22152483}.
CC -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
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DR EMBL; Z49702; CAA89756.1; -; Genomic_DNA.
DR EMBL; AY557968; AAS56294.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10015.1; -; Genomic_DNA.
DR PIR; S54580; S54580.
DR RefSeq; NP_013836.1; NM_001182618.1.
DR AlphaFoldDB; Q04487; -.
DR SMR; Q04487; -.
DR BioGRID; 35294; 48.
DR DIP; DIP-5316N; -.
DR MINT; Q04487; -.
DR STRING; 4932.YMR118C; -.
DR PaxDb; Q04487; -.
DR PRIDE; Q04487; -.
DR EnsemblFungi; YMR118C_mRNA; YMR118C; YMR118C.
DR GeneID; 855145; -.
DR KEGG; sce:YMR118C; -.
DR SGD; S000004724; SHH3.
DR VEuPathDB; FungiDB:YMR118C; -.
DR eggNOG; KOG0449; Eukaryota.
DR GeneTree; ENSGT00390000000566; -.
DR HOGENOM; CLU_094691_0_0_1; -.
DR InParanoid; Q04487; -.
DR OMA; IHTAKSA; -.
DR BioCyc; YEAST:G3O-32813-MON; -.
DR PRO; PR:Q04487; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04487; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR018495; Succ_DH_cyt_bsu_CS.
DR InterPro; IPR014314; Succ_DH_cytb556.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR PANTHER; PTHR10978; PTHR10978; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
DR TIGRFAMs; TIGR02970; succ_dehyd_cytB; 1.
DR PROSITE; PS01000; SDH_CYT_1; 1.
DR PROSITE; PS01001; SDH_CYT_2; 1.
PE 3: Inferred from homology;
KW Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Quinone; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 54..196
FT /note="Mitochondrial inner membrane protein SHH3"
FT /id="PRO_0000003639"
FT TOPO_DOM 54..97
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P33421"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..137
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P33421"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..174
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P33421"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P33421"
FT BINDING 91
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P33421"
FT BINDING 95
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P33421"
FT BINDING 154
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P33421"
SQ SEQUENCE 196 AA; 22309 MW; 41413998B9B2B057 CRC64;
MKATIQRVTS VFGVPRASVF VPRISTPFIL HNYISNGRMD LFSKEFHNGR VSKSDLWSSN
KEEELLVSQR KKRPISPHLT VYEPEMSWYL SSLHRISGVL LALGFYAFTI TLGVTTIMGM
DTTFQDLNKW YHEKMPKWSQ WVAKGSAAYL FAFHFGNGIR HLIWDMGYEL TNRGVIKTGS
IVLAGTLVLG TYLLAQ
