SHH4_YEAST
ID SHH4_YEAST Reviewed; 168 AA.
AC Q06236; D6VYH0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Mitochondrial inner membrane protein SHH4 {ECO:0000305};
DE AltName: Full=SDH4 homolog {ECO:0000303|PubMed:22152483};
DE Flags: Precursor;
GN Name=SHH4 {ECO:0000303|PubMed:22152483};
GN OrderedLocusNames=YLR164W {ECO:0000312|SGD:S000004154};
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 SUBCELLULAR LOCATION.
RX PubMed=10637294; DOI=10.1091/mbc.11.1.103;
RA Kerscher O., Sepuri N.B., Jensen R.E.;
RT "Tim18p is a new component of the Tim54p-Tim22p translocon in the
RT mitochondrial inner membrane.";
RL Mol. Biol. Cell 11:103-116(2000).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH SDH3, AND 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 SDH4, 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 -!- SUBUNIT: Interacts with SDH3. {ECO:0000269|PubMed:22152483}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10637294, ECO:0000269|PubMed:22152483}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Does not affect SDH or TIM22 complex formation.
CC {ECO:0000269|PubMed:22152483}.
CC -!- SIMILARITY: Belongs to the CybS family. {ECO:0000305}.
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DR EMBL; U51921; AAB67488.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09486.1; -; Genomic_DNA.
DR PIR; S68480; S68480.
DR RefSeq; NP_013265.1; NM_001182051.1.
DR AlphaFoldDB; Q06236; -.
DR SMR; Q06236; -.
DR BioGRID; 31437; 46.
DR DIP; DIP-5582N; -.
DR STRING; 4932.YLR164W; -.
DR PaxDb; Q06236; -.
DR PRIDE; Q06236; -.
DR EnsemblFungi; YLR164W_mRNA; YLR164W; YLR164W.
DR GeneID; 850861; -.
DR KEGG; sce:YLR164W; -.
DR SGD; S000004154; SHH4.
DR VEuPathDB; FungiDB:YLR164W; -.
DR eggNOG; KOG4097; Eukaryota.
DR GeneTree; ENSGT00940000176639; -.
DR HOGENOM; CLU_096618_0_0_1; -.
DR InParanoid; Q06236; -.
DR OMA; CGTILMH; -.
DR BioCyc; YEAST:G3O-32294-MON; -.
DR ChiTaRS; SHH4; yeast.
DR PRO; PR:Q06236; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06236; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IGI:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048039; F:ubiquinone binding; IBA:GO_Central.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IGI:SGD.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd03496; SQR_TypeC_CybS; 1.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR007992; CybS.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR PANTHER; PTHR13337; PTHR13337; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..168
FT /note="Mitochondrial inner membrane protein SHH4"
FT /id="PRO_0000268180"
FT TOPO_DOM 24..65
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q08749"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..92
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q08749"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..120
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q08749"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..168
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q08749"
FT BINDING 101
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:P37298"
FT BINDING 112
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P37298"
SQ SEQUENCE 168 AA; 18632 MW; 296AE82172DE9DCD CRC64;
MSSTKFLKPL CRIRAFHTSI ARSFTIPFLP KIPQKPGGVS GTANDSSYMP PESRAQGSYH
WIVERGLSLA VLPLIAVPLV TTGPISTFTD TFLSLVLLGH CHIGFQSCII DYISERVYGK
VHHYAMYLLS LGSFLSFVGI YKLESQEAGL IASLKSLWDN KPVEKKRQ
