DHSD_SCHPO
ID DHSD_SCHPO Reviewed; 159 AA.
AC Q9P7X0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;
DE Short=CybS;
DE AltName: Full=Succinate-ubiquinone reductase membrane anchor subunit;
DE Flags: Precursor;
GN Name=sdh4; Synonyms=tim18; ORFNames=SPBP23A10.16;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP INDUCTION.
RX PubMed=16963626; DOI=10.1128/ec.00199-06;
RA Mercier A., Pelletier B., Labbe S.;
RT "A transcription factor cascade involving Fep1 and the CCAAT-binding factor
RT Php4 regulates gene expression in response to iron deficiency in the
RT fission yeast Schizosaccharomyces pombe.";
RL Eukaryot. Cell 5:1866-1881(2006).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH)
CC that is involved in complex II of the mitochondrial electron transport
CC chain and is responsible for transferring electrons from succinate to
CC ubiquinone (coenzyme Q). {ECO:0000250}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC -!- SUBUNIT: Forms part of complex II containing four subunits: a
CC flavoprotein (FP), an iron-sulfur protein (IP) and a cytochrome b
CC composed of a large and a small subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: Expression is down-regulated under conditions of iron
CC depletion. {ECO:0000269|PubMed:16963626}.
CC -!- SIMILARITY: Belongs to the CybS family. {ECO:0000305}.
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DR EMBL; CU329671; CAB66444.2; -; Genomic_DNA.
DR PIR; T50403; T50403.
DR RefSeq; NP_595828.2; NM_001021732.2.
DR AlphaFoldDB; Q9P7X0; -.
DR SMR; Q9P7X0; -.
DR BioGRID; 277804; 181.
DR ComplexPortal; CPX-566; Mitochondrial respiratory chain complex II.
DR STRING; 4896.SPBP23A10.16.1; -.
DR MaxQB; Q9P7X0; -.
DR PaxDb; Q9P7X0; -.
DR EnsemblFungi; SPBP23A10.16.1; SPBP23A10.16.1:pep; SPBP23A10.16.
DR GeneID; 2541292; -.
DR KEGG; spo:SPBP23A10.16; -.
DR PomBase; SPBP23A10.16; sdh4.
DR VEuPathDB; FungiDB:SPBP23A10.16; -.
DR eggNOG; KOG4097; Eukaryota.
DR HOGENOM; CLU_096618_0_2_1; -.
DR InParanoid; Q9P7X0; -.
DR OMA; SEGSYHW; -.
DR Reactome; R-SPO-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; -.
DR PRO; PR:Q9P7X0; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; ISS:PomBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; ISS:PomBase.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043495; F:protein-membrane adaptor activity; NAS:PomBase.
DR GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISO:PomBase.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISS:PomBase.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:PomBase.
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 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..159
FT /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT small subunit, mitochondrial"
FT /id="PRO_0000006495"
FT TOPO_DOM 31..65
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..89
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..122
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..159
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 99
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with large subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with IP"
FT /evidence="ECO:0000250"
SQ SEQUENCE 159 AA; 17744 MW; A4677656920A96C9 CRC64;
MLQTRLGLGA LRQGRLLFAV KSFSTTSVAK IFPPPPQTIK GTVNDAAVFP HHSKLHGSYH
WDFERIIAIA MVPQVMIPLF TGTSHPLMDA ALACTLITHA HLGFESCVID YFPARRFKKL
SPLMHWILRG CTVLTLIGVY EFNTNDIGLT EGIKKLWKS
