SDHF4_SCHPO
ID SDHF4_SCHPO Reviewed; 100 AA.
AC C6Y4C4;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Succinate dehydrogenase assembly factor 4, mitochondrial {ECO:0000250|UniProtKB:P38345};
DE Short=SDH assembly factor 4 {ECO:0000250|UniProtKB:P38345};
DE Short=SDHAF4 {ECO:0000250|UniProtKB:P38345};
DE Flags: Precursor;
GN ORFNames=SPBC26H8.16 {ECO:0000312|PomBase:SPBC26H8.16};
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 IDENTIFICATION.
RX PubMed=18488015; DOI=10.1038/nature07002;
RA Wilhelm B.T., Marguerat S., Watt S., Schubert F., Wood V., Goodhead I.,
RA Penkett C.J., Rogers J., Baehler J.;
RT "Dynamic repertoire of a eukaryotic transcriptome surveyed at single-
RT nucleotide resolution.";
RL Nature 453:1239-1243(2008).
CC -!- FUNCTION: Plays an essential role in the assembly of succinate
CC dehydrogenase (SDH), an enzyme complex (also referred to as respiratory
CC complex II) that is a component of both the tricarboxylic acid (TCA)
CC cycle and the mitochondrial electron transport chain, and which couples
CC the oxidation of succinate to fumarate with the reduction of ubiquinone
CC (coenzyme Q) to ubiquinol. Binds to the flavoprotein subunit sdh1 in
CC its FAD-bound form, blocking the generation of excess reactive oxigen
CC species (ROS) and facilitating its assembly with the iron-sulfur
CC protein subunit sdh2 into the SDH catalytic dimer.
CC {ECO:0000250|UniProtKB:P38345}.
CC -!- SUBUNIT: Interacts with sdh1 in its FAD-bound form.
CC {ECO:0000250|UniProtKB:P38345}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P38345}.
CC -!- SIMILARITY: Belongs to the SDHAF4 family. {ECO:0000305}.
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DR EMBL; CU329671; CBA11511.1; -; Genomic_DNA.
DR RefSeq; XP_002788943.1; XM_002788897.2.
DR AlphaFoldDB; C6Y4C4; -.
DR STRING; 4896.SPBC26H8.16.1; -.
DR MaxQB; C6Y4C4; -.
DR PaxDb; C6Y4C4; -.
DR EnsemblFungi; SPBC26H8.16.1; SPBC26H8.16.1:pep; SPBC26H8.16.
DR PomBase; SPBC26H8.16; -.
DR VEuPathDB; FungiDB:SPBC26H8.16; -.
DR eggNOG; ENOG502S6UN; Eukaryota.
DR HOGENOM; CLU_101052_2_1_1; -.
DR InParanoid; C6Y4C4; -.
DR OMA; PEFEGNI; -.
DR PRO; PR:C6Y4C4; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; ISO:PomBase.
DR InterPro; IPR012875; SDHF4.
DR Pfam; PF07896; DUF1674; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..100
FT /note="Succinate dehydrogenase assembly factor 4,
FT mitochondrial"
FT /id="PRO_0000389141"
FT REGION 24..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 100 AA; 11649 MW; 77AB9C6F413C060C CRC64;
MFNRNLRAVI LKNYNKALTR CLHDAGNLKR PTPPRLPKEQ QEEWDRLQKE SSKRPVDVMR
REKHKDFEGD VNPKTGEIGG PKSEPTVHGD YSYEGRVTDF
