SDHF4_HUMAN
ID SDHF4_HUMAN Reviewed; 108 AA.
AC Q5VUM1; E1P532;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Succinate dehydrogenase assembly factor 4, mitochondrial {ECO:0000303|PubMed:24954416, ECO:0000312|HGNC:HGNC:20957};
DE Short=SDH assembly factor 4 {ECO:0000303|PubMed:24954416};
DE Short=SDHAF4 {ECO:0000303|PubMed:24954416};
DE Flags: Precursor;
GN Name=SDHAF4 {ECO:0000303|PubMed:24954416, ECO:0000312|HGNC:HGNC:20957};
GN Synonyms=C6orf57;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=24954416; DOI=10.1016/j.cmet.2014.05.012;
RA Van Vranken J.G., Bricker D.K., Dephoure N., Gygi S.P., Cox J.E.,
RA Thummel C.S., Rutter J.;
RT "SDHAF4 promotes mitochondrial succinate dehydrogenase activity and
RT prevents neurodegeneration.";
RL Cell Metab. 20:241-252(2014).
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 (PubMed:24954416). Binds to the flavoprotein
CC subunit SDHA in its FAD-bound form, blocking the generation of excess
CC reactive oxigen species (ROS) and facilitating its assembly with the
CC iron-sulfur protein subunit SDHB into the SDH catalytic dimer (By
CC similarity). {ECO:0000250|UniProtKB:P38345,
CC ECO:0000269|PubMed:24954416}.
CC -!- SUBUNIT: Interacts with SDHA in its FAD-bound form.
CC {ECO:0000250|UniProtKB:P38345}.
CC -!- INTERACTION:
CC Q5VUM1; P60033: CD81; NbExp=3; IntAct=EBI-16769525, EBI-712921;
CC Q5VUM1; O43169: CYB5B; NbExp=3; IntAct=EBI-16769525, EBI-1058710;
CC Q5VUM1; O75841: UPK1B; NbExp=3; IntAct=EBI-16769525, EBI-12237619;
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; AL583856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48810.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48812.1; -; Genomic_DNA.
DR EMBL; BC104649; AAI04650.1; -; mRNA.
DR CCDS; CCDS4972.1; -.
DR RefSeq; NP_660310.2; NM_145267.2.
DR AlphaFoldDB; Q5VUM1; -.
DR SMR; Q5VUM1; -.
DR BioGRID; 126423; 11.
DR IntAct; Q5VUM1; 11.
DR STRING; 9606.ENSP00000359505; -.
DR iPTMnet; Q5VUM1; -.
DR PhosphoSitePlus; Q5VUM1; -.
DR BioMuta; SDHAF4; -.
DR DMDM; 74747126; -.
DR EPD; Q5VUM1; -.
DR jPOST; Q5VUM1; -.
DR MassIVE; Q5VUM1; -.
DR MaxQB; Q5VUM1; -.
DR PaxDb; Q5VUM1; -.
DR PeptideAtlas; Q5VUM1; -.
DR PRIDE; Q5VUM1; -.
DR ProteomicsDB; 65425; -.
DR TopDownProteomics; Q5VUM1; -.
DR Antibodypedia; 31244; 42 antibodies from 10 providers.
DR DNASU; 135154; -.
DR Ensembl; ENST00000370474.4; ENSP00000359505.3; ENSG00000154079.6.
DR GeneID; 135154; -.
DR KEGG; hsa:135154; -.
DR MANE-Select; ENST00000370474.4; ENSP00000359505.3; NM_145267.3; NP_660310.2.
DR UCSC; uc003pfq.2; human.
DR CTD; 135154; -.
DR DisGeNET; 135154; -.
DR GeneCards; SDHAF4; -.
DR HGNC; HGNC:20957; SDHAF4.
DR HPA; ENSG00000154079; Low tissue specificity.
DR MIM; 619198; gene.
DR neXtProt; NX_Q5VUM1; -.
DR OpenTargets; ENSG00000154079; -.
DR PharmGKB; PA134932684; -.
DR VEuPathDB; HostDB:ENSG00000154079; -.
DR eggNOG; KOG3245; Eukaryota.
DR GeneTree; ENSGT00390000009155; -.
DR HOGENOM; CLU_160299_0_0_1; -.
DR InParanoid; Q5VUM1; -.
DR OMA; SLLCHSR; -.
DR OrthoDB; 1530126at2759; -.
DR PhylomeDB; Q5VUM1; -.
DR TreeFam; TF106123; -.
DR PathwayCommons; Q5VUM1; -.
DR SignaLink; Q5VUM1; -.
DR BioGRID-ORCS; 135154; 13 hits in 1006 CRISPR screens.
DR ChiTaRS; SDHAF4; human.
DR GenomeRNAi; 135154; -.
DR Pharos; Q5VUM1; Tbio.
DR PRO; PR:Q5VUM1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5VUM1; protein.
DR Bgee; ENSG00000154079; Expressed in hindlimb stylopod muscle and 169 other tissues.
DR Genevisible; Q5VUM1; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; ISS:UniProtKB.
DR GO; GO:0045333; P:cellular respiration; IGI:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IGI:UniProtKB.
DR GO; GO:1904231; P:positive regulation of succinate dehydrogenase activity; IEA:Ensembl.
DR InterPro; IPR012875; SDHF4.
DR Pfam; PF07896; DUF1674; 1.
PE 1: Evidence at protein level;
KW Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..108
FT /note="Succinate dehydrogenase assembly factor 4,
FT mitochondrial"
FT /id="PRO_0000244340"
FT REGION 31..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 46
FT /note="Q -> R (in dbSNP:rs1048886)"
FT /id="VAR_026890"
FT VARIANT 57
FT /note="R -> C (in dbSNP:rs34711085)"
FT /id="VAR_053598"
SQ SEQUENCE 108 AA; 12213 MW; 4D782514AA9D4FCE CRC64;
MTPSRLPWLL SWVSATAWRA ARSPLLCHSL RKTSSSQGGK SELVKQSLKK PKLPEGRFDA
PEDSHLEKEP LEKFPDDVNP VTKEKGGPRG PEPTRYGDWE RKGRCIDF
