SDHF3_MOUSE
ID SDHF3_MOUSE Reviewed; 125 AA.
AC Q8BQU3; Q8BT21;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Succinate dehydrogenase assembly factor 3, mitochondrial {ECO:0000250|UniProtKB:Q04401};
DE Short=SDH assembly factor 3 {ECO:0000250|UniProtKB:Q04401};
DE Short=SDHAF3 {ECO:0000250|UniProtKB:Q04401};
DE Flags: Precursor;
GN Name=Sdhaf3 {ECO:0000250|UniProtKB:Q9NRP4};
GN Synonyms=Acn9 {ECO:0000250|UniProtKB:Q9NRP4};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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. Promotes maturation of the iron-sulfur
CC protein subunit Sdhb of the SDH catalytic dimer, protecting it from the
CC deleterious effects of oxidants. May act together with SDHAF1.
CC {ECO:0000250|UniProtKB:Q04401, ECO:0000250|UniProtKB:Q8SZ16}.
CC -!- SUBUNIT: Interacts with Sdhb within an Sdha-Sdhb subcomplex.
CC {ECO:0000250|UniProtKB:Q04401}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q04401}.
CC -!- SIMILARITY: Belongs to the complex I LYR family. SDHAF3 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK028031; BAC25710.1; -; mRNA.
DR EMBL; AK046436; BAC32728.1; -; mRNA.
DR CCDS; CCDS39423.1; -.
DR RefSeq; NP_001071181.1; NM_001077713.1.
DR AlphaFoldDB; Q8BQU3; -.
DR SMR; Q8BQU3; -.
DR BioGRID; 214573; 9.
DR STRING; 10090.ENSMUSP00000040935; -.
DR PhosphoSitePlus; Q8BQU3; -.
DR MaxQB; Q8BQU3; -.
DR PaxDb; Q8BQU3; -.
DR PRIDE; Q8BQU3; -.
DR ProteomicsDB; 255506; -.
DR Antibodypedia; 55557; 71 antibodies from 14 providers.
DR Ensembl; ENSMUST00000040826; ENSMUSP00000040935; ENSMUSG00000042505.
DR GeneID; 71238; -.
DR KEGG; mmu:71238; -.
DR UCSC; uc009axa.1; mouse.
DR CTD; 57001; -.
DR MGI; MGI:1913288; Sdhaf3.
DR VEuPathDB; HostDB:ENSMUSG00000042505; -.
DR eggNOG; KOG4100; Eukaryota.
DR GeneTree; ENSGT00390000010029; -.
DR HOGENOM; CLU_102310_2_1_1; -.
DR InParanoid; Q8BQU3; -.
DR OMA; LTEWQMY; -.
DR OrthoDB; 1613308at2759; -.
DR PhylomeDB; Q8BQU3; -.
DR TreeFam; TF105635; -.
DR BioGRID-ORCS; 71238; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Sdhaf3; mouse.
DR PRO; PR:Q8BQU3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BQU3; protein.
DR Bgee; ENSMUSG00000042505; Expressed in facial nucleus and 220 other tissues.
DR ExpressionAtlas; Q8BQU3; baseline and differential.
DR Genevisible; Q8BQU3; MM.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:HGNC-UCL.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IBA:GO_Central.
DR GO; GO:0006105; P:succinate metabolic process; IBA:GO_Central.
DR InterPro; IPR008381; SDHAF3/Sdh7.
DR PANTHER; PTHR13137; PTHR13137; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..125
FT /note="Succinate dehydrogenase assembly factor 3,
FT mitochondrial"
FT /id="PRO_0000042654"
SQ SEQUENCE 125 AA; 14468 MW; 46787E6C1C74E3ED CRC64;
MPGKHVSRVR ALYRRILLLH RALPPDLKAL GDQYVKDEFR RHKTVGPGEA QRFLKEWETY
AAVLWQQAED SRQSSTGKAC FGTSLPEEKL NDFRDEQIGQ LQELMQEATK PNRQFSITES
TKPQL
