SDHF2_MOUSE
ID SDHF2_MOUSE Reviewed; 164 AA.
AC Q8C6I2; Q3TVE5; Q6PAS5; Q80ZJ9; Q8K2W8; Q9CYQ2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Succinate dehydrogenase assembly factor 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03057};
DE Short=SDH assembly factor 2 {ECO:0000255|HAMAP-Rule:MF_03057};
DE Short=SDHAF2 {ECO:0000255|HAMAP-Rule:MF_03057};
DE Flags: Precursor;
GN Name=Sdhaf2 {ECO:0000255|HAMAP-Rule:MF_03057};
GN Synonyms=Pgl2 {ECO:0000255|HAMAP-Rule:MF_03057},
GN Sdh5 {ECO:0000255|HAMAP-Rule:MF_03057};
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head, Kidney, and Stomach;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Embryo, Eye, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Required for flavinylation (covalent
CC attachment of FAD) of the flavoprotein subunit SDHA of the SDH
CC catalytic dimer. {ECO:0000255|HAMAP-Rule:MF_03057}.
CC -!- SUBUNIT: Interacts with SDHA within the SDH catalytic dimer.
CC {ECO:0000255|HAMAP-Rule:MF_03057}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03057}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C6I2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C6I2-2; Sequence=VSP_026634;
CC Name=3;
CC IsoId=Q8C6I2-3; Sequence=VSP_026633;
CC -!- SIMILARITY: Belongs to the SDHAF2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03057}.
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DR EMBL; AK160175; BAE35674.1; -; mRNA.
DR EMBL; AK013454; BAB28863.1; -; mRNA.
DR EMBL; AK075594; BAC35843.1; -; mRNA.
DR EMBL; AK160957; BAE36113.1; -; mRNA.
DR EMBL; AK167228; BAE39352.1; -; mRNA.
DR EMBL; BC029630; AAH29630.1; -; mRNA.
DR EMBL; BC038924; AAH38924.1; -; mRNA.
DR EMBL; BC048913; AAH48913.1; -; mRNA.
DR EMBL; BC060090; AAH60090.1; -; mRNA.
DR EMBL; BC085277; AAH85277.1; -; mRNA.
DR CCDS; CCDS29578.1; -. [Q8C6I2-1]
DR RefSeq; NP_079609.2; NM_025333.4. [Q8C6I2-1]
DR AlphaFoldDB; Q8C6I2; -.
DR SMR; Q8C6I2; -.
DR BioGRID; 211194; 5.
DR STRING; 10090.ENSMUSP00000025570; -.
DR iPTMnet; Q8C6I2; -.
DR PhosphoSitePlus; Q8C6I2; -.
DR EPD; Q8C6I2; -.
DR MaxQB; Q8C6I2; -.
DR PaxDb; Q8C6I2; -.
DR PeptideAtlas; Q8C6I2; -.
DR PRIDE; Q8C6I2; -.
DR ProteomicsDB; 257108; -. [Q8C6I2-1]
DR ProteomicsDB; 257109; -. [Q8C6I2-2]
DR ProteomicsDB; 257110; -. [Q8C6I2-3]
DR Antibodypedia; 51652; 62 antibodies from 23 providers.
DR Ensembl; ENSMUST00000025570; ENSMUSP00000025570; ENSMUSG00000024668. [Q8C6I2-1]
DR Ensembl; ENSMUST00000236455; ENSMUSP00000158166; ENSMUSG00000024668. [Q8C6I2-2]
DR GeneID; 66072; -.
DR KEGG; mmu:66072; -.
DR UCSC; uc008gpt.2; mouse. [Q8C6I2-1]
DR UCSC; uc008gpv.1; mouse. [Q8C6I2-2]
DR CTD; 54949; -.
DR MGI; MGI:1913322; Sdhaf2.
DR VEuPathDB; HostDB:ENSMUSG00000024668; -.
DR eggNOG; KOG3326; Eukaryota.
DR GeneTree; ENSGT00390000001149; -.
DR HOGENOM; CLU_103054_0_2_1; -.
DR InParanoid; Q8C6I2; -.
DR OMA; YGKPQNP; -.
DR OrthoDB; 1492851at2759; -.
DR PhylomeDB; Q8C6I2; -.
DR TreeFam; TF300175; -.
DR BioGRID-ORCS; 66072; 17 hits in 74 CRISPR screens.
DR ChiTaRS; Sdhaf2; mouse.
DR PRO; PR:Q8C6I2; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8C6I2; protein.
DR Bgee; ENSMUSG00000024668; Expressed in otic placode and 258 other tissues.
DR ExpressionAtlas; Q8C6I2; baseline and differential.
DR Genevisible; Q8C6I2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISS:UniProtKB.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IBA:GO_Central.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR GO; GO:0018293; P:protein-FAD linkage; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 1.10.150.250; -; 1.
DR HAMAP; MF_03057; SDHAF2; 1.
DR InterPro; IPR005631; SDH.
DR InterPro; IPR036714; SDH_sf.
DR InterPro; IPR028882; SDHAF2.
DR Pfam; PF03937; Sdh5; 1.
DR SUPFAM; SSF109910; SSF109910; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..164
FT /note="Succinate dehydrogenase assembly factor 2,
FT mitochondrial"
FT /id="PRO_0000294358"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026633"
FT VAR_SEQ 122..164
FT /note="EAKPAPEIFENEVMELLREFAKNKNKEQRLRAPDLEYLFEKPH -> GMPYA
FT ELHLGIIR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026634"
FT CONFLICT 27
FT /note="T -> K (in Ref. 1; BAB28863)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 164 AA; 19431 MW; CDC12D451D532BA4 CRC64;
MAVVTLIPTL ARALSKHSLL SPLPSVTSFR RFYRGDSPTD SQKDMIEIPL PPWQERTDES
IETKRARLLY ESRKRGMLEN CILLSLFAKE YLHNMTEKQL NLYDRLINEP SNDWDIYYWA
TEAKPAPEIF ENEVMELLRE FAKNKNKEQR LRAPDLEYLF EKPH
