SDHF3_RAT
ID SDHF3_RAT Reviewed; 125 AA.
AC Q6TUF2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 86.
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 AltName: Full=Liver regeneration-related protein LRRGT00092;
DE Flags: Precursor;
GN Name=Sdhaf3 {ECO:0000250|UniProtKB:Q9NRP4};
GN Synonyms=Acn9 {ECO:0000250|UniProtKB:Q9NRP4};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Xu C.S., Chang C.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J.,
RA Zhao L.F., Ma H., Wang L., Wang S.F., Xing X.K., Shen G.M., Shi J.B.,
RA Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6TUF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6TUF2-2; Sequence=VSP_016050;
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; AY387078; AAQ91048.1; -; mRNA.
DR EMBL; AABR03035336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03033448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001041379.1; NM_001047914.1. [Q6TUF2-2]
DR AlphaFoldDB; Q6TUF2; -.
DR SMR; Q6TUF2; -.
DR STRING; 10116.ENSRNOP00000015286; -.
DR PaxDb; Q6TUF2; -.
DR Ensembl; ENSRNOT00000015286; ENSRNOP00000015286; ENSRNOG00000011283. [Q6TUF2-1]
DR GeneID; 362323; -.
DR KEGG; rno:362323; -.
DR UCSC; RGD:1305143; rat. [Q6TUF2-1]
DR CTD; 57001; -.
DR RGD; 1305143; Sdhaf3.
DR eggNOG; KOG4100; Eukaryota.
DR GeneTree; ENSGT00390000010029; -.
DR HOGENOM; CLU_102310_2_1_1; -.
DR InParanoid; Q6TUF2; -.
DR OMA; LTEWQMY; -.
DR OrthoDB; 1613308at2759; -.
DR PhylomeDB; Q6TUF2; -.
DR TreeFam; TF105635; -.
DR PRO; PR:Q6TUF2; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000011283; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; Q6TUF2; RN.
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 Alternative splicing; Chaperone; Mitochondrion; Reference proteome;
KW 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_0000042712"
FT VAR_SEQ 1..58
FT /note="MTGRHVSRVRSLYRRILQLHRALPPDLKALGDQYVKDEFRRHKTVGPGEAQR
FT FLKEWE -> MARSGWQKFDCVVVTARGSDTSTLAKDADENRPPSFGSFGGNEI (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016050"
SQ SEQUENCE 125 AA; 14525 MW; B7CEAAADA68269DC CRC64;
MTGRHVSRVR SLYRRILQLH RALPPDLKAL GDQYVKDEFR RHKTVGPGEA QRFLKEWETY
AAVLWQQAKD SRQSSSGKAC FGTSLPEEKL NDFRDEQIGQ LQELMQEATK PNRQFSITES
TKPHL
