ID   Q91VA7_MOUSE            Unreviewed;       384 AA.
AC   Q91VA7;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] subunit, mitochondrial {ECO:0000256|RuleBase:RU361266};
GN   Name=Idh3b {ECO:0000313|EMBL:AAH09022.1,
GN   ECO:0000313|Ensembl:ENSMUSP00000028892.5,
GN   ECO:0000313|MGI:MGI:2158650};
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 {ECO:0000313|EMBL:AAK64606.1};
RN   [1] {ECO:0000313|EMBL:AAK64606.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Swiss {ECO:0000313|EMBL:AAK64606.1};
RA   Yang J.S., Chen S.S., Zheng X.M.;
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAH09022.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI {ECO:0000313|EMBL:AAH09022.1};
RC   TISSUE=Mammary tumor. WAP-Tag model. 5 months old
RC   {ECO:0000313|EMBL:AAH09022.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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] {ECO:0000313|Ensembl:ENSMUSP00000028892.5, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000028892.5,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [5] {ECO:0000313|Ensembl:ENSMUSP00000028892.5}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000028892.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Plays a structural role to facilitate the assembly and ensure
CC       the full activity of the enzyme catalyzing the decarboxylation of
CC       isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of
CC       the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer
CC       composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have
CC       considerable basal activity but the full activity of the heterotetramer
CC       (containing two subunits of IDH3A, one of IDH3B and one of IDH3G)
CC       requires the assembly and cooperative function of both heterodimers.
CC       {ECO:0000256|ARBA:ARBA00037063}.
CC   -!- SUBUNIT: Heterooligomer of subunits alpha (IDH3A), beta (IDH3B), and
CC       gamma (IDH3G) in the apparent ratio of 2:1:1. The heterodimer
CC       containing one IDH3A and one IDH3B subunit and the heterodimer
CC       containing one IDH3A and one IDH3G subunit assemble into a
CC       heterotetramer (which contains two subunits of IDH3A, one of IDH3B and
CC       one of IDH3G) and further into the heterooctamer.
CC       {ECO:0000256|ARBA:ARBA00011525}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|RuleBase:RU361266}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769,
CC       ECO:0000256|RuleBase:RU361266}.
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; BC009022; AAH09022.1; -; mRNA.
DR   EMBL; AY035212; AAK64606.1; -; mRNA.
DR   RefSeq; NP_570954.1; NM_130884.4.
DR   ComplexPortal; CPX-556; Mitochondrial isocitrate dehydrogenase complex (NAD+).
DR   IntAct; Q91VA7; 7.
DR   STRING; 10090.ENSMUSP00000028892; -.
DR   PaxDb; 10090-ENSMUSP00000028892; -.
DR   ProteomicsDB; 342887; -.
DR   Antibodypedia; 23248; 286 antibodies from 32 providers.
DR   DNASU; 170718; -.
DR   Ensembl; ENSMUST00000028892.11; ENSMUSP00000028892.5; ENSMUSG00000027406.14.
DR   GeneID; 170718; -.
DR   UCSC; uc008min.2; mouse.
DR   AGR; MGI:2158650; -.
DR   CTD; 3420; -.
DR   MGI; MGI:2158650; Idh3b.
DR   VEuPathDB; HostDB:ENSMUSG00000027406; -.
DR   eggNOG; KOG0784; Eukaryota.
DR   GeneTree; ENSGT00950000182989; -.
DR   HOGENOM; CLU_031953_0_1_1; -.
DR   OMA; TCAHKAN; -.
DR   OrthoDB; 143577at2759; -.
DR   TreeFam; TF315033; -.
DR   Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR   BioGRID-ORCS; 170718; 6 hits in 77 CRISPR screens.
DR   ChiTaRS; Idh3b; mouse.
DR   PRO; PR:Q91VA7; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000027406; Expressed in interventricular septum and 260 other cell types or tissues.
DR   GO; GO:0005962; C:mitochondrial isocitrate dehydrogenase complex (NAD+); IMP:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; ISO:MGI.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; ISO:MGI.
DR   GO; GO:0006102; P:isocitrate metabolic process; ISO:MGI.
DR   GO; GO:0006734; P:NADH metabolic process; ISO:MGI.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISO:MGI.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004434; Isocitrate_DH_NAD.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   NCBIfam; TIGR00175; mito_nad_idh; 1.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF80; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Mitochondrion {ECO:0000256|RuleBase:RU361266};
KW   Proteomics identification {ECO:0007829|EPD:Q91VA7,
KW   ECO:0007829|MaxQB:Q91VA7};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU361266};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU361266}.
FT   DOMAIN          49..375
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   384 AA;  42195 MW;  49162354C2A4DFBE CRC64;
     MAALSNVRWL TRAVLAARNS GAWRGLGTST AHAASQSQAQ DVRVEGAFPV TMLPGDGVGP
     ELMHAVKEVF KAAAVPVEFK EHHLSEVQNM ASEEKLEQVL SSMKENKVAI IGKIYTPMEY
     KGELASYDMQ LRRKLDLFAN VVHVKSLPGY KTRHNNLDLV IIREQTEGEY SSLEHESAKG
     VIECLKIVTR TKSQRIAKFA FDYATKKGRS KVTAVHKANI MKLGDGLFLQ CCEEVAELYP
     KIKFETMIID NCCMQLVQNP YQFDVLVMPN LYGNIIDNLA AGLVGGAGVV PGESYSAEYA
     VFETGARHPF AQAVGRNIAN PTAMLLSATN MLRHLNLEYH SSMIADAVKK VIKAGKVRTR
     DMGGYSTTTD FIKSVIGHLH PHGG
//