ID   KGD4_YEAST              Reviewed;         123 AA.
AC   P19955; D6VTT2;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Alpha-ketoglutarate dehydrogenase subunit 4, mitochondrial {ECO:0000303|PubMed:25165143};
DE            Short=alpha-KGDH subunit 4;
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component 4;
DE            Short=OGDHC subunit 4;
DE   Flags: Precursor;
GN   Name=YMR31 {ECO:0000303|PubMed:2693936};
GN   Synonyms=KGD4 {ECO:0000303|PubMed:25165143};
GN   OrderedLocusNames=YFR049W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 9-32, AND SUBUNIT.
RC   STRAIN=ATCC 64665 / S288c / DC5;
RX   PubMed=2693936; DOI=10.1007/bf00261166;
RA   Matsushita Y., Kitakawa M., Isono K.;
RT   "Cloning and analysis of the nuclear genes for two mitochondrial ribosomal
RT   proteins in yeast.";
RL   Mol. Gen. Genet. 219:119-124(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA   Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA   Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT   cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8686379;
RX   DOI=10.1002/(sici)1097-0061(199602)12:2<149::aid-yea893>3.0.co;2-g;
RA   Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M.,
RA   Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.;
RT   "Analysis of a 36.2 kb DNA sequence including the right telomere of
RT   chromosome VI from Saccharomyces cerevisiae.";
RL   Yeast 12:149-167(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [9]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25165143; DOI=10.1091/mbc.e14-07-1178;
RA   Heublein M., Burguillos M.A., Voegtle F.N., Teixeira P.F., Imhof A.,
RA   Meisinger C., Ott M.;
RT   "The novel component Kgd4 recruits the E3 subunit to the mitochondrial
RT   alpha-ketoglutarate dehydrogenase.";
RL   Mol. Biol. Cell 25:3342-3349(2014).
RN   [10]
RP   ALTERNATIVE INITIATION.
RX   PubMed=30822412; DOI=10.1016/j.jmb.2019.02.023;
RA   Heublein M., Ndi M., Vazquez-Calvo C., Voegtle F.N., Ott M.;
RT   "Alternative translation initiation at a UUG codon gives rise to two
RT   functional variants of the mitochondrial protein Kgd4.";
RL   J. Mol. Biol. 431:1460-1467(2019).
CC   -!- FUNCTION: Molecular adapter that is necessary to a form a stable 2-
CC       oxoglutarate dehydrogenase enzyme complex (OGDC). Required for
CC       incorporation of the E3 subunit (LPD1) into the E1-E2 core (KGD1-KGD2)
CC       of mitochondrial OGDC, and acting as a stability factor for the fully
CC       assembled complex. {ECO:0000269|PubMed:25165143}.
CC   -!- SUBUNIT: Component of the 2-oxoglutarate dehydrogenase complex (OGDC),
CC       also called alpha-ketoglutarate dehydrogenase (KGDH) complex. The
CC       copmplex is composed of the catalytic subunits OGDH (2-oxoglutarate
CC       dehydrogenase KGD1; also called E1 subunit), DLST (dihydrolipoamide
CC       succinyltransferase KGD2; also called E2 subunit) and DLD
CC       (dihydrolipoamide dehydrogenase LPD1; also called E3 subunit), and the
CC       assembly factor KGD4. Within OGDC, interacts (via N-terminus) with E3
CC       subunit and (via C-terminus) with the complex core formed by E1 and E2
CC       subunits. {ECO:0000269|PubMed:25165143}.
CC   -!- INTERACTION:
CC       P19955; P09624: LPD1; NbExp=5; IntAct=EBI-16295, EBI-5940;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:25165143}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC         Comment=Isoform 2 derives from alternative initiation at an upstream
CC         UUG codon. The sequence context surrounding the codons dictates their
CC         use as alternative start sites. {ECO:0000269|PubMed:30822412};
CC       Name=1; Synonyms=Kgd4S {ECO:0000303|PubMed:30822412};
CC         IsoId=P19955-1; Sequence=Displayed;
CC       Name=2; Synonyms=Kgd4L {ECO:0000303|PubMed:30822412};
CC         IsoId=P19955-2; Sequence=VSP_061954;
CC   -!- DISRUPTION PHENOTYPE: Decreases OGDH activity in vitro without
CC       destabilizing the catalytic subunits. {ECO:0000269|PubMed:25165143}.
CC   -!- MISCELLANEOUS: Present with 2050 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase component
CC       4 family. {ECO:0000305}.
CC   -!- CAUTION: Was originally identified in the small subunit (28S) of
CC       mitochondrial ribosomes that were purified on sucrose gradients
CC       (PubMed:2693936). This observation has been challenged by experiments
CC       showing YMR31 copurification with the oxoglutarate dehydrogenase
CC       complex (OGDC), also called alpha-ketoglutarate dehydrogenase complex
CC       (KGDH). Both mitochondrial ribosome 28S subunit and OGDC have a similar
CC       size and OGDC is highly abundant, therefore OGDC has been found to
CC       contaminate ribosomal preparations performed by sequential
CC       centrifugation steps (PubMed:25165143). In addition, YMR31 could not be
CC       located in the structure of the yeast mitochondrial ribosome,
CC       supporting the hypothesis that it is not a mitoribosomal protein.
CC       {ECO:0000269|PubMed:25165143, ECO:0000269|PubMed:2693936, ECO:0000305}.
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DR   EMBL; X17540; CAA35577.1; -; Genomic_DNA.
DR   EMBL; D50617; BAA09288.1; -; Genomic_DNA.
DR   EMBL; AY558475; AAS56801.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12492.1; -; Genomic_DNA.
DR   PIR; JQ0368; JQ0368.
DR   RefSeq; NP_116707.3; NM_001180014.3. [P19955-1]
DR   AlphaFoldDB; P19955; -.
DR   BioGRID; 31207; 59.
DR   ComplexPortal; CPX-1293; Mitochondrial 2-oxoglutarate dehydrogenase complex.
DR   DIP; DIP-5447N; -.
DR   IntAct; P19955; 7.
DR   MINT; P19955; -.
DR   STRING; 4932.YFR049W; -.
DR   MaxQB; P19955; -.
DR   PaxDb; 4932-YFR049W; -.
DR   PeptideAtlas; P19955; -.
DR   EnsemblFungi; YFR049W_mRNA; YFR049W; YFR049W. [P19955-1]
DR   GeneID; 850610; -.
DR   KEGG; sce:YFR049W; -.
DR   AGR; SGD:S000001945; -.
DR   SGD; S000001945; YMR31.
DR   VEuPathDB; FungiDB:YFR049W; -.
DR   eggNOG; ENOG502S4IB; Eukaryota.
DR   HOGENOM; CLU_1981974_0_0_1; -.
DR   InParanoid; P19955; -.
DR   OMA; AKSYTPM; -.
DR   OrthoDB; 2016387at2759; -.
DR   BioCyc; YEAST:G3O-30495-MONOMER; -.
DR   BioGRID-ORCS; 850610; 10 hits in 10 CRISPR screens.
DR   PRO; PR:P19955; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P19955; Protein.
DR   GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IPI:ComplexPortal.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:ComplexPortal.
DR   GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IDA:SGD.
DR   GO; GO:0005761; C:mitochondrial ribosome; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:ComplexPortal.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IMP:SGD.
DR   InterPro; IPR020373; Kgd4/YMR-31.
DR   PANTHER; PTHR31601; 28S RIBOSOMAL PROTEIN S36, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR31601:SF2; ALPHA-KETOGLUTARATE DEHYDROGENASE COMPONENT 4; 1.
DR   Pfam; PF10937; Kgd4-YMR31; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; Direct protein sequencing; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..8
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2693936"
FT   CHAIN           9..123
FT                   /note="Alpha-ketoglutarate dehydrogenase subunit 4,
FT                   mitochondrial"
FT                   /id="PRO_0000030587"
FT   VAR_SEQ         1
FT                   /note="M -> MNSLKQTIKEYFPRFLTDNKSKIKVQEDREM (in isoform 2)"
FT                   /id="VSP_061954"
SQ   SEQUENCE   123 AA;  13689 MW;  25E491375CE7A137 CRC64;
     MIATPIRLAK SAYEPMIKFV GTRHPLVKHA TEVVVHPCAT NGMLPGSKEC IPVSKFMENY
     KPFRVVPIKH SANAGLSSSK TSVFVNRPLQ KDELASIFEL PARFRYKPIN EHELESINSG
     GAW
//