KGD4_MOUSE
ID KGD4_MOUSE Reviewed; 102 AA.
AC Q9CQX8; Q4VA25;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Alpha-ketoglutarate dehydrogenase component 4 {ECO:0000303|PubMed:25165143};
GN Name=Mrps36; Synonyms=Kgd4 {ECO:0000303|PubMed:25165143};
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=Embryo, Heart, Pancreas, and Tongue;
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].
RC TISSUE=Mammary gland;
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=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-4, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP FUNCTION, IDENTIFICATION IN OGDC, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: May be necessary to recruit DLD/E3 to the mitochondrial 2-
CC oxoglutarate dehydrogenase complex (OGDC) core composed of OGDH/E1-
CC DLST/E2, hence stabilizes the complex. {ECO:0000305|PubMed:25165143}.
CC -!- SUBUNIT: Probable component of the 2-oxoglutarate dehydrogenase complex
CC (OGDC), composed of OGDH (2-oxoglutarate dehydrogenase; also called E1
CC subunit), DLST (dihydrolipoamide succinyltransferase; also called E2
CC subunit) and DLD (dihydrolipoamide dehydrogenase; also called E3
CC subunit) (Probable). Within OGDC, may interact (via N-terminus) with E3
CC subunit and (via C-terminus) with the complex core formed by E1 and E2
CC subunits (Probable). {ECO:0000305|PubMed:25165143}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:25165143}.
CC -!- CAUTION: Was originally identified in the small subunit (28S) of
CC mitochondrial ribosomes that were purified on sucrose gradients (By
CC similarity). This observation has been challenged by experiments
CC showing MRPS36 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, MRPS36 could not
CC be located in the structure of the human mitochondrial ribosome,
CC supporting the hypothesis that it is not a mitoribosomal protein (By
CC similarity). {ECO:0000250|UniProtKB:P82908,
CC ECO:0000250|UniProtKB:P82909, ECO:0000269|PubMed:25165143}.
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; AK003111; BAB22573.1; -; mRNA.
DR EMBL; AK003765; BAB22983.1; -; mRNA.
DR EMBL; AK007512; BAB25081.1; -; mRNA.
DR EMBL; AK009050; BAB26047.1; -; mRNA.
DR EMBL; BC028499; AAH28499.1; -; mRNA.
DR EMBL; BC096576; AAH96576.1; -; mRNA.
DR CCDS; CCDS36767.1; -.
DR RefSeq; NP_079645.1; NM_025369.3.
DR AlphaFoldDB; Q9CQX8; -.
DR SMR; Q9CQX8; -.
DR BioGRID; 211236; 25.
DR IntAct; Q9CQX8; 1.
DR STRING; 10090.ENSMUSP00000104957; -.
DR iPTMnet; Q9CQX8; -.
DR PhosphoSitePlus; Q9CQX8; -.
DR EPD; Q9CQX8; -.
DR jPOST; Q9CQX8; -.
DR MaxQB; Q9CQX8; -.
DR PaxDb; Q9CQX8; -.
DR PeptideAtlas; Q9CQX8; -.
DR PRIDE; Q9CQX8; -.
DR ProteomicsDB; 257050; -.
DR Antibodypedia; 23923; 192 antibodies from 28 providers.
DR DNASU; 66128; -.
DR Ensembl; ENSMUST00000109333; ENSMUSP00000104957; ENSMUSG00000061474.
DR GeneID; 66128; -.
DR KEGG; mmu:66128; -.
DR UCSC; uc007rrl.2; mouse.
DR CTD; 92259; -.
DR MGI; MGI:1913378; Mrps36.
DR VEuPathDB; HostDB:ENSMUSG00000061474; -.
DR eggNOG; ENOG502S7A7; Eukaryota.
DR GeneTree; ENSGT00390000017443; -.
DR InParanoid; Q9CQX8; -.
DR OMA; DRKGYPK; -.
DR OrthoDB; 1643642at2759; -.
DR PhylomeDB; Q9CQX8; -.
DR TreeFam; TF333436; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 66128; 5 hits in 51 CRISPR screens.
DR ChiTaRS; Mrps36; mouse.
DR PRO; PR:Q9CQX8; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9CQX8; protein.
DR Bgee; ENSMUSG00000061474; Expressed in primary oocyte and 63 other tissues.
DR ExpressionAtlas; Q9CQX8; baseline and differential.
DR Genevisible; Q9CQX8; MM.
DR GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IMP:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IMP:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IMP:UniProtKB.
DR InterPro; IPR020373; Kgd4/YMR-31.
DR PANTHER; PTHR31601; PTHR31601; 1.
DR Pfam; PF10937; S36_mt; 1.
PE 1: Evidence at protein level;
KW Acetylation; Mitochondrion; Phosphoprotein; Reference proteome;
KW Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..102
FT /note="Alpha-ketoglutarate dehydrogenase component 4"
FT /id="PRO_0000087734"
FT REGION 23..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82909"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P82909"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 102 AA; 11101 MW; 4582A0E4603BA764 CRC64;
MGSKMASATR VVQVVKPHAP LIKFPNRRDK PKLSASEALG SAALPSHSSA ISQHSKGSTS
PDLLMHQGPP DTAEIIKSLP QKYRRKPMSQ EEMEFIQRGG PE
