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Hydroxymethylglutaryl-CoA lyase, mitochondrial (HL) (HMG-CoA lyase) (EC 4.1.3.4) (3-hydroxy-3-methylglutarate-CoA lyase)

 HMGCL_MOUSE             Reviewed;         325 AA.
P38060; Q8QZS6;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
20-JUN-2018, entry version 140.
RecName: Full=Hydroxymethylglutaryl-CoA lyase, mitochondrial;
Short=HL;
Short=HMG-CoA lyase;
EC=4.1.3.4;
AltName: Full=3-hydroxy-3-methylglutarate-CoA lyase;
Flags: Precursor;
Name=Hmgcl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8102917; DOI=10.1007/BF00360589;
Wang S., Nadeau J.H., Duncan A., Robert M.-F., Fontaine G.,
Schappert K., Johnson K.R., Zietkiewicz E., Hruz P., Miziorko H.;
"3-hydroxy-3-methylglutaryl coenzyme A lyase (HL): cloning and
characterization of a mouse liver HL cDNA and subchromosomal mapping
of the human and mouse HL genes.";
Mamm. Genome 4:382-387(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129;
PubMed=8617516; DOI=10.1006/geno.1996.0164;
Wang S.P., Robert M.-F., Gibson K.M., Wanders R.J.A., Mitchell G.A.;
"3-hydroxy-3-methylglutaryl CoA lyase (HL): mouse and human HL gene
(HMGCL) cloning and detection of large gene deletions in two unrelated
HL-deficient patients.";
Genomics 33:99-104(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Hippocampus, Mammary gland, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
SUBCELLULAR LOCATION.
PubMed=7527399;
Ashmarina L.I., Rusnak N., Miziorko H.M., Mitchell G.A.;
"3-Hydroxy-3-methylglutaryl-CoA lyase is present in mouse and human
liver peroxisomes.";
J. Biol. Chem. 269:31929-31932(1994).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48, SUCCINYLATION [LARGE
SCALE ANALYSIS] AT LYS-48; LYS-137 AND LYS-179, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast, and Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-111; LYS-137;
LYS-179 AND LYS-324, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- FUNCTION: Key enzyme in ketogenesis (ketone body formation).
Terminal step in leucine catabolism. Ketone bodies (beta-
hydroxybutyrate, acetoacetate and acetone) are essential as an
alternative source of energy to glucose, as lipid precursors and
as regulators of metabolism (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-
CoA + acetoacetate. {ECO:0000255|PROSITE-ProRule:PRU10115}.
-!- PATHWAY: Metabolic intermediate metabolism; (S)-3-hydroxy-3-
methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-
methylglutaryl-CoA: step 1/1.
-!- SUBUNIT: Homodimer; disulfide-linked. Can also form homotetramers.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:7527399}. Peroxisome
{ECO:0000269|PubMed:7527399}. Note=Unprocessed form is
peroxisomal.
-!- SIMILARITY: Belongs to the HMG-CoA lyase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S65036; AAB27965.1; -; mRNA.
EMBL; U49878; AAB03107.1; -; Genomic_DNA.
EMBL; U49870; AAB03107.1; JOINED; Genomic_DNA.
EMBL; U49871; AAB03107.1; JOINED; Genomic_DNA.
EMBL; U49872; AAB03107.1; JOINED; Genomic_DNA.
EMBL; U49873; AAB03107.1; JOINED; Genomic_DNA.
EMBL; U49874; AAB03107.1; JOINED; Genomic_DNA.
EMBL; U49875; AAB03107.1; JOINED; Genomic_DNA.
EMBL; U49876; AAB03107.1; JOINED; Genomic_DNA.
EMBL; U49877; AAB03107.1; JOINED; Genomic_DNA.
EMBL; AK132035; BAE20956.1; -; mRNA.
EMBL; AK145251; BAE26328.1; -; mRNA.
EMBL; AK154033; BAE32329.1; -; mRNA.
EMBL; AL672076; CAM15901.1; -; Genomic_DNA.
EMBL; CH466552; EDL29963.1; -; Genomic_DNA.
EMBL; BC025440; AAH25440.1; -; mRNA.
CCDS; CCDS18795.1; -.
RefSeq; NP_032280.2; NM_008254.2.
UniGene; Mm.482102; -.
ProteinModelPortal; P38060; -.
SMR; P38060; -.
BioGrid; 200337; 2.
IntAct; P38060; 2.
MINT; P38060; -.
STRING; 10090.ENSMUSP00000030432; -.
iPTMnet; P38060; -.
PhosphoSitePlus; P38060; -.
SwissPalm; P38060; -.
EPD; P38060; -.
MaxQB; P38060; -.
PaxDb; P38060; -.
PeptideAtlas; P38060; -.
PRIDE; P38060; -.
Ensembl; ENSMUST00000030432; ENSMUSP00000030432; ENSMUSG00000028672.
GeneID; 15356; -.
KEGG; mmu:15356; -.
UCSC; uc012dnc.1; mouse.
CTD; 3155; -.
MGI; MGI:96158; Hmgcl.
eggNOG; KOG2368; Eukaryota.
eggNOG; COG0119; LUCA.
GeneTree; ENSGT00390000017690; -.
HOGENOM; HOG000219757; -.
HOVERGEN; HBG064656; -.
InParanoid; P38060; -.
KO; K01640; -.
OMA; FGGCPMA; -.
OrthoDB; EOG091G0DA9; -.
TreeFam; TF105363; -.
Reactome; R-MMU-77111; Synthesis of Ketone Bodies.
Reactome; R-MMU-9033241; Peroxisomal protein import.
UniPathway; UPA00896; UER00863.
PRO; PR:P38060; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028672; -.
CleanEx; MM_HMGCL; -.
Genevisible; P38060; MM.
GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005777; C:peroxisome; ISO:MGI.
GO; GO:0031406; F:carboxylic acid binding; ISO:MGI.
GO; GO:0000062; F:fatty-acyl-CoA binding; ISO:MGI.
GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; ISS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
GO; GO:0030145; F:manganese ion binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0006637; P:acyl-CoA metabolic process; ISO:MGI.
GO; GO:0046951; P:ketone body biosynthetic process; ISS:UniProtKB.
GO; GO:0006629; P:lipid metabolic process; ISO:MGI.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
GO; GO:0051262; P:protein tetramerization; ISO:MGI.
GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0042594; P:response to starvation; IEA:Ensembl.
Gene3D; 3.20.20.70; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR000138; HMG_CoA_lyase_AS.
InterPro; IPR000891; PYR_CT.
Pfam; PF00682; HMGL-like; 1.
PROSITE; PS01062; HMG_COA_LYASE; 1.
PROSITE; PS50991; PYR_CT; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Disulfide bond; Lyase; Metal-binding;
Mitochondrion; Peroxisome; Reference proteome; Transit peptide.
TRANSIT 1 27 Mitochondrion. {ECO:0000250}.
CHAIN 28 325 Hydroxymethylglutaryl-CoA lyase,
mitochondrial.
/FTId=PRO_0000013480.
DOMAIN 33 300 Pyruvate carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01151}.
MOTIF 323 325 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 266 266 {ECO:0000255|PROSITE-ProRule:PRU10115}.
METAL 42 42 Divalent metal cation. {ECO:0000250}.
METAL 233 233 Divalent metal cation. {ECO:0000250}.
METAL 235 235 Divalent metal cation. {ECO:0000250}.
METAL 275 275 Divalent metal cation. {ECO:0000250}.
BINDING 41 41 Substrate. {ECO:0000250}.
MOD_RES 48 48 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753,
ECO:0000244|PubMed:23806337}.
MOD_RES 48 48 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 111 111 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 137 137 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 137 137 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 179 179 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 179 179 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 324 324 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
DISULFID 323 323 Interchain. {ECO:0000250}.
CONFLICT 62 63 ML -> IV (in Ref. 2; AAB03107).
{ECO:0000305}.
CONFLICT 80 80 K -> N (in Ref. 1; AAB27965).
{ECO:0000305}.
CONFLICT 231 231 A -> G (in Ref. 1; AAB27965).
{ECO:0000305}.
CONFLICT 238 238 Y -> I (in Ref. 1; AAB27965).
{ECO:0000305}.
SEQUENCE 325 AA; 34239 MW; E6A85659EBA1D87F CRC64;
MASVRKAFPR RLVGLTSLRA VSTSSMGTLP KQVKIVEVGP RDGLQNEKSI VPTPVKIRLI
DMLSEAGLPV IEATSFVSPK WVPQMADHSD VLKGIQKFPG INYPVLTPNM KGFEEAVAAG
AKEVSVFGAV SELFTRKNAN CSIEESFQRF AGVMQAAQAA SISVRGYVSC ALGCPYEGKV
SPAKVAEVAK KLYSMGCYEI SLGDTIGVGT PGLMKDMLTA VMHEVPVTAL AVHCHDTYGQ
ALANTLVALQ MGVSVVDSSV AGLGGCPYAK GASGNLATED LVYMLNGLGI HTGVNLQKLL
EAGDFICQAL NRKTSSKVAQ ATCKL


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