Reviewed, UniProtKB/Swiss-Prot Q8JZK9 (HMCS1_MOUSE)

Names and origin

Protein names

Recommended name:
    Hydroxymethylglutaryl-CoA synthase, cytoplasmic
      Short name=HMG-CoA synthase
    EC=2.3.3.10
Alternative name(s):
    3-hydroxy-3-methylglutaryl coenzyme A synthase

Gene names

Name:

Hmgcs1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase By similarity.
Catalytic activity	Acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA.
Pathway	Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the HMG-CoA synthase family.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Cytoplasm
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW isoprenoid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydroxymethylglutaryl-CoA synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 520	520	Hydroxymethylglutaryl-CoA synthase, cytoplasmic		PRO_0000213748
Sites
	Active site	129	1	Potential
Amino acid modifications
	Modified residue	4	1	Phosphoserine By similarity
	Modified residue	46	1	N6-acetyllysine By similarity
	Modified residue	246	1	N6-acetyllysine By similarity
	Modified residue	273	1	N6-acetyllysine By similarity
	Modified residue	321	1	N6-acetyllysine By similarity
	Modified residue	495	1	Phosphoserine By similarity
	Modified residue	516	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8JZK9-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: E28F8772CF64D85C	FASTA	520	57,569
	10 20 30 40 50 60 MPGSLPLNAE ACWPKDVGIV ALEIYFPSQY VDQAELEKYD GVDAGKYTIG LGQARMGFCT 70 80 90 100 110 120 DREDINSLCL TVVQKLMERH SLSYDCIGRL EVGTETIIDK SKSVKSNLMQ LFEESGNTDI 130 140 150 160 170 180 EGIDTTNACY GGTAAVFNAV NWVESSSWDG RYALVVAGDI AIYATGNARP TGGVGAVALL 190 200 210 220 230 240 IGPNAPLIFD RGLRGTHMQH AYDFYKPDML SEYPVVDGKL SIQCYLSALD RCYSVYRKKI 250 260 270 280 290 300 RAQWQKEGKD KDFTLNDFGF MIFHSPYCKL VQKSLARMFL NDFLNDQNRD KNSIYSGLEA 310 320 330 340 350 360 FGDVKLEDTY FDRDVEKAFM KASSELFNQK TKASLLVSNQ NGNMYTSSVY GSLASVLAQY 370 380 390 400 410 420 SPQQLAGKRV GVFSYGSGLA ATLYSLKVTQ DATPGSALDK ITASLCDLKS RLDSRTCVAP 430 440 450 460 470 480 DVFAENMKLR EDTHHLANYI PQCSIDSLFE GTWYLVRVDE KHRRTYARRP FTNDHSLDEG 490 500 510 520 MGLVHSNTAT EHIPSPAKKV PRLPATSAES ESAVISNGEH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Muellerian duct and Testis.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N and FVB/N-3. Tissue: Eye and Mammary tumor.
[3]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 47-75; 90-100; 220-231; 278-289; 292-313; 322-330; 370-409; 416-428 AND 469-498, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC023851 mRNA. Translation: AAH23851.1. BC029693 mRNA. Translation: AAH29693.1. BC034317 mRNA. Translation: AAH34317.1. AK031297 mRNA. Translation: BAC27338.1. AK044835 mRNA. Translation: BAC32112.1. AK045094 mRNA. Translation: BAC32218.1. AK135551 mRNA. Translation: BAE22579.1.
IPI	IPI00331707.
RefSeq	NP_666054.2. XP_001475239.1. XP_001475257.1. XP_001475280.1.
UniGene	Mm.61526
3D structure databases
SMR	Q8JZK9. Positions 16-470.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8JZK9.
PTM databases
PhosphoSite	Q8JZK9.
2-D gel databases
REPRODUCTION-2DPAGE	Q8JZK9.
Proteomic databases
PRIDE	Q8JZK9.
Genome annotation databases
Ensembl	ENSMUST00000100285; ENSMUSP00000097858; ENSMUSG00000079828; Mus musculus. [Genome view] ENSMUST00000112117; ENSMUSP00000107745; ENSMUSG00000079301; Mus musculus. [Genome view]
GeneID	100040592. 208715.
KEGG	mmu:100040592. mmu:208715.
UCSC	uc007rzv.1. mouse.
Organism-specific databases
CTD	208715.
MGI	MGI:107592. Hmgcs1.
Phylogenomic databases
HOGENOM	HBG578402.
HOVERGEN	Q8JZK9.
InParanoid	Q8JZK9.
OMA	MKASAEL.
OrthoDB	EOG9S4S1K.
PhylomeDB	Q8JZK9.
Enzyme and pathway databases
BRENDA	2.3.3.10. 244.
Gene expression databases
ArrayExpress	Q8JZK9.
CleanEx	MM_HMGCS1.
Genevestigator	Q8JZK9.
GermOnline	ENSMUSG00000075461. Mus musculus.
Family and domain databases
InterPro	IPR000590. HMG_CoA_synt_AS. IPR013746. HMG_CoA_synt_C. IPR013528. HMG_CoA_synth_N. IPR010122. HMG_CoA_synthase_euk. IPR016039. Thiolase-like. [Graphical view]
Pfam	PF08540. HMG_CoA_synt_C. 1 hit. PF01154. HMG_CoA_synt_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITE	PS01226. HMG_COA_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	449244.
SOURCE	Search...

Entry information

Entry name

HMCS1_MOUSE

Accession

Primary (citable) accession number: Q8JZK9
Secondary accession number(s): Q3UXI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	October 1, 2002
Last modified:	February 9, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)