Reviewed, UniProtKB/Swiss-Prot Q3UNX5 (ACSM3_MOUSE)

Names and origin

Protein names

Recommended name:
    Acyl-coenzyme A synthetase ACSM3, mitochondrial
    EC=6.2.1.2
Alternative name(s):
    Acyl-CoA synthetase medium-chain family member 3
    Middle-chain acyl-CoA synthetase 3
    Butyryl coenzyme A synthetase 3
    Butyrate--CoA ligase 3
    Protein SA homolog

Gene names

Name:	Acsm3
Synonyms:	Sa, Sah

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	580 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C4 to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro). Ref.6
Catalytic activity	ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA.
Cofactor	Magnesium or manganese By similarity.
Subcellular location	Mitochondrion matrix. Ref.6 Ref.3
Tissue specificity	Detected in kidney (at protein level). Detected in kidney proximal tubules and in liver. Detected at low levels in testis, stomach, heart and lung. Ref.6 Ref.3 Ref.1 Ref.2
Induction	Up-regulated in kidney by androgens. Down-regulated in kidney by estrogens. Levels in kidney are very low in female C57BL/6 mice and in castrated male C57BL/6, 129/SvJ and BALB/c mice. Constitutively expressed in liver. Ref.3 Ref.1
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Caution	It is uncertain whether Met-1 or Met-3 is the initiator.
Sequence caution	The sequence BAA37141.1 differs from that shown. Reason: Frameshift at positions 1, 63 and 72.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Ref.6 Inferred from direct assay. Source: MGI
Cellular component	mitochondrial matrix Ref.6 Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW butyrate-CoA ligase activity Inferred from electronic annotation. Source: EC fatty-acid ligase activity Ref.6 Inferred from direct assay. Source: MGI magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q3UNX5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q3UNX5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     578-580: VTT → EQGLLHEQMTVDRLLGKSARHERHVPSVCMNCSGVAAVLRYAEAA

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 21	21	Mitochondrion Potential
	Chain	22 – 580	559	Acyl-coenzyme A synthetase ACSM3, mitochondrial		PRO_0000306098
Regions
	Nucleotide binding	229 – 237	9	ATP By similarity
	Nucleotide binding	368 – 373	6	ATP By similarity
Sites
	Binding site	455	1	ATP By similarity
	Binding site	470	1	ATP By similarity
	Binding site	566	1	ATP By similarity
Amino acid modifications
	Modified residue	37	1	Phosphotyrosine By similarity
Natural variations
	Alternative sequence	578 – 580	3	VTT → EQGLLHEQMTVDRLLGKSAR HERHVPSVCMNCSGVAAVLR YAEAA in isoform 2.		VSP_028397
Experimental info
	Sequence conflict	137	1	T → P in AAC79656. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 2, 2007. Version 2. Checksum: CAF3D06A0B4A2778	FASTA	580	65,623
	10 20 30 40 50 60 MVMLLRARCF QRLAIPDPMR VLYKDYRTAT PQNFSNYESM KQDFKIEIPE YFNFAKDVLD 70 80 90 100 110 120 QWTNMEKAGK RLSNPAFWWI DGNGEELRWS FEELGLLSRK FANILTEACS LQRGDRVMVI 130 140 150 160 170 180 LPKIPEWWLA NVACLRTGTV LIPGTTQLTQ KDILYRLQSS KAKCIITDDT LAPAVDAVAA 190 200 210 220 230 240 KCENLHSKLI VSQHSREGWG NLKEMMKYAS DSHTCVDTKH DEMMAIYFTS GTTGPPKMIG 250 260 270 280 290 300 HTHSSFGLGL SVNGRFWLDL IASDVMWNTS DTGWAKSAWS SVFSPWTQGA CVFAHYLPRF 310 320 330 340 350 360 ESTSILQTLS KFPITVFCSA PTAYRMLVQN DMSSYKFNSL KHCVSAGEPI NPEVMEQWRK 370 380 390 400 410 420 KTGLDIYEGY GQTETVLICG NFKGMKIKPG SMGKPSPAFD VKILDENGAT LPPGQEGDIA 430 440 450 460 470 480 LQVLPERPFG LFTHYVDNPS KTASTLRGSF YITGDRGYMD EDGYFWFVAR SDDIILSSGY 490 500 510 520 530 540 RIGPFEVESA LIEHPSIAES AVVSSPDPIR GEVVKAFIVL NPDYKSHDQE QLKKEIQEHV 550 560 570 580 KKTTAPYKYP RKVEFIEELP KTVSGKVKRN ELRKKEWVTT
	Isoform 2. Checksum: 4F98E4406704D0F2	FASTA	622	70,238
	10 20 30 40 50 60 MVMLLRARCF QRLAIPDPMR VLYKDYRTAT PQNFSNYESM KQDFKIEIPE YFNFAKDVLD 70 80 90 100 110 120 QWTNMEKAGK RLSNPAFWWI DGNGEELRWS FEELGLLSRK FANILTEACS LQRGDRVMVI 130 140 150 160 170 180 LPKIPEWWLA NVACLRTGTV LIPGTTQLTQ KDILYRLQSS KAKCIITDDT LAPAVDAVAA 190 200 210 220 230 240 KCENLHSKLI VSQHSREGWG NLKEMMKYAS DSHTCVDTKH DEMMAIYFTS GTTGPPKMIG 250 260 270 280 290 300 HTHSSFGLGL SVNGRFWLDL IASDVMWNTS DTGWAKSAWS SVFSPWTQGA CVFAHYLPRF 310 320 330 340 350 360 ESTSILQTLS KFPITVFCSA PTAYRMLVQN DMSSYKFNSL KHCVSAGEPI NPEVMEQWRK 370 380 390 400 410 420 KTGLDIYEGY GQTETVLICG NFKGMKIKPG SMGKPSPAFD VKILDENGAT LPPGQEGDIA 430 440 450 460 470 480 LQVLPERPFG LFTHYVDNPS KTASTLRGSF YITGDRGYMD EDGYFWFVAR SDDIILSSGY 490 500 510 520 530 540 RIGPFEVESA LIEHPSIAES AVVSSPDPIR GEVVKAFIVL NPDYKSHDQE QLKKEIQEHV 550 560 570 580 590 600 KKTTAPYKYP RKVEFIEELP KTVSGKVKRN ELRKKEWEQG LLHEQMTVDR LLGKSARHER 610 620 HVPSVCMNCS GVAAVLRYAE AA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of androgen-regulated genes in mouse kidney by representational difference analysis and random arbitrarily primed polymerase chain reaction." Melia M.J., Bofill N., Hubank M., Meseguer A. Endocrinology 139:688-695(1998) [PubMed: 9449642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION. Strain: C57BL/6.
[2]	"Isolation of genes identified in mouse renal proximal tubule by comparing different gene expression profiles." Takenaka M., Imai E., Kaneko T., Ito T., Moriyama T., Yamauchi A., Hori M., Kawamoto S., Okubo K. Kidney Int. 53:562-572(1998) [PubMed: 9507200] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Strain: C57BL/6. Tissue: Kidney.
[3]	"Sex steroid regulation and identification of different transcription units of the SA gene in mouse kidney." Areste C., Melia M.J., Isern J., Tovar J.L., Meseguer A. J. Endocrinol. 183:101-114(2004) [PubMed: 15525578] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY. Strain: 129/SvJ. Tissue: Kidney.
[4]	"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] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Aorta, Kidney and Vein.
[5]	"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] (ISOFORM 1). Strain: FVB/N. Tissue: Kidney.
[6]	"Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product." Fujino T., Takei Y.A., Sone H., Ioka R.X., Kamataki A., Magoori K., Takahashi S., Sakai J., Yamamoto T.T. J. Biol. Chem. 276:35961-35966(2001) [PubMed: 11470804] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY064696 mRNA. Translation: AAL40880.1. Different initiation. AB022340 mRNA. Translation: BAA37141.1. Frameshift. AF068246 mRNA. Translation: AAC79656.1. Different initiation. AK041060 mRNA. Translation: BAC30805.1. AK143946 mRNA. Translation: BAE25622.1. AK165516 mRNA. Translation: BAE38232.1. Different initiation. BC015248 mRNA. Translation: AAH15248.1. Different initiation.
IPI	IPI00387345. IPI00762478.
RefSeq	NP_058566.3. NP_997606.2. NP_997607.2.
UniGene	Mm.334199
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q3UNX5.
Genome annotation databases
Ensembl	ENSMUSG00000030935. Mus musculus. [Contig view]
GeneID	20216.
KEGG	mmu:20216.
Organism-specific databases
MGI	MGI:99538. Acsm3.
Phylogenomic databases
HOGENOM	Q3UNX5.
HOVERGEN	Q3UNX5.
OMA	Q3UNX5. CENLHSK.
Enzyme and pathway databases
BRENDA	6.2.1.2. 244.
Gene expression databases
Bgee	Q3UNX5.
CleanEx	MM_ACSM3.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	297817.
SOURCE	Search...

Entry information

Entry name

ACSM3_MOUSE

Accession

Primary (citable) accession number: Q3UNX5
Secondary accession number(s): Q8BRY2 , Q91WI1, Q9Z2F3, Q9Z2X0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	October 2, 2007
Last modified:	June 16, 2009
This is version 31 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)