Reviewed, UniProtKB/Swiss-Prot Q91VA0 (ACSM1_MOUSE)

Names and origin

Protein names

Recommended name:
    Acyl-coenzyme A synthetase ACSM1, mitochondrial
    EC=6.2.1.2
Alternative name(s):
    Acyl-CoA synthetase medium-chain family member 1
    Middle-chain acyl-CoA synthetase 1
    Butyryl coenzyme A synthetase 1
    Butyrate--CoA ligase 1
    Lipoate-activating enzyme

Gene names

Name:	Acsm1
Synonyms:	Bucs1, Lae, Macs1

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	573 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	Functions as GTP-dependent lipoate-activating enzyme that generates the substrate for lipoyltransferase By similarity. 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).
Catalytic activity	ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA. GTP + lipoate = diphosphate + lipoyl-GMP.
Cofactor	Magnesium By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion matrix. Ref.1
Tissue specificity	Highly expressed in liver and kidney. Ref.1
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	ATP-binding GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Ref.1 Inferred from direct assay. Source: MGI
Cellular component	mitochondrial matrix Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW acyl-CoA ligase activity Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB butyrate-CoA ligase activity Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB fatty-acid ligase activity Ref.1 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: Q91VA0-1)

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: Q91VA0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     369-395: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 35	35	Mitochondrion Potential
	Chain	36 – 573	538	Acyl-coenzyme A synthetase ACSM1, mitochondrial		PRO_0000306092
Regions
	Nucleotide binding	222 – 230	9	ATP By similarity
Sites
	Binding site	448	1	ATP By similarity
	Binding site	463	1	ATP By similarity
	Binding site	559	1	ATP By similarity
Natural variations
	Alternative sequence	369 – 395	27	Missing in isoform 2.		VSP_028392
Experimental info
	Sequence conflict	465	1	D → V in BAE28977. Ref.2
	Sequence conflict	525	1	L → F in BAE28977. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 557F25D467CA305B	FASTA	573	64,760
	10 20 30 40 50 60 MQWLKSFQIC KVLQGFSLSP TQLHRRLFSR VGAPRWNDHD SPEEFNFASD VLDYWAQMEE 70 80 90 100 110 120 EGKRGPSPAF WWVNGQGDEI KWSFRKLRDL TCRTANVFEQ ICGLQQGDHL ALILPRVPEW 130 140 150 160 170 180 WLVTVGCMRT GIIFMPGTTQ LKAKDILYRI QISRAKAIVT TASLVPEVES VASECPDLKT 190 200 210 220 230 240 KLVVSDHSHE GWLDFCSLIK SASPDHTCIK SKMKDPMAIF FTSGTTGYPK MAKHNQGLAF 250 260 270 280 290 300 RSYIPSCRKL LKLKTSDILW CMSDPGWILA TVGCLIEPWT SGCTVFIHHL PQFDPKVIVE 310 320 330 340 350 360 VLFKYPITQC LAAPGVYRMV LQQKTSNLRF PTLEHCTTGG ESLLPEEYEQ WKQRTGLSIH 370 380 390 400 410 420 EVYGQSETGI SSATLREMKI KRGSIGKAIL PFDLQIIDEK GNILPPNTEG YIGIRIKPTR 430 440 450 460 470 480 PLGLFMEYEN SPESTSEVEC GDFYNSGDRA TIDEEGYIWF LGRGDDVINA SGYRIGPVEV 490 500 510 520 530 540 ENALAEHPAV AESAVVSSPD KDRGEVVKAF IVLNPEFLSH DQEQLIKELQ HHVKSVTAPY 550 560 570 KYPRKVEFVS ELPKTVTGKI KRKELRNKEF GQL
	Isoform 2. Checksum: DAAF1F2C5EADB8F4	FASTA	546	61,848
	10 20 30 40 50 60 MQWLKSFQIC KVLQGFSLSP TQLHRRLFSR VGAPRWNDHD SPEEFNFASD VLDYWAQMEE 70 80 90 100 110 120 EGKRGPSPAF WWVNGQGDEI KWSFRKLRDL TCRTANVFEQ ICGLQQGDHL ALILPRVPEW 130 140 150 160 170 180 WLVTVGCMRT GIIFMPGTTQ LKAKDILYRI QISRAKAIVT TASLVPEVES VASECPDLKT 190 200 210 220 230 240 KLVVSDHSHE GWLDFCSLIK SASPDHTCIK SKMKDPMAIF FTSGTTGYPK MAKHNQGLAF 250 260 270 280 290 300 RSYIPSCRKL LKLKTSDILW CMSDPGWILA TVGCLIEPWT SGCTVFIHHL PQFDPKVIVE 310 320 330 340 350 360 VLFKYPITQC LAAPGVYRMV LQQKTSNLRF PTLEHCTTGG ESLLPEEYEQ WKQRTGLSIH 370 380 390 400 410 420 EVYGQSETII DEKGNILPPN TEGYIGIRIK PTRPLGLFME YENSPESTSE VECGDFYNSG 430 440 450 460 470 480 DRATIDEEGY IWFLGRGDDV INASGYRIGP VEVENALAEH PAVAESAVVS SPDKDRGEVV 490 500 510 520 530 540 KAFIVLNPEF LSHDQEQLIK ELQHHVKSVT APYKYPRKVE FVSELPKTVT GKIKRKELRN KEFGQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Kidney.
[2]	"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: Liver.
[3]	"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 and Liver.
[4]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 249-254, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[5]	"Purification, characterization, and mass spectrometric sequencing of a medium chain acyl-CoA synthetase from mouse liver mitochondria and comparisons with the homologues of rat and bovine." Kasuya F., Tatsuki T., Ohta M., Kawai Y., Igarashi K. Protein Expr. Purif. 47:405-414(2006) [PubMed: 16378734] [Abstract] Cited for: MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB059428 mRNA. Translation: BAB64534.1. AK149550 mRNA. Translation: BAE28952.1. AK149586 mRNA. Translation: BAE28977.1. BC016414 mRNA. Translation: AAH16414.1. BC022149 mRNA. Translation: AAH22149.1.
IPI	IPI00126625. IPI00654116.
RefSeq	NP_473435.1.
UniGene	Mm.427560
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Protein-protein interaction databases
STRING	Q91VA0.
Proteomic databases
PRIDE	Q91VA0.
Genome annotation databases
Ensembl	ENSMUST00000047929; ENSMUSP00000036140; ENSMUSG00000033533; Mus musculus. [Genome view] ENSMUST00000098083; ENSMUSP00000095689; ENSMUSG00000033533; Mus musculus. [Genome view]
GeneID	117147.
KEGG	mmu:117147.
UCSC	uc009jlm.1. mouse.
Organism-specific databases
CTD	117147.
MGI	MGI:2152200. Acsm1.
Phylogenomic databases
HOGENOM	Q91VA0.
HOVERGEN	Q91VA0.
OMA	FTSIRFP.
Enzyme and pathway databases
BRENDA	6.2.1.2. 244.
Gene expression databases
ArrayExpress	Q91VA0.
Bgee	Q91VA0.
CleanEx	MM_ACSM1.
Genevestigator	Q91VA0.
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	369520.
SOURCE	Search...

Entry information

Entry name

ACSM1_MOUSE

Accession

Primary (citable) accession number: Q91VA0
Secondary accession number(s): Q3UED4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)