Q8K0L3 (ACSM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-coenzyme A synthetase ACSM2, mitochondrial
EC=6.2.1.2

Alternative name(s):
Acyl-CoA synthetase medium-chain family member 2
Butyrate--CoA ligase 2
Butyryl-coenzyme A synthetase 2
Middle-chain acyl-CoA synthetase 2

Gene names

Name:

Acsm2

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 › Mus

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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) By similarity.
Catalytic activity	ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA.
Cofactor	Magnesium or manganese By similarity.
Enzyme regulation	Activated by monovalent cations, such as potassium, rubidium or ammonium By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion matrix By similarity.
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 Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW butyrate-CoA ligase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8K0L3-1)

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: Q8K0L3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTTGSLDLPFVGSHRWIKWTTASLTM

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8K0L3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     471-471: G → GAYFCR

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 46	46	Mitochondrion Potential
	Chain	47 – 575	529	Acyl-coenzyme A synthetase ACSM2, mitochondrial		PRO_0000306095
Regions
	Nucleotide binding	221 – 229	9	ATP By similarity
	Nucleotide binding	360 – 365	6	ATP By similarity
	Region	470 – 472	3	Coenzyme A binding By similarity
	Region	541 – 543	3	Coenzyme A binding By similarity
Sites
	Binding site	139	1	Coenzyme A By similarity
	Binding site	365	1	Substrate By similarity
	Binding site	447	1	ATP By similarity
	Binding site	462	1	ATP By similarity
	Binding site	473	1	Substrate By similarity
	Binding site	502	1	Coenzyme A By similarity
	Binding site	533	1	Coenzyme A By similarity
	Binding site	558	1	ATP By similarity
Natural variations
	Alternative sequence	1	1	M → MTTGSLDLPFVGSHRWIKWT TASLTM in isoform 2.		VSP_028393
	Alternative sequence	471	1	G → GAYFCR in isoform 3.		VSP_028394
Experimental info
	Sequence conflict	515	1	E → G in BAB71542. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: A7E5956D54B119D8	FASTA	575	64,269
	10 20 30 40 50 60 MHHLWKIPRL FTLWGNEISC RTFHMNIKKL IPIQWGHQEA PAKFNFASDV IDHWASVEKA 70 80 90 100 110 120 GKRSSGPALW WMNGSGKEIK WSFRELSEAS KQTANVLSGA CGLHRGDRVA VVLPRIPEWW 130 140 150 160 170 180 LMILGCMRTG LVFMPGTIQM RSSDILYRLQ ASKARAIVAG DEVAQEVDAV APDCSFLKIK 190 200 210 220 230 240 LLVSENSREG WLNFKALLKE ASTIHQCVET ESRESAAIYF TSGTSGPPKM AEHSHCSLGI 250 260 270 280 290 300 KAKMDAASWT GLSTSDIIWT ISDTAWIMNI LGAFLEPWVL GACIFVHLLP KFDSQTVLKV 310 320 330 340 350 360 LSSYPINTLV GAPIIYRMLL QQDLSSYKFP HLHSCFSGGE TLLPETLENW KAKTGLEIRE 370 380 390 400 410 420 IYGQTETGLI CRVSRTMKVK PGYLGTAFAH YDVQVIDEQG NVLPPGKEGD IAIRVKPIWP 430 440 450 460 470 480 IGMFSGYVDN PKKTQDNIRG DFWLMGDRGI KDPEGYFHFI GRSDDIINSS GYRIGPSEVE 490 500 510 520 530 540 NALMEHPAVS ETAVISSPDP SRGEVVKAFV VLAPEFLSHD RDQLTKVLQE HVKSVTAPYK 550 560 570 YPRKVEFVLD LPKTVTGKIE RAKLRAKEWK TSGRA
	Isoform 2 [UniParc]. Checksum: CD0F661EC08E1C4F	FASTA	600	67,057
	10 20 30 40 50 60 MTTGSLDLPF VGSHRWIKWT TASLTMHHLW KIPRLFTLWG NEISCRTFHM NIKKLIPIQW 70 80 90 100 110 120 GHQEAPAKFN FASDVIDHWA SVEKAGKRSS GPALWWMNGS GKEIKWSFRE LSEASKQTAN 130 140 150 160 170 180 VLSGACGLHR GDRVAVVLPR IPEWWLMILG CMRTGLVFMP GTIQMRSSDI LYRLQASKAR 190 200 210 220 230 240 AIVAGDEVAQ EVDAVAPDCS FLKIKLLVSE NSREGWLNFK ALLKEASTIH QCVETESRES 250 260 270 280 290 300 AAIYFTSGTS GPPKMAEHSH CSLGIKAKMD AASWTGLSTS DIIWTISDTA WIMNILGAFL 310 320 330 340 350 360 EPWVLGACIF VHLLPKFDSQ TVLKVLSSYP INTLVGAPII YRMLLQQDLS SYKFPHLHSC 370 380 390 400 410 420 FSGGETLLPE TLENWKAKTG LEIREIYGQT ETGLICRVSR TMKVKPGYLG TAFAHYDVQV 430 440 450 460 470 480 IDEQGNVLPP GKEGDIAIRV KPIWPIGMFS GYVDNPKKTQ DNIRGDFWLM GDRGIKDPEG 490 500 510 520 530 540 YFHFIGRSDD IINSSGYRIG PSEVENALME HPAVSETAVI SSPDPSRGEV VKAFVVLAPE 550 560 570 580 590 600 FLSHDRDQLT KVLQEHVKSV TAPYKYPRKV EFVLDLPKTV TGKIERAKLR AKEWKTSGRA
	Isoform 3 [UniParc]. Checksum: 2D228B445D3D2DF3	FASTA	580	64,910
	10 20 30 40 50 60 MHHLWKIPRL FTLWGNEISC RTFHMNIKKL IPIQWGHQEA PAKFNFASDV IDHWASVEKA 70 80 90 100 110 120 GKRSSGPALW WMNGSGKEIK WSFRELSEAS KQTANVLSGA CGLHRGDRVA VVLPRIPEWW 130 140 150 160 170 180 LMILGCMRTG LVFMPGTIQM RSSDILYRLQ ASKARAIVAG DEVAQEVDAV APDCSFLKIK 190 200 210 220 230 240 LLVSENSREG WLNFKALLKE ASTIHQCVET ESRESAAIYF TSGTSGPPKM AEHSHCSLGI 250 260 270 280 290 300 KAKMDAASWT GLSTSDIIWT ISDTAWIMNI LGAFLEPWVL GACIFVHLLP KFDSQTVLKV 310 320 330 340 350 360 LSSYPINTLV GAPIIYRMLL QQDLSSYKFP HLHSCFSGGE TLLPETLENW KAKTGLEIRE 370 380 390 400 410 420 IYGQTETGLI CRVSRTMKVK PGYLGTAFAH YDVQVIDEQG NVLPPGKEGD IAIRVKPIWP 430 440 450 460 470 480 IGMFSGYVDN PKKTQDNIRG DFWLMGDRGI KDPEGYFHFI GRSDDIINSS GAYFCRYRIG 490 500 510 520 530 540 PSEVENALME HPAVSETAVI SSPDPSRGEV VKAFVVLAPE FLSHDRDQLT KVLQEHVKSV 550 560 570 580 TAPYKYPRKV EFVLDLPKTV TGKIERAKLR AKEWKTSGRA

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] (ISOFORMS 1; 2 AND 3). Strain: C57BL/6J. Tissue: Embryonic head, Kidney and Spleen.
[2]	"NEDO cDNA sequencing project." Suzuki O., Sasaki N., Aotsuka S., Shoji T., Ichihara T., Shiohata N., Matsumoto K., Hirano M., Sano S., Nomura R., Yoshikawa Y., Matsumura Y., Moriya S., Chiba E., Momiyama H., Onogawa S., Kaeriyama S., Satoh N. , Matsunawa H., Takahashi E., Kataoka R., Kuga N., Kuroda A., Satoh I., Kamata K., Takami S., Terashima Y., Watanabe M., Sugiyama T., Irie R., Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S., Yamamoto J., Isono Y., Kawai-Hio Y., Saito K., Nishikawa T., Kimura K., Yamashita H., Matsuo K., Nakamura Y., Sekine M., Kikuchi H., Kanda K., Wagatsuma M., Murakawa K., Kanehori K., Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B., Suzuki Y., Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T. Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK140827 mRNA. Translation: BAE24490.1. AK143757 mRNA. Translation: BAE25526.1. AK165353 mRNA. Translation: BAE38146.1. AK165401 mRNA. Translation: BAE38163.1. AK057650 mRNA. Translation: BAB71542.1. BC024424 mRNA. Translation: AAH24424.1. BC031140 mRNA. Translation: AAH31140.1.
IPI	IPI00169586. IPI00761916. IPI00867792.
RefSeq	NP_001171448.1. NM_001177977.1. NP_001171449.1. NM_001177978.1. NP_666309.1. NM_146197.4.
UniGene	Mm.268448.
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortal	Q8K0L3.
SMR	Q8K0L3. Positions 34-570.
ModBase	Search...
PTM databases
PhosphoSite	Q8K0L3.
Proteomic databases
PRIDE	Q8K0L3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000084647; ENSMUSP00000081697; ENSMUSG00000030945. ENSMUST00000098084; ENSMUSP00000095690; ENSMUSG00000030945. ENSMUST00000167935; ENSMUSP00000126670; ENSMUSG00000030945.
GeneID	233799.
KEGG	mmu:233799.
NMPDR	fig|10090.3.peg.17514.
UCSC	uc009jlh.2. mouse. uc009jli.2. mouse.
Organism-specific databases
CTD	233799.
MGI	MGI:2385289. Acsm2.
Phylogenomic databases
HOGENOM	HBG547964.
HOVERGEN	HBG053031.
InParanoid	Q8K0L3.
OMA	ISDTAWI.
OrthoDB	EOG40ZQXB.
PhylomeDB	Q8K0L3.
Gene expression databases
ArrayExpress	Q8K0L3.
Bgee	Q8K0L3.
CleanEx	MM_ACSM2.
Genevestigator	Q8K0L3.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
KO	K01896.
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	381829.
SOURCE	Search...

Entry information

Entry name

ACSM2_MOUSE

Accession

Primary (citable) accession number: Q8K0L3
Secondary accession number(s): Q3TNC6 , Q3US47, Q8R1L3, Q96LX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	October 1, 2002
Last modified:	November 16, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program