ACSM2_MOUSE
ID ACSM2_MOUSE Reviewed; 575 AA.
AC Q8K0L3; Q3TNC6; Q3US47; Q8R1L3; Q96LX4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Acyl-coenzyme A synthetase ACSM2, mitochondrial;
DE EC=6.2.1.2 {ECO:0000250|UniProtKB:Q68CK6};
DE AltName: Full=Acyl-CoA synthetase medium-chain family member 2;
DE AltName: Full=Benzoate--CoA ligase;
DE EC=6.2.1.25 {ECO:0000250|UniProtKB:Q68CK6};
DE AltName: Full=Butyrate--CoA ligase 2;
DE AltName: Full=Butyryl-coenzyme A synthetase 2;
DE AltName: Full=Middle-chain acyl-CoA synthetase 2;
DE Flags: Precursor;
GN Name=Acsm2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, Kidney, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Suzuki O., Sasaki N., Aotsuka S., Shoji T., Ichihara T., Shiohata N.,
RA Matsumoto K., Hirano M., Sano S., Nomura R., Yoshikawa Y., Matsumura Y.,
RA Moriya S., Chiba E., Momiyama H., Onogawa S., Kaeriyama S., Satoh N.,
RA Matsunawa H., Takahashi E., Kataoka R., Kuga N., Kuroda A., Satoh I.,
RA Kamata K., Takami S., Terashima Y., Watanabe M., Sugiyama T., Irie R.,
RA Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S., Yamamoto J., Isono Y.,
RA Kawai-Hio Y., Saito K., Nishikawa T., Kimura K., Yamashita H., Matsuo K.,
RA Nakamura Y., Sekine M., Kikuchi H., Kanda K., Wagatsuma M., Murakawa K.,
RA Kanehori K., Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B.,
RA Suzuki Y., Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.;
RT "NEDO cDNA sequencing project.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC acyl-CoA, the first step in fatty acid metabolism (By similarity).
CC Capable of activating medium-chain fatty acids (e.g. butyric (C4) to
CC decanoic (C10) acids), and certain carboxylate-containing xenobiotics,
CC e.g. benzoate (By similarity). {ECO:0000250|UniProtKB:Q68CK6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:10132, ChEBI:CHEBI:16150, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369,
CC ChEBI:CHEBI:456215; EC=6.2.1.25;
CC Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10133;
CC Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q68CK6};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q68CK6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q68CK6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8K0L3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K0L3-2; Sequence=VSP_028393;
CC Name=3;
CC IsoId=Q8K0L3-3; Sequence=VSP_028394;
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AK140827; BAE24490.1; -; mRNA.
DR EMBL; AK143757; BAE25526.1; -; mRNA.
DR EMBL; AK165353; BAE38146.1; -; mRNA.
DR EMBL; AK165401; BAE38163.1; -; mRNA.
DR EMBL; AK057650; BAB71542.1; -; mRNA.
DR EMBL; BC024424; AAH24424.1; -; mRNA.
DR EMBL; BC031140; AAH31140.1; -; mRNA.
DR CCDS; CCDS21782.1; -. [Q8K0L3-1]
DR CCDS; CCDS52379.1; -. [Q8K0L3-2]
DR CCDS; CCDS52380.1; -. [Q8K0L3-3]
DR RefSeq; NP_001171448.1; NM_001177977.1. [Q8K0L3-2]
DR RefSeq; NP_001171449.1; NM_001177978.1. [Q8K0L3-3]
DR RefSeq; NP_666309.1; NM_146197.4. [Q8K0L3-1]
DR AlphaFoldDB; Q8K0L3; -.
DR SMR; Q8K0L3; -.
DR BioGRID; 231445; 1.
DR STRING; 10090.ENSMUSP00000081697; -.
DR iPTMnet; Q8K0L3; -.
DR PhosphoSitePlus; Q8K0L3; -.
DR jPOST; Q8K0L3; -.
DR MaxQB; Q8K0L3; -.
DR PaxDb; Q8K0L3; -.
DR PeptideAtlas; Q8K0L3; -.
DR PRIDE; Q8K0L3; -.
DR ProteomicsDB; 285710; -. [Q8K0L3-1]
DR ProteomicsDB; 285711; -. [Q8K0L3-2]
DR ProteomicsDB; 285712; -. [Q8K0L3-3]
DR DNASU; 233799; -.
DR Ensembl; ENSMUST00000084647; ENSMUSP00000081697; ENSMUSG00000030945. [Q8K0L3-3]
DR Ensembl; ENSMUST00000098084; ENSMUSP00000095690; ENSMUSG00000030945. [Q8K0L3-2]
DR Ensembl; ENSMUST00000167935; ENSMUSP00000126670; ENSMUSG00000030945. [Q8K0L3-1]
DR GeneID; 233799; -.
DR KEGG; mmu:233799; -.
DR UCSC; uc009jlh.2; mouse. [Q8K0L3-1]
DR UCSC; uc009jli.2; mouse. [Q8K0L3-3]
DR UCSC; uc009jlj.2; mouse. [Q8K0L3-2]
DR CTD; 233799; -.
DR MGI; MGI:2385289; Acsm2.
DR VEuPathDB; HostDB:ENSMUSG00000030945; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000163352; -.
DR HOGENOM; CLU_000022_59_10_1; -.
DR InParanoid; Q8K0L3; -.
DR OMA; TPSDWAW; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q8K0L3; -.
DR TreeFam; TF354287; -.
DR Reactome; R-MMU-177128; Conjugation of salicylate with glycine.
DR Reactome; R-MMU-177135; Conjugation of benzoate with glycine.
DR Reactome; R-MMU-177162; Conjugation of phenylacetate with glutamine.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR BioGRID-ORCS; 233799; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Acsm2; mouse.
DR PRO; PR:Q8K0L3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K0L3; protein.
DR Bgee; ENSMUSG00000030945; Expressed in right kidney and 51 other tissues.
DR ExpressionAtlas; Q8K0L3; baseline and differential.
DR Genevisible; Q8K0L3; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0018858; F:benzoate-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; ISO:MGI.
DR GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:RHEA.
DR GO; GO:0015645; F:fatty acid ligase activity; IBA:GO_Central.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..575
FT /note="Acyl-coenzyme A synthetase ACSM2, mitochondrial"
FT /id="PRO_0000306095"
FT BINDING 139
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 221..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 360..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 470..472
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 502
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 533
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 541..543
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 558
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MTTGSLDLPFVGSHRWIKWTTASLTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028393"
FT VAR_SEQ 471
FT /note="G -> GAYFCR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028394"
FT CONFLICT 515
FT /note="E -> G (in Ref. 2; BAB71542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 64269 MW; A7E5956D54B119D8 CRC64;
MHHLWKIPRL FTLWGNEISC RTFHMNIKKL IPIQWGHQEA PAKFNFASDV IDHWASVEKA
GKRSSGPALW WMNGSGKEIK WSFRELSEAS KQTANVLSGA CGLHRGDRVA VVLPRIPEWW
LMILGCMRTG LVFMPGTIQM RSSDILYRLQ ASKARAIVAG DEVAQEVDAV APDCSFLKIK
LLVSENSREG WLNFKALLKE ASTIHQCVET ESRESAAIYF TSGTSGPPKM AEHSHCSLGI
KAKMDAASWT GLSTSDIIWT ISDTAWIMNI LGAFLEPWVL GACIFVHLLP KFDSQTVLKV
LSSYPINTLV GAPIIYRMLL QQDLSSYKFP HLHSCFSGGE TLLPETLENW KAKTGLEIRE
IYGQTETGLI CRVSRTMKVK PGYLGTAFAH YDVQVIDEQG NVLPPGKEGD IAIRVKPIWP
IGMFSGYVDN PKKTQDNIRG DFWLMGDRGI KDPEGYFHFI GRSDDIINSS GYRIGPSEVE
NALMEHPAVS ETAVISSPDP SRGEVVKAFV VLAPEFLSHD RDQLTKVLQE HVKSVTAPYK
YPRKVEFVLD LPKTVTGKIE RAKLRAKEWK TSGRA
