ACSM5_MOUSE
ID ACSM5_MOUSE Reviewed; 578 AA.
AC Q8BGA8; Q8BJS0; Q8BM02; Q8BWQ8; Q8BWS7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Acyl-coenzyme A synthetase ACSM5, mitochondrial;
DE EC=6.2.1.2 {ECO:0000250|UniProtKB:Q08AH1};
DE Flags: Precursor;
GN Name=Acsm5; Synonyms=Macs3;
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 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Liver, and Vein;
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 2).
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 [3]
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).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-96 AND LYS-302, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-151; LYS-302 AND LYS-335,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC acyl-CoA, the first step in fatty acid metabolism.
CC {ECO:0000250|UniProtKB:Q08AH1}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q91VA0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BGA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGA8-2; Sequence=VSP_028399, VSP_028400;
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AK040650; BAC30656.1; -; mRNA.
DR EMBL; AK050132; BAC34084.1; -; mRNA.
DR EMBL; AK050219; BAC34130.1; -; mRNA.
DR EMBL; AK050288; BAC34167.1; -; mRNA.
DR EMBL; AK050458; BAC34268.1; -; mRNA.
DR EMBL; AK080219; BAC37850.1; -; mRNA.
DR EMBL; AK149591; BAE28980.1; -; mRNA.
DR EMBL; BC095985; AAH95985.1; -; mRNA.
DR CCDS; CCDS40106.1; -. [Q8BGA8-1]
DR RefSeq; NP_848873.1; NM_178758.3. [Q8BGA8-1]
DR AlphaFoldDB; Q8BGA8; -.
DR SMR; Q8BGA8; -.
DR STRING; 10090.ENSMUSP00000063416; -.
DR iPTMnet; Q8BGA8; -.
DR PhosphoSitePlus; Q8BGA8; -.
DR SwissPalm; Q8BGA8; -.
DR jPOST; Q8BGA8; -.
DR MaxQB; Q8BGA8; -.
DR PaxDb; Q8BGA8; -.
DR PeptideAtlas; Q8BGA8; -.
DR PRIDE; Q8BGA8; -.
DR ProteomicsDB; 285715; -. [Q8BGA8-1]
DR ProteomicsDB; 285716; -. [Q8BGA8-2]
DR Antibodypedia; 25526; 111 antibodies from 18 providers.
DR DNASU; 272428; -.
DR Ensembl; ENSMUST00000066465; ENSMUSP00000063416; ENSMUSG00000030972. [Q8BGA8-1]
DR Ensembl; ENSMUST00000207387; ENSMUSP00000146357; ENSMUSG00000030972. [Q8BGA8-2]
DR Ensembl; ENSMUST00000207440; ENSMUSP00000146938; ENSMUSG00000030972. [Q8BGA8-1]
DR GeneID; 272428; -.
DR KEGG; mmu:272428; -.
DR UCSC; uc009jle.1; mouse. [Q8BGA8-2]
DR UCSC; uc009jlf.1; mouse. [Q8BGA8-1]
DR CTD; 54988; -.
DR MGI; MGI:2444086; Acsm5.
DR VEuPathDB; HostDB:ENSMUSG00000030972; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000161148; -.
DR HOGENOM; CLU_000022_59_10_1; -.
DR InParanoid; Q8BGA8; -.
DR OMA; TTFYDGP; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q8BGA8; -.
DR TreeFam; TF354287; -.
DR Reactome; R-MMU-177128; Conjugation of salicylate with glycine.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR BioGRID-ORCS; 272428; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Marcksl1; mouse.
DR PRO; PR:Q8BGA8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BGA8; protein.
DR Bgee; ENSMUSG00000030972; Expressed in left lobe of liver and 55 other tissues.
DR ExpressionAtlas; Q8BGA8; baseline and differential.
DR Genevisible; Q8BGA8; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
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:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
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 Acetylation; Alternative splicing; ATP-binding; Fatty acid metabolism;
KW Ligase; Lipid metabolism; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..578
FT /note="Acyl-coenzyme A synthetase ACSM5, mitochondrial"
FT /id="PRO_0000306102"
FT BINDING 229..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 367..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 96
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 96
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 151
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 302
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 302
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 335
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 307..310
FT /note="TLCR -> VRRKI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_028399"
FT VAR_SEQ 311..578
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_028400"
FT CONFLICT 6
FT /note="R -> T (in Ref. 1; BAC34084)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="L -> S (in Ref. 1; BAC34084)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="K -> N (in Ref. 1; BAC34084)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="G -> E (in Ref. 1; BAC30656)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="S -> G (in Ref. 1; BAC34167/BAE28980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 64328 MW; AF6BE6B148FEC91E CRC64;
MRLWLRGLAC QALRSSWGVC RIHTQPPPPP IPEVVATWEA ISLGRQPVPE YFNFAHDVLD
VWSQLEKTGH RPPNPAFWWV NGSGTEVKWT FEELGKQSRK AANVLEGVCG LQPGDRMMLV
LPRLPDWWLI SVACMRTGVV MIPGVSQLTA KDLKYRLQAA RAKSIVTSDA LAPQVDAISA
DCPSLQTKLL VSDTSRPGWI NFRELLRAAS PEHNCVRTRS GDSVAIYFTS GTTGAPKMVE
HSQSSYGLGF VASGRRWMAL TESDIFWNTT DTGWVKAAWT LFSAWSNGAC IFVHELPRVD
AKTILNTLCR FPITTLCCVP TLFRLLVQED LTRYKFQCLR HCLTGGEALN PDVRDKWKSQ
TGLELHEGYG QSETVVICGN SRNSTIKSGS MGKASPPYDV QIVDEEGNVL PPGKEGNIAV
RIKPTRPFCF FNCYLDNPEK TAASEQGDFY ITGDRAHMDE DGYFWFLGRN DDVINSSSYR
IGPVEVESAL AEHPAVLESA VVSSPDPIRG EVVKAFIVLS PAYASHDPEA LTRELQEHVK
TVTAPYKYPR KVAFISELPK TVSGKILRSK LRNQEWGR
