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

 ACSM1_MOUSE             Reviewed;         573 AA.
Q91VA0; Q3UED4;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
07-JUN-2017, entry version 130.
RecName: Full=Acyl-coenzyme A synthetase ACSM1, mitochondrial;
EC=6.2.1.2;
AltName: Full=Acyl-CoA synthetase medium-chain family member 1;
AltName: Full=Butyrate--CoA ligase 1;
AltName: Full=Butyryl-coenzyme A synthetase 1;
AltName: Full=Lipoate-activating enzyme;
AltName: Full=Middle-chain acyl-CoA synthetase 1;
Flags: Precursor;
Name=Acsm1; Synonyms=Bucs1, Lae, Macs1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=11470804; DOI=10.1074/jbc.M106651200;
Fujino T., Takei Y.A., Sone H., Ioka R.X., Kamataki A., Magoori K.,
Takahashi S., Sakai J., Yamamoto T.T.;
"Molecular identification and characterization of two medium-chain
acyl-CoA synthetases, MACS1 and the Sa gene product.";
J. Biol. Chem. 276:35961-35966(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Kidney, and Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 249-254, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16378734; DOI=10.1016/j.pep.2005.11.006;
Kasuya F., Tatsuki T., Ohta M., Kawai Y., Igarashi K.;
"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.";
Protein Expr. Purif. 47:405-414(2006).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-142; LYS-179;
LYS-200; LYS-233; LYS-324; LYS-352; LYS-387; LYS-501 AND LYS-534, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142; LYS-200; LYS-210;
LYS-352; LYS-387; LYS-527; LYS-534 AND LYS-545, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- 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 C(4) to
C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-
unsaturated acids (in vitro). {ECO:0000250,
ECO:0000269|PubMed:11470804}.
-!- CATALYTIC ACTIVITY: ATP + a carboxylate + CoA = AMP + diphosphate
+ an acyl-CoA.
-!- CATALYTIC ACTIVITY: GTP + lipoate = diphosphate + lipoyl-GMP.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:11470804}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q91VA0-1; Sequence=Displayed;
Name=2;
IsoId=Q91VA0-2; Sequence=VSP_028392;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in liver and kidney.
{ECO:0000269|PubMed:11470804}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB059428; BAB64534.1; -; mRNA.
EMBL; AK149550; BAE28952.1; -; mRNA.
EMBL; AK149586; BAE28977.1; -; mRNA.
EMBL; BC016414; AAH16414.1; -; mRNA.
EMBL; BC022149; AAH22149.1; -; mRNA.
CCDS; CCDS21783.1; -. [Q91VA0-1]
RefSeq; NP_473435.1; NM_054094.5. [Q91VA0-1]
UniGene; Mm.427560; -.
ProteinModelPortal; Q91VA0; -.
SMR; Q91VA0; -.
IntAct; Q91VA0; 3.
MINT; MINT-1860696; -.
STRING; 10090.ENSMUSP00000036140; -.
SwissLipids; SLP:000001205; -.
iPTMnet; Q91VA0; -.
PhosphoSitePlus; Q91VA0; -.
SwissPalm; Q91VA0; -.
PaxDb; Q91VA0; -.
PeptideAtlas; Q91VA0; -.
PRIDE; Q91VA0; -.
DNASU; 117147; -.
Ensembl; ENSMUST00000047929; ENSMUSP00000036140; ENSMUSG00000033533. [Q91VA0-1]
GeneID; 117147; -.
KEGG; mmu:117147; -.
UCSC; uc009jlm.1; mouse. [Q91VA0-1]
UCSC; uc012fsv.1; mouse. [Q91VA0-2]
CTD; 116285; -.
MGI; MGI:2152200; Acsm1.
eggNOG; KOG1175; Eukaryota.
eggNOG; COG0365; LUCA.
GeneTree; ENSGT00760000119178; -.
HOGENOM; HOG000229982; -.
HOVERGEN; HBG053031; -.
InParanoid; Q91VA0; -.
KO; K01896; -.
OMA; FTSIRFP; -.
OrthoDB; EOG091G03NW; -.
PhylomeDB; Q91VA0; -.
TreeFam; TF354287; -.
Reactome; R-MMU-177135; Conjugation of benzoate with glycine.
Reactome; R-MMU-177162; Conjugation of phenylacetate with glutamine.
PRO; PR:Q91VA0; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000033533; -.
CleanEx; MM_ACSM1; -.
ExpressionAtlas; Q91VA0; baseline and differential.
Genevisible; Q91VA0; MM.
GO; GO:0072562; C:blood microparticle; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0003996; F:acyl-CoA ligase activity; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0047760; F:butyrate-CoA ligase activity; ISS:UniProtKB.
GO; GO:0015645; F:fatty acid ligase activity; IDA:MGI.
GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
GO; GO:0006633; P:fatty acid biosynthetic process; IDA:MGI.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Direct protein sequencing; Fatty acid metabolism; GTP-binding; Ligase;
Lipid metabolism; Magnesium; Metal-binding; Mitochondrion;
Nucleotide-binding; Reference proteome; Transit peptide.
TRANSIT 1 35 Mitochondrion. {ECO:0000255}.
CHAIN 36 573 Acyl-coenzyme A synthetase ACSM1,
mitochondrial.
/FTId=PRO_0000306092.
NP_BIND 222 230 ATP. {ECO:0000250}.
BINDING 448 448 ATP. {ECO:0000250}.
BINDING 463 463 ATP. {ECO:0000250}.
BINDING 559 559 ATP. {ECO:0000250}.
MOD_RES 81 81 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 142 142 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 142 142 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 179 179 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 200 200 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 200 200 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 210 210 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 233 233 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 324 324 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 352 352 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 352 352 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 387 387 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 387 387 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 501 501 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 527 527 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 534 534 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 534 534 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 545 545 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
VAR_SEQ 369 395 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_028392.
CONFLICT 465 465 D -> V (in Ref. 2; BAE28977).
{ECO:0000305}.
CONFLICT 525 525 L -> F (in Ref. 2; BAE28977).
{ECO:0000305}.
SEQUENCE 573 AA; 64760 MW; 557F25D467CA305B CRC64;
MQWLKSFQIC KVLQGFSLSP TQLHRRLFSR VGAPRWNDHD SPEEFNFASD VLDYWAQMEE
EGKRGPSPAF WWVNGQGDEI KWSFRKLRDL TCRTANVFEQ ICGLQQGDHL ALILPRVPEW
WLVTVGCMRT GIIFMPGTTQ LKAKDILYRI QISRAKAIVT TASLVPEVES VASECPDLKT
KLVVSDHSHE GWLDFCSLIK SASPDHTCIK SKMKDPMAIF FTSGTTGYPK MAKHNQGLAF
RSYIPSCRKL LKLKTSDILW CMSDPGWILA TVGCLIEPWT SGCTVFIHHL PQFDPKVIVE
VLFKYPITQC LAAPGVYRMV LQQKTSNLRF PTLEHCTTGG ESLLPEEYEQ WKQRTGLSIH
EVYGQSETGI SSATLREMKI KRGSIGKAIL PFDLQIIDEK GNILPPNTEG YIGIRIKPTR
PLGLFMEYEN SPESTSEVEC GDFYNSGDRA TIDEEGYIWF LGRGDDVINA SGYRIGPVEV
ENALAEHPAV AESAVVSSPD KDRGEVVKAF IVLNPEFLSH DQEQLIKELQ HHVKSVTAPY
KYPRKVEFVS ELPKTVTGKI KRKELRNKEF GQL


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