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Acyl-coenzyme A synthetase ACSM3, mitochondrial (EC 6.2.1.2) (Acyl-CoA synthetase medium-chain family member 3) (Butyrate--CoA ligase 3) (Butyryl-coenzyme A synthetase 3) (Middle-chain acyl-CoA synthetase 3) (Protein SA homolog)

 ACSM3_MOUSE             Reviewed;         580 AA.
Q3UNX5; Q8BRY2; Q91WI1; Q9Z2F3; Q9Z2X0;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 2.
05-JUL-2017, entry version 98.
RecName: Full=Acyl-coenzyme A synthetase ACSM3, mitochondrial;
EC=6.2.1.2;
AltName: Full=Acyl-CoA synthetase medium-chain family member 3;
AltName: Full=Butyrate--CoA ligase 3;
AltName: Full=Butyryl-coenzyme A synthetase 3;
AltName: Full=Middle-chain acyl-CoA synthetase 3;
AltName: Full=Protein SA homolog;
Flags: Precursor;
Name=Acsm3; Synonyms=Sa, Sah;
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), TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=C57BL/6J;
PubMed=9449642; DOI=10.1210/endo.139.2.5763;
Melia M.J., Bofill N., Hubank M., Meseguer A.;
"Identification of androgen-regulated genes in mouse kidney by
representational difference analysis and random arbitrarily primed
polymerase chain reaction.";
Endocrinology 139:688-695(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=9507200; DOI=10.1046/j.1523-1755.1998.00808.x;
Takenaka M., Imai E., Kaneko T., Ito T., Moriyama T., Yamauchi A.,
Hori M., Kawamoto S., Okubo K.;
"Isolation of genes identified in mouse renal proximal tubule by
comparing different gene expression profiles.";
Kidney Int. 53:562-572(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
INDUCTION, AND TISSUE SPECIFICITY.
STRAIN=129/SvJ; TISSUE=Kidney;
PubMed=15525578; DOI=10.1677/joe.1.05649;
Areste C., Melia M.J., Isern J., Tovar J.L., Meseguer A.;
"Sex steroid regulation and identification of different transcription
units of the SA gene in mouse kidney.";
J. Endocrinol. 183:101-114(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Aorta, Kidney, and Vein;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Kidney;
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).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, and Liver;
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).
[8]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-67 AND LYS-100, 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).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-151, 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: 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:0000269|PubMed:11470804}.
-!- CATALYTIC ACTIVITY: ATP + a carboxylate + CoA = AMP + diphosphate
+ an acyl-CoA.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:11470804, ECO:0000269|PubMed:15525578}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q3UNX5-1; Sequence=Displayed;
Name=2;
IsoId=Q3UNX5-2; Sequence=VSP_028397;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in kidney (at protein level).
Detected in kidney proximal tubules and in liver. Detected at low
levels in testis, stomach, heart and lung.
{ECO:0000269|PubMed:11470804, ECO:0000269|PubMed:15525578,
ECO:0000269|PubMed:9449642, ECO:0000269|PubMed:9507200}.
-!- INDUCTION: Up-regulated in kidney by androgens. Down-regulated in
kidney by estrogens. Levels in kidney are very low in female
C57BL/6 mice and in castrated male C57BL/6, 129/SvJ and BALB/c
mice. Constitutively expressed in liver.
{ECO:0000269|PubMed:15525578, ECO:0000269|PubMed:9449642}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC79656.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH15248.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAL40880.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA37141.1; Type=Frameshift; Positions=1, 63, 72; Evidence={ECO:0000305};
Sequence=BAE38232.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY064696; AAL40880.1; ALT_INIT; mRNA.
EMBL; AB022340; BAA37141.1; ALT_FRAME; mRNA.
EMBL; AF068246; AAC79656.1; ALT_INIT; mRNA.
EMBL; AK041060; BAC30805.1; -; mRNA.
EMBL; AK143946; BAE25622.1; -; mRNA.
EMBL; AK165516; BAE38232.1; ALT_INIT; mRNA.
EMBL; BC015248; AAH15248.1; ALT_INIT; mRNA.
CCDS; CCDS21786.1; -. [Q3UNX5-1]
RefSeq; NP_058566.3; NM_016870.3. [Q3UNX5-1]
RefSeq; NP_997606.2; NM_212441.2. [Q3UNX5-1]
RefSeq; NP_997607.2; NM_212442.2. [Q3UNX5-1]
UniGene; Mm.334199; -.
ProteinModelPortal; Q3UNX5; -.
SMR; Q3UNX5; -.
STRING; 10090.ENSMUSP00000068803; -.
SwissLipids; SLP:000001206; -.
iPTMnet; Q3UNX5; -.
PhosphoSitePlus; Q3UNX5; -.
SwissPalm; Q3UNX5; -.
MaxQB; Q3UNX5; -.
PaxDb; Q3UNX5; -.
PeptideAtlas; Q3UNX5; -.
PRIDE; Q3UNX5; -.
Ensembl; ENSMUST00000063770; ENSMUSP00000068803; ENSMUSG00000030935. [Q3UNX5-1]
Ensembl; ENSMUST00000106526; ENSMUSP00000102136; ENSMUSG00000030935. [Q3UNX5-1]
Ensembl; ENSMUST00000106527; ENSMUSP00000102137; ENSMUSG00000030935. [Q3UNX5-1]
Ensembl; ENSMUST00000106528; ENSMUSP00000102138; ENSMUSG00000030935. [Q3UNX5-1]
Ensembl; ENSMUST00000106529; ENSMUSP00000102139; ENSMUSG00000030935. [Q3UNX5-2]
GeneID; 20216; -.
KEGG; mmu:20216; -.
UCSC; uc009jlq.1; mouse. [Q3UNX5-1]
CTD; 6296; -.
MGI; MGI:99538; Acsm3.
eggNOG; KOG1175; Eukaryota.
eggNOG; COG0365; LUCA.
GeneTree; ENSGT00760000119178; -.
HOGENOM; HOG000229982; -.
HOVERGEN; HBG053031; -.
InParanoid; Q3UNX5; -.
KO; K01896; -.
OMA; RGYMDED; -.
OrthoDB; EOG091G03NW; -.
PhylomeDB; Q3UNX5; -.
TreeFam; TF354287; -.
Reactome; R-MMU-77352; Beta oxidation of butanoyl-CoA to acetyl-CoA.
ChiTaRS; Acsm3; mouse.
PRO; PR:Q3UNX5; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030935; -.
CleanEx; MM_ACSM3; -.
Genevisible; Q3UNX5; MM.
GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0003996; F:acyl-CoA ligase activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0047760; F:butyrate-CoA ligase activity; TAS:Reactome.
GO; GO:0015645; F:fatty acid ligase activity; IDA:MGI.
GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
GO; GO:0006635; P:fatty acid beta-oxidation; TAS:Reactome.
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;
Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium;
Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
Transit peptide.
TRANSIT 1 21 Mitochondrion. {ECO:0000255}.
CHAIN 22 580 Acyl-coenzyme A synthetase ACSM3,
mitochondrial.
/FTId=PRO_0000306098.
NP_BIND 229 237 ATP. {ECO:0000250}.
NP_BIND 368 373 ATP. {ECO:0000250}.
BINDING 455 455 ATP. {ECO:0000250}.
BINDING 470 470 ATP. {ECO:0000250}.
BINDING 566 566 ATP. {ECO:0000250}.
MOD_RES 67 67 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 100 100 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 151 151 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
VAR_SEQ 578 580 VTT -> EQGLLHEQMTVDRLLGKSARHERHVPSVCMNCSG
VAAVLRYAEAA (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_028397.
CONFLICT 137 137 T -> P (in Ref. 3; AAC79656).
{ECO:0000305}.
SEQUENCE 580 AA; 65623 MW; CAF3D06A0B4A2778 CRC64;
MVMLLRARCF QRLAIPDPMR VLYKDYRTAT PQNFSNYESM KQDFKIEIPE YFNFAKDVLD
QWTNMEKAGK RLSNPAFWWI DGNGEELRWS FEELGLLSRK FANILTEACS LQRGDRVMVI
LPKIPEWWLA NVACLRTGTV LIPGTTQLTQ KDILYRLQSS KAKCIITDDT LAPAVDAVAA
KCENLHSKLI VSQHSREGWG NLKEMMKYAS DSHTCVDTKH DEMMAIYFTS GTTGPPKMIG
HTHSSFGLGL SVNGRFWLDL IASDVMWNTS DTGWAKSAWS SVFSPWTQGA CVFAHYLPRF
ESTSILQTLS KFPITVFCSA PTAYRMLVQN DMSSYKFNSL KHCVSAGEPI NPEVMEQWRK
KTGLDIYEGY GQTETVLICG NFKGMKIKPG SMGKPSPAFD VKILDENGAT LPPGQEGDIA
LQVLPERPFG LFTHYVDNPS KTASTLRGSF YITGDRGYMD EDGYFWFVAR SDDIILSSGY
RIGPFEVESA LIEHPSIAES AVVSSPDPIR GEVVKAFIVL NPDYKSHDQE QLKKEIQEHV
KKTTAPYKYP RKVEFIEELP KTVSGKVKRN ELRKKEWVTT


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