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ACS2L_MOUSE
ID   ACS2L_MOUSE             Reviewed;         682 AA.
AC   Q99NB1; Q8K0M6;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Acetyl-coenzyme A synthetase 2-like, mitochondrial;
DE            EC=6.2.1.1 {ECO:0000269|PubMed:11150295, ECO:0000269|PubMed:16790548};
DE   AltName: Full=Acetate--CoA ligase 2;
DE   AltName: Full=Acetyl-CoA synthetase 2 {ECO:0000303|PubMed:11150295, ECO:0000303|PubMed:16790548};
DE            Short=AceCS2 {ECO:0000303|PubMed:11150295, ECO:0000303|PubMed:16790548};
DE   AltName: Full=Acyl-CoA synthetase short-chain family member 1;
DE   AltName: Full=Propionate--CoA ligase;
DE            EC=6.2.1.17 {ECO:0000269|PubMed:11150295};
DE   Flags: Precursor;
GN   Name=Acss1; Synonyms=Acas2, Acas2l;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX   PubMed=11150295; DOI=10.1074/jbc.m008782200;
RA   Fujino T., Kondo J., Ishikawa M., Morikawa K., Yamamoto T.T.;
RT   "Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the
RT   oxidation of acetate.";
RL   J. Biol. Chem. 276:11420-11426(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-682.
RC   TISSUE=Salivary gland;
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   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, ACETYLATION AT LYS-635,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16790548; DOI=10.1073/pnas.0604392103;
RA   Hallows W.C., Lee S., Denu J.M.;
RT   "Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:10230-10235(2006).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19187775; DOI=10.1016/j.cmet.2008.12.008;
RA   Sakakibara I., Fujino T., Ishii M., Tanaka T., Shimosawa T., Miura S.,
RA   Zhang W., Tokutake Y., Yamamoto J., Awano M., Iwasaki S., Motoike T.,
RA   Okamura M., Inagaki T., Kita K., Ezaki O., Naito M., Kuwaki T., Chohnan S.,
RA   Yamamoto T.T., Hammer R.E., Kodama T., Yanagisawa M., Sakai J.;
RT   "Fasting-induced hypothermia and reduced energy production in mice lacking
RT   acetyl-CoA synthetase 2.";
RL   Cell Metab. 9:191-202(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC   Testis;
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 synthesis of acetyl-CoA from short-chain fatty
CC       acids (PubMed:11150295, PubMed:16790548). Acetate is the preferred
CC       substrate (PubMed:11150295, PubMed:16790548). Can also utilize
CC       propionate with a much lower affinity (PubMed:11150295). Provides
CC       acetyl-CoA that is utilized mainly for oxidation under ketogenic
CC       conditions (PubMed:11150295). Involved in thermogenesis under ketogenic
CC       conditions, using acetate as a vital fuel when carbohydrate
CC       availability is insufficient (PubMed:19187775).
CC       {ECO:0000269|PubMed:11150295, ECO:0000269|PubMed:16790548,
CC       ECO:0000269|PubMed:19187775}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456215; EC=6.2.1.1;
CC         Evidence={ECO:0000269|PubMed:11150295, ECO:0000269|PubMed:16790548};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC         Evidence={ECO:0000305|PubMed:11150295, ECO:0000305|PubMed:16790548};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC         Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC         ChEBI:CHEBI:456215; EC=6.2.1.17;
CC         Evidence={ECO:0000269|PubMed:11150295};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC         Evidence={ECO:0000305|PubMed:11150295};
CC   -!- ACTIVITY REGULATION: Inhibited by acetylation at Lys-635 and activated
CC       by deacetylation mediated by the deacetylase SIRT3.
CC       {ECO:0000269|PubMed:16790548}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.06 mM for acetate {ECO:0000269|PubMed:11150295};
CC         KM=4.1 mM for propionate {ECO:0000269|PubMed:11150295};
CC   -!- SUBUNIT: Interacts with SIRT3. {ECO:0000250|UniProtKB:Q9NUB1}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:11150295}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, testis, kidney, skeletal
CC       muscle, lung and spleen. Detected at low levels in brain.
CC       {ECO:0000269|PubMed:11150295}.
CC   -!- INDUCTION: By fasting. {ECO:0000269|PubMed:11150295}.
CC   -!- PTM: Reversibly acetylated at Lys-635 (PubMed:16790548). The acetyl-CoA
CC       synthase activity is inhibited by acetylation and activated by
CC       deacetylation mediated by the deacetylase SIRT3.
CC       {ECO:0000269|PubMed:16790548}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype at birth, but exhibit
CC       significant growth retardation at the time of weaning. Attain normal
CC       size and weight when fed normally. Exhibit hypothermia and hypoglycemia
CC       when fed high-fat, low-carbohydrate diet, leading to 50% mortality.
CC       Display strongly reduced whole-body acetate oxidation when fasting.
CC       Fasting adults exhibit hypothermia, reduced capacity to sustain running
CC       and low ATP levels. {ECO:0000269|PubMed:19187775}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30930.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB046742; BAB21612.1; -; mRNA.
DR   EMBL; AK088244; BAC40232.1; -; mRNA.
DR   EMBL; BC030930; AAH30930.1; ALT_INIT; mRNA.
DR   CCDS; CCDS16859.1; -.
DR   RefSeq; NP_542142.1; NM_080575.2.
DR   AlphaFoldDB; Q99NB1; -.
DR   SMR; Q99NB1; -.
DR   BioGRID; 213026; 2.
DR   DIP; DIP-61209N; -.
DR   IntAct; Q99NB1; 6.
DR   MINT; Q99NB1; -.
DR   STRING; 10090.ENSMUSP00000028944; -.
DR   iPTMnet; Q99NB1; -.
DR   PhosphoSitePlus; Q99NB1; -.
DR   EPD; Q99NB1; -.
DR   jPOST; Q99NB1; -.
DR   MaxQB; Q99NB1; -.
DR   PaxDb; Q99NB1; -.
DR   PRIDE; Q99NB1; -.
DR   ProteomicsDB; 285542; -.
DR   Antibodypedia; 24959; 141 antibodies from 24 providers.
DR   DNASU; 68738; -.
DR   Ensembl; ENSMUST00000028944; ENSMUSP00000028944; ENSMUSG00000027452.
DR   GeneID; 68738; -.
DR   KEGG; mmu:68738; -.
DR   UCSC; uc008muf.2; mouse.
DR   CTD; 84532; -.
DR   MGI; MGI:1915988; Acss1.
DR   VEuPathDB; HostDB:ENSMUSG00000027452; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   GeneTree; ENSGT00940000158550; -.
DR   HOGENOM; CLU_000022_3_6_1; -.
DR   InParanoid; Q99NB1; -.
DR   OMA; AIKASWP; -.
DR   OrthoDB; 288915at2759; -.
DR   PhylomeDB; Q99NB1; -.
DR   TreeFam; TF354241; -.
DR   BRENDA; 6.2.1.1; 3474.
DR   Reactome; R-MMU-71384; Ethanol oxidation.
DR   BioGRID-ORCS; 68738; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Acss1; mouse.
DR   PRO; PR:Q99NB1; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q99NB1; protein.
DR   Bgee; ENSMUSG00000027452; Expressed in submandibular gland and 257 other tissues.
DR   ExpressionAtlas; Q99NB1; baseline and differential.
DR   Genevisible; Q99NB1; MM.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0019413; P:acetate biosynthetic process; ISO:MGI.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IDA:MGI.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   GO; GO:0019542; P:propionate biosynthetic process; ISO:MGI.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR011904; Ac_CoA_lig.
DR   InterPro; IPR032387; ACAS_N.
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; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Ligase; Lipid metabolism; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Transit peptide.
FT   TRANSIT         1..38
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..682
FT                   /note="Acetyl-coenzyme A synthetase 2-like, mitochondrial"
FT                   /id="PRO_0000000597"
FT   BINDING         217..220
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         334
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         410..412
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         434..439
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         526
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         541
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         549
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         552
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         389
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUB1"
FT   MOD_RES         635
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:16790548"
FT   CONFLICT        332
FT                   /note="W -> C (in Ref. 3; AAH30930)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   682 AA;  74623 MW;  1B21981D29F9C8E7 CRC64;
     MAARSLGSGV GRLLRGLQGR SGQSGWSLSV SRSTATRLPG CVPAAAQPGS YPALSAQAAQ
     EPAAFWGPLA RDTLVWDTPY HTVWDCDFRT GKIGWFLGGQ LNVSVNCLDQ HVQKSPETIA
     LIWERDEPGT EVRITYRELL ETTCRLANTL KRHGVHRGDR VAIYMPVSPL AVAAMLACAR
     IGAIHTVVFA GFSAESLAGR INDAKCKAVI TFNQGLRGGR VVELKKIVDE AVKSCPTVQH
     VLVAHRTDTK VPMGSLDIPL EQEMAKEAPV CTPESMSSED MLFMLYTSGS TGTPKGLVHT
     QAGYLLYAAM THKLVFDYQP GDVFGCVADI GWITGHSYVV YGPLCNGATT VLFESTPVYP
     DAGRYWETVQ RLKINQFYGA PTAVRLLLKY GDAWVKKYDR SSLRTLGSVG EPINHEAWEW
     LHKVVGDGRC TLVDTWWQTE TGGICIAPRP SEDGAEILPG MAMRPFFGIV PVLMDEKGNV
     LEGGDVSGAL CISQAWPGMA RTIYGDHQRF VDAYFRAYPG YYFTGDGAHR TEGGYYQITG
     RMDDVINISG HRLGTAEIED AMADHPAVPE TAVIGYPHDI KGEAAFAFIV LKDNISDENM
     VVNELKLSVA TKIAKYAVPD QILVVKRLPK TRSGKVMRRL LRKIITSRGQ DLGDTTTLED
     PSVITEILSA FQKYEEQRAA TN
 
 
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