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ACSS3_MOUSE
ID   ACSS3_MOUSE             Reviewed;         682 AA.
AC   Q14DH7; Q8BZX0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Acyl-CoA synthetase short-chain family member 3, mitochondrial;
DE            EC=6.2.1.1 {ECO:0000250|UniProtKB:A0A0G2K047};
DE   AltName: Full=Acetate--CoA ligase 3;
DE   AltName: Full=Propionate--CoA ligase;
DE            EC=6.2.1.17 {ECO:0000250|UniProtKB:A0A0G2K047};
DE   Flags: Precursor;
GN   Name=Acss3;
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] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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=Brown adipose tissue, Kidney, Liver, and Lung;
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   [5]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-513, AND IDENTIFICATION BY MASS
RP   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   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-519, AND IDENTIFICATION BY MASS
RP   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 synthesis of acetyl-CoA from short-chain fatty
CC       acids (By similarity). Propionate is the preferred substrate but can
CC       also utilize acetate and butyrate with a much lower affinity (By
CC       similarity). {ECO:0000250|UniProtKB:A0A0G2K047}.
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:0000250|UniProtKB:A0A0G2K047};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC         Evidence={ECO:0000250|UniProtKB:A0A0G2K047};
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:0000250|UniProtKB:A0A0G2K047};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC         Evidence={ECO:0000250|UniProtKB:A0A0G2K047};
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:A0A0G2K047};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC         Evidence={ECO:0000250|UniProtKB:A0A0G2K047};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:A0A0G2K047}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q14DH7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14DH7-2; Sequence=VSP_031693, VSP_031694;
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AK033376; BAC28254.1; -; mRNA.
DR   EMBL; AC111014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC121946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC134457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC113198; AAI13199.1; -; mRNA.
DR   CCDS; CCDS24159.1; -. [Q14DH7-2]
DR   CCDS; CCDS48688.1; -. [Q14DH7-1]
DR   RefSeq; NP_001136276.1; NM_001142804.1. [Q14DH7-1]
DR   RefSeq; NP_941038.2; NM_198636.3. [Q14DH7-2]
DR   AlphaFoldDB; Q14DH7; -.
DR   SMR; Q14DH7; -.
DR   STRING; 10090.ENSMUSP00000040823; -.
DR   iPTMnet; Q14DH7; -.
DR   PhosphoSitePlus; Q14DH7; -.
DR   jPOST; Q14DH7; -.
DR   MaxQB; Q14DH7; -.
DR   PaxDb; Q14DH7; -.
DR   PeptideAtlas; Q14DH7; -.
DR   PRIDE; Q14DH7; -.
DR   ProteomicsDB; 285851; -. [Q14DH7-1]
DR   ProteomicsDB; 285852; -. [Q14DH7-2]
DR   Antibodypedia; 29817; 121 antibodies from 27 providers.
DR   DNASU; 380660; -.
DR   Ensembl; ENSMUST00000044668; ENSMUSP00000040823; ENSMUSG00000035948. [Q14DH7-2]
DR   Ensembl; ENSMUST00000165067; ENSMUSP00000128209; ENSMUSG00000035948. [Q14DH7-1]
DR   GeneID; 380660; -.
DR   KEGG; mmu:380660; -.
DR   UCSC; uc007gyv.2; mouse. [Q14DH7-2]
DR   UCSC; uc011xna.1; mouse. [Q14DH7-1]
DR   CTD; 79611; -.
DR   MGI; MGI:2685720; Acss3.
DR   VEuPathDB; HostDB:ENSMUSG00000035948; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   GeneTree; ENSGT00940000157479; -.
DR   HOGENOM; CLU_000022_3_5_1; -.
DR   InParanoid; Q14DH7; -.
DR   OMA; YVFVMGR; -.
DR   OrthoDB; 288915at2759; -.
DR   PhylomeDB; Q14DH7; -.
DR   TreeFam; TF354241; -.
DR   Reactome; R-MMU-77111; Synthesis of Ketone Bodies.
DR   BioGRID-ORCS; 380660; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Acss3; mouse.
DR   PRO; PR:Q14DH7; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q14DH7; protein.
DR   Bgee; ENSMUSG00000035948; Expressed in white adipose tissue and 155 other tissues.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047760; F:butyrate-CoA ligase activity; ISS:UniProtKB.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
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   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Ligase; Lipid metabolism;
KW   Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..682
FT                   /note="Acyl-CoA synthetase short-chain family member 3,
FT                   mitochondrial"
FT                   /id="PRO_0000320625"
FT   BINDING         222..225
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         420..422
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         441..446
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         534
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         549
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         560
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         619
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         513
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         519
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   VAR_SEQ         479
FT                   /note="V -> GRYLLHHSAESLTPPAMGK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031693"
FT   VAR_SEQ         480..682
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031694"
FT   CONFLICT        477
FT                   /note="Y -> N (in Ref. 1; BAC28254)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   682 AA;  74518 MW;  B865D534C631D5D1 CRC64;
     MKPSWLQCRK VTGAGTLGAP LPGSPSVRGA AVTRRALVAG FGGRGCRALT TGSGGEYKTH
     FAASVADPER FWGKAAEQIS WYKPWTKTLE SRYPPSTSWF VEGMLNICYN AIDRHIENGQ
     GDKIAIIYDS PVTDTKATIS YKEVLEQVSK LAGVLVKQGV KKGDTVVIYM PMIPQAIYTM
     LACARIGAIH SLIFGGFASK ELSTRIDHAK PKVVVTASFG IEPGRKVEYI PLLEEALRIG
     QHRPDRVLIY SRPNMEKVPL MSGRDLDWEE EMAKAQSHDC VPVLSEHPLY ILYTSGTTGL
     PKGVVRPTGG YAVMLNWTMS SIYGLKPGEV WWAASDLGWV VGHSYICYGP LLHGNTTVLY
     EGKPVGTPDA GAYFRVLAEH GVAALFTAPT AIRAIRQQDP GAALGKQYSL TRFKTLFVAG
     ERCDVETLEW SKKVFRVPVL DHWWQTETGS PITASCIGLG NSKTPPPGQA GKCVPGYNVM
     ILDDNMQKLK ARSLGNIVVK LPLPPGAFSG LWKNQEAFKH LYFEKFPGYY DTMDAGYMDE
     EGYLYVMSRV DDVINVAGHR ISAGAIEESV LSHGTVADCA VVGKEDPLKG HVPLALCVLK
     KDVNASEEQV LEEIVKHVRQ SIGPVAAFRN AVFVKQLPKT RSGKIPRSTL SALVNGKPYK
     VTPTIEDPSI FGHIEEVLKQ AV
 
 
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