ACSS3_RAT
ID ACSS3_RAT Reviewed; 683 AA.
AC A0A0G2K047;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Acyl-CoA synthetase short-chain family member 3, mitochondrial;
DE EC=6.2.1.1 {ECO:0000269|PubMed:28003429};
DE AltName: Full=Acetate--CoA ligase 3;
DE AltName: Full=Acyl-CoA synthetase short-chain family member 3;
DE AltName: Full=Propionate--CoA ligase;
DE EC=6.2.1.17 {ECO:0000269|PubMed:28003429};
DE Flags: Precursor;
GN Name=Acss3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=28003429; DOI=10.1093/jb/mvw067;
RA Yoshimura Y., Araki A., Maruta H., Takahashi Y., Yamashita H.;
RT "Molecular cloning of rat acss3 and characterization of mammalian
RT propionyl-CoA synthetase in the liver mitochondrial matrix.";
RL J. Biochem. 161:279-289(2017).
CC -!- FUNCTION: Catalyzes the synthesis of acetyl-CoA from short-chain fatty
CC acids (PubMed:28003429). Propionate is the preferred substrate but can
CC also utilize acetate and butyrate with a much lower affinity
CC (PubMed:28003429). {ECO:0000269|PubMed:28003429}.
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:28003429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC Evidence={ECO:0000305|PubMed:28003429};
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:28003429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC Evidence={ECO:0000305|PubMed:28003429};
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:0000269|PubMed:28003429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC Evidence={ECO:0000305|PubMed:28003429};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 mM for acetate {ECO:0000269|PubMed:28003429};
CC KM=3.7 mM for butyrate {ECO:0000269|PubMed:28003429};
CC KM=0.19 mM for propionate {ECO:0000269|PubMed:28003429};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:28003429}.
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of tissues, with the
CC highest levels observed in the liver followed by kidney.
CC {ECO:0000269|PubMed:28003429}.
CC -!- INDUCTION: Expression is up-regulated by fasting.
CC {ECO:0000269|PubMed:28003429}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AABR07056959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07056960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07056961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473960; EDM16777.1; -; Genomic_DNA.
DR RefSeq; XP_006241364.1; XM_006241302.3.
DR AlphaFoldDB; A0A0G2K047; -.
DR SMR; A0A0G2K047; -.
DR IntAct; A0A0G2K047; 1.
DR STRING; 10116.ENSRNOP00000062459; -.
DR SwissLipids; SLP:000001690; -.
DR PhosphoSitePlus; A0A0G2K047; -.
DR Ensembl; ENSRNOT00000082141; ENSRNOP00000071300; ENSRNOG00000004448.
DR GeneID; 314800; -.
DR CTD; 79611; -.
DR RGD; 1307051; Acss3.
DR GeneTree; ENSGT00940000157479; -.
DR OMA; YVFVMGR; -.
DR OrthoDB; 288915at2759; -.
DR BRENDA; 6.2.1.17; 5301.
DR Reactome; R-RNO-77111; Synthesis of Ketone Bodies.
DR PRO; PR:A0A0G2K047; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000004448; Expressed in liver and 18 other tissues.
DR ExpressionAtlas; A0A0G2K047; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; ATP-binding; Ligase; Lipid metabolism; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..683
FT /note="Acyl-CoA synthetase short-chain family member 3,
FT mitochondrial"
FT /id="PRO_0000447679"
FT BINDING 223..226
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 421..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 442..447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 550
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 561
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 620
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 514
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14DH7"
FT MOD_RES 520
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14DH7"
SQ SEQUENCE 683 AA; 74675 MW; 853A77EF7F42C0D2 CRC64;
MKPSWLQCRK VTGAGTLGAP LPGSPSVRGA GVARRALVAG FGGRGCRALT TSSGGGEYKT
HFAASVADPE RFWGKAAEQI SWYKPWTKTL ENRYPPSTSW FVEGMLNICY NAIDRHIENG
QGDKIAIIYD SPVTDTKATI SYKEVLEQVS KLAGVLVKQG VKKGDTVVIY MPMIPQAIYA
MLACARIGAI HSLIFGGFAS KELSTRIDHV KPKVVVTASF GIEPGRKVEY MPLLEEALRI
GQHKPDRLLI YNRPNMEKVP LMSGRDLDWE EEMAKAQSHD CVPVLSEHPL YILYTSGTTG
LPKGVVRPTG GYAVMLNWTM SSIYGLKPGE VWWAASDLGW VVGHSYICYG PLLHGNTTVL
YEGKPVGTPD AGAYFRVLAE HGVAALFTAP TAIRAIRQQD PGAALGKQYS LTRFKTLFVA
GERCDVETLE WSKKVFRVPV LDHWWQTETG SPITASCIGL GNSKTPPPGQ AGKCVPGYNV
MILDDNMQKL KARSLGNIVV KLPLPPGAFS GLWKNQEAFK HLYFEKFPGY YDTMDAGYMD
EEGYLYVMSR VDDVINVAGH RISAGAIEES VLSHGTVTDC AVVGKEDPLK GHVPLALCVL
KKDVNATEEQ VLEEIVKHVR QSIGPVAAFR NAVFVKQLPK TRSGKIPRST LSALVNGKPY
KVTPTIEDPS IFGHIEEVLK QAL
