SCOT1_MOUSE
ID SCOT1_MOUSE Reviewed; 520 AA.
AC Q9D0K2; Q3TIW6; Q9CV92;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial;
DE Short=SCOT;
DE EC=2.8.3.5 {ECO:0000250|UniProtKB:Q29551};
DE AltName: Full=3-oxoacid CoA-transferase 1;
DE AltName: Full=Somatic-type succinyl-CoA:3-oxoacid CoA-transferase;
DE Short=SCOT-s;
DE AltName: Full=Succinyl-CoA:3-oxoacid CoA transferase;
DE Flags: Precursor;
GN Name=Oxct1; Synonyms=Oxct, Scot;
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].
RX PubMed=12534938; DOI=10.1046/j.1365-2605.2003.00389.x;
RA Tanaka H., Iguchi N., Miyagawa Y., Koga M., Kohroki J., Nishimune Y.;
RT "Differential expression of succinyl CoA transferase (SCOT) genes in
RT somatic and germline cells of the mouse testis.";
RL Int. J. Androl. 26:52-56(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Tongue;
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].
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 PROTEIN SEQUENCE OF 42-51; 84-104; 147-173; 191-211 AND 437-455, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-185; LYS-418; LYS-421 AND
RP LYS-455, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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).
CC -!- FUNCTION: Key enzyme for ketone body catabolism. Catalyzes the first,
CC rate-limiting step of ketone body utilization in extrahepatic tissues,
CC by transferring coenzyme A (CoA) from a donor thiolester species
CC (succinyl-CoA) to an acceptor carboxylate (acetoacetate), and produces
CC acetoacetyl-CoA. Acetoacetyl-CoA is further metabolized by acetoacetyl-
CC CoA thiolase into two acetyl-CoA molecules which enter the citric acid
CC cycle for energy production (By similarity). Forms a dimeric enzyme
CC where both of the subunits are able to form enzyme-CoA thiolester
CC intermediates, but only one subunit is competent to transfer the CoA
CC moiety to the acceptor (3-oxo acid) carboxylate and produce a new acyl-
CC CoA. Formation of the enzyme-CoA intermediate proceeds via an unstable
CC anhydride species formed between the carboxylate groups of the enzyme
CC and substrate (By similarity). {ECO:0000250|UniProtKB:P55809,
CC ECO:0000250|UniProtKB:Q29551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate;
CC Xref=Rhea:RHEA:24564, ChEBI:CHEBI:30031, ChEBI:CHEBI:35973,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:90726; EC=2.8.3.5;
CC Evidence={ECO:0000250|UniProtKB:P55809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24565;
CC Evidence={ECO:0000250|UniProtKB:P55809};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetate + succinyl-CoA = acetoacetyl-CoA + succinate;
CC Xref=Rhea:RHEA:25480, ChEBI:CHEBI:13705, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57292; EC=2.8.3.5;
CC Evidence={ECO:0000250|UniProtKB:P55809};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25481;
CC Evidence={ECO:0000250|UniProtKB:P55809};
CC -!- PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA
CC from succinyl-CoA: step 1/1. {ECO:0000250|UniProtKB:P55809}.
CC -!- SUBUNIT: Homodimer. Only one subunit is competent to transfer the CoA
CC moiety to the acceptor carboxylate (3-oxo acid).
CC {ECO:0000250|UniProtKB:Q29551}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:B2GV06}.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000305}.
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DR EMBL; AB085609; BAC05524.1; -; mRNA.
DR EMBL; AK009027; BAB26035.1; -; mRNA.
DR EMBL; AK011354; BAB27562.1; -; mRNA.
DR EMBL; AK151662; BAE30590.1; -; mRNA.
DR EMBL; AK167681; BAE39730.1; -; mRNA.
DR EMBL; BC003422; AAH03422.1; -; mRNA.
DR CCDS; CCDS27361.1; -.
DR PIR; PD0443; PD0443.
DR RefSeq; NP_077150.1; NM_024188.6.
DR AlphaFoldDB; Q9D0K2; -.
DR SMR; Q9D0K2; -.
DR BioGRID; 211895; 5.
DR IntAct; Q9D0K2; 6.
DR MINT; Q9D0K2; -.
DR STRING; 10090.ENSMUSP00000106318; -.
DR iPTMnet; Q9D0K2; -.
DR PhosphoSitePlus; Q9D0K2; -.
DR SwissPalm; Q9D0K2; -.
DR REPRODUCTION-2DPAGE; IPI00132653; -.
DR EPD; Q9D0K2; -.
DR jPOST; Q9D0K2; -.
DR MaxQB; Q9D0K2; -.
DR PaxDb; Q9D0K2; -.
DR PeptideAtlas; Q9D0K2; -.
DR PRIDE; Q9D0K2; -.
DR ProteomicsDB; 256713; -.
DR Antibodypedia; 1558; 192 antibodies from 26 providers.
DR DNASU; 67041; -.
DR Ensembl; ENSMUST00000110690; ENSMUSP00000106318; ENSMUSG00000022186.
DR GeneID; 67041; -.
DR KEGG; mmu:67041; -.
DR UCSC; uc007vck.2; mouse.
DR CTD; 5019; -.
DR MGI; MGI:1914291; Oxct1.
DR VEuPathDB; HostDB:ENSMUSG00000022186; -.
DR eggNOG; KOG3822; Eukaryota.
DR GeneTree; ENSGT00390000009130; -.
DR InParanoid; Q9D0K2; -.
DR OMA; GTDYNKR; -.
DR OrthoDB; 460209at2759; -.
DR PhylomeDB; Q9D0K2; -.
DR TreeFam; TF313991; -.
DR BRENDA; 2.8.3.5; 3474.
DR Reactome; R-MMU-77108; Utilization of Ketone Bodies.
DR UniPathway; UPA00929; UER00894.
DR BioGRID-ORCS; 67041; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Oxct1; mouse.
DR PRO; PR:Q9D0K2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D0K2; protein.
DR Bgee; ENSMUSG00000022186; Expressed in adult mammalian kidney and 253 other tissues.
DR ExpressionAtlas; Q9D0K2; baseline and differential.
DR Genevisible; Q9D0K2; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008260; F:3-oxoacid CoA-transferase activity; IDA:MGI.
DR GO; GO:0008410; F:CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0046950; P:cellular ketone body metabolic process; IDA:MGI.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0046952; P:ketone body catabolic process; IMP:MGI.
DR GO; GO:0042182; P:ketone catabolic process; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR InterPro; IPR012792; 3-oxoacid_CoA-transf_A.
DR InterPro; IPR012791; 3-oxoacid_CoA-transf_B.
DR InterPro; IPR014388; 3-oxoacid_CoA-transferase.
DR InterPro; IPR004165; CoA_trans_fam_I.
DR InterPro; IPR004164; CoA_transf_AS.
DR InterPro; IPR004163; CoA_transf_BS.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR13707; PTHR13707; 1.
DR Pfam; PF01144; CoA_trans; 2.
DR PIRSF; PIRSF000858; SCOT-t; 1.
DR SMART; SM00882; CoA_trans; 2.
DR SUPFAM; SSF100950; SSF100950; 2.
DR TIGRFAMs; TIGR02429; pcaI_scoA_fam; 1.
DR TIGRFAMs; TIGR02428; pcaJ_scoB_fam; 1.
DR PROSITE; PS01273; COA_TRANSF_1; 1.
DR PROSITE; PS01274; COA_TRANSF_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lipid metabolism; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 40..520
FT /note="Succinyl-CoA:3-ketoacid coenzyme A transferase 1,
FT mitochondrial"
FT /id="PRO_0000002414"
FT ACT_SITE 344
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55809"
FT MOD_RES 185
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 418
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 421
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 455
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 478
FT /note="V -> G (in Ref. 2; BAB27562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 55989 MW; 6C8CB60C756FA6A9 CRC64;
MAALKLLSSG LRLGASARSS RGALHKGCVC YFSVSTRHHT KFYTDPVEAV KDIPNGATLL
VGGFGLCGIP ENLIGALLKT GVKDLTAVSN NAGVDNFGLG LLLRSKQIKR MISSYVGENA
EFERQFLSGE LEVELTPQGT LAERIRAGGA GVPAFYTSTG YGTLVQEGGS PIKYNKDGSV
AIASKPREVR EFNGQHFILE EAITGDFALV KAWKADRAGN VIFRKSARNF NLPMCKAAGT
TVVEVEEIVD IGSFAPEDIH IPKIYVHRLI KGEKYEKRIE RLSLRKEGDG KGKSGKPGGD
VRERIIKRAA LEFEDGMYAN LGIGIPLLAS NFISPNMTVH LQSENGVLGL GPYPLKDEAD
ADLINAGKET VTVLPGASFF SSDESFAMIR GGHVNLTMLG AMQVSKYGDL ANWMIPGKMV
KGMGGAMDLV SSSKTKVVVT MEHSAKGNAH KIMEKCTLPL TGKQCVNRII TEKGVFDVDK
KNGLTLIELW EGLTVDDIKK STGCDFAVSP NLMPMQQIST
