SCOT1_HUMAN
ID SCOT1_HUMAN Reviewed; 520 AA.
AC P55809; B2R5V2; B7Z528;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial {ECO:0000303|PubMed:10964512};
DE Short=SCOT {ECO:0000303|PubMed:10964512};
DE EC=2.8.3.5 {ECO:0000269|PubMed:10964512};
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Heart;
RX PubMed=8751852;
RA Kassovska-Bratinova S., Fukao T., Song X.-Q., Duncan A.M.V., Chen H.S.,
RA Robert M.-F., Perez-Cerda C., Ugarte M., Chartrand C., Vobecky S.,
RA Kondo N., Mitchell G.A.;
RT "Succinyl CoA:3-oxoacid CoA transferase (SCOT): human cDNA cloning, human
RT chromosomal mapping to 5p13, and mutation detection in a SCOT-deficient
RT patient.";
RL Am. J. Hum. Genet. 59:519-528(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SCOTD GLU-219; MET-221 AND
RP GLU-324, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=10964512; DOI=10.1006/geno.2000.6282;
RA Fukao T., Mitchell G.A., Song X.-Q., Nakamura H., Kassovska-Bratinova S.,
RA Orii K.E., Wraith J.E., Besley G., Wanders R.J.A., Niezen-Koning K.E.,
RA Berry G.T., Palmieri M., Kondo N.;
RT "Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human SCOT
RT gene, tertiary structural modeling of the human SCOT monomer, and
RT characterization of three pathogenic mutations.";
RL Genomics 68:144-151(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP PROTEIN SEQUENCE OF 40-50.
RC TISSUE=Colon;
RA Reymond M.A., Sanchez J.-C., Hughes G.J., Riese J., Tortola S.,
RA Peinado M.A., Kirchner T., Hohenberger W., Hochstrasser D.F.,
RA Kockerling F.;
RL Submitted (FEB-1997) to UniProtKB.
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=9380443; DOI=10.1203/00006450-199710000-00013;
RA Fukao T., Song X.Q., Mitchell G.A., Yamaguchi S., Sukegawa K., Orii T.,
RA Kondo N.;
RT "Enzymes of ketone body utilization in human tissues: protein and messenger
RT RNA levels of succinyl-coenzyme A (CoA):3-ketoacid CoA transferase and
RT mitochondrial and cytosolic acetoacetyl-CoA thiolases.";
RL Pediatr. Res. 42:498-502(1997).
RN [8]
RP PROTEIN SEQUENCE OF 84-104; 111-124; 147-173; 191-211; 391-418; 422-434 AND
RP 501-511, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP SUBUNIT.
RX PubMed=23420214; DOI=10.1007/s10545-013-9589-z;
RA Shafqat N., Kavanagh K.L., Sass J.O., Christensen E., Fukao T., Lee W.H.,
RA Oppermann U., Yue W.W.;
RT "A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA
RT transferase (SCOT) deficiency.";
RL J. Inherit. Metab. Dis. 36:983-987(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 40-520.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human 3-oxoacid CoA transferase 1.";
RL Submitted (AUG-2008) to the PDB data bank.
RN [15]
RP VARIANTS SCOTD GLU-133 AND PHE-456, AND VARIANT MET-58.
RX PubMed=9671268;
RX DOI=10.1002/(sici)1098-1004(1998)12:2<83::aid-humu2>3.0.co;2-p;
RA Song X.-Q., Fukao T., Watanabe H., Shintaku H., Hirayama K.,
RA Kassovska-Bratinova S., Kondo N., Mitchell G.A.;
RT "Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency: two pathogenic
RT mutations, V133E and C456F, in Japanese siblings.";
RL Hum. Mutat. 12:83-88(1998).
RN [16]
RP VARIANTS SCOTD VAL-215; ASN-226; PRO-327; PHE-404; PRO-405 AND CYS-468,
RP VARIANT MET-58, AND CHARACTERIZATION OF VARIANTS SCOTD VAL-215; ASN-226;
RP PRO-327; PHE-404; PRO-405 AND CYS-468.
RX PubMed=21296660; DOI=10.1016/j.bbadis.2011.01.015;
RA Fukao T., Sass J.O., Kursula P., Thimm E., Wendel U., Ficicioglu C.,
RA Monastiri K., Guffon N., Baric I., Zabot M.T., Kondo N.;
RT "Clinical and molecular characterization of five patients with succinyl-
RT CoA:3-ketoacid CoA transferase (SCOT) deficiency.";
RL Biochim. Biophys. Acta 1812:619-624(2011).
RN [17]
RP VARIANT SCOTD PHE-245.
RX PubMed=31073471; DOI=10.1055/s-0037-1604270;
RA Zheng D.J., Hooper M., Spencer-Manzon M., Pierce R.W.;
RT "A Case of Succinyl-CoA:3-Oxoacid CoA Transferase Deficiency Presenting
RT with Severe Acidosis in a 14-Month-Old Female: Evidence for Pathogenicity
RT of a Point Mutation in the OXCT1 Gene.";
RL J. Pediatr. Intensive Care 7:62-66(2018).
RN [18]
RP VARIANTS SCOTD 124-ARG--ASN-520 DEL; LYS-270; ALA-280 AND MET-437.
RX PubMed=33596448; DOI=10.1016/j.biochi.2021.02.003;
RA Gruenert S.C., Foster W., Schumann A., Lund A., Pontes C., Roloff S.,
RA Weinhold N., Yue W.W., AlAsmari A., Obaid O.A., Faqeih E.A., Stuebbe L.,
RA Yamamoto R., Gemperle-Britschgi C., Walter M., Spiekerkoetter U.,
RA Mackinnon S., Sass J.O.;
RT "Succinyl-CoA:3-oxoacid coenzyme A transferase (SCOT) deficiency: A rare
RT and potentially fatal metabolic disease.";
RL Biochimie 183:55-62(2021).
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 (PubMed:10964512). 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 carboxylate (3-oxo acid) 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:Q29551,
CC ECO:0000269|PubMed:10964512}.
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:0000269|PubMed:10964512};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24565;
CC Evidence={ECO:0000305|PubMed:10964512};
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:0000269|PubMed:10964512};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25481;
CC Evidence={ECO:0000269|PubMed:10964512};
CC -!- PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA
CC from succinyl-CoA: step 1/1. {ECO:0000305|PubMed:10964512}.
CC -!- SUBUNIT: Homodimer (PubMed:10964512, PubMed:23420214). Only one subunit
CC is competent to transfer the CoA moiety to the acceptor carboxylate (3-
CC oxo acid) (By similarity). {ECO:0000250|UniProtKB:Q29551,
CC ECO:0000269|PubMed:10964512, ECO:0000269|PubMed:23420214}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:B2GV06}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55809-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55809-2; Sequence=VSP_056310;
CC -!- TISSUE SPECIFICITY: Abundant in heart, followed in order by brain,
CC kidney, skeletal muscle, and lung, whereas in liver it is undetectable.
CC Expressed (at protein level) in all tissues (except in liver), most
CC abundant in myocardium, then brain, kidney, adrenal glands, skeletal
CC muscle and lung; also detectable in leukocytes and fibroblasts.
CC {ECO:0000269|PubMed:9380443}.
CC -!- DISEASE: Succinyl-CoA:3-oxoacid CoA transferase deficiency (SCOTD)
CC [MIM:245050]: A disorder of ketone body metabolism, characterized by
CC episodic ketoacidosis. Patients are usually asymptomatic between
CC episodes. {ECO:0000269|PubMed:10964512, ECO:0000269|PubMed:21296660,
CC ECO:0000269|PubMed:31073471, ECO:0000269|PubMed:33596448,
CC ECO:0000269|PubMed:9671268}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000305}.
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DR EMBL; U62961; AAB07366.1; -; mRNA.
DR EMBL; AB029576; BAB13733.1; -; Genomic_DNA.
DR EMBL; AK298352; BAH12764.1; -; mRNA.
DR EMBL; AK312327; BAG35249.1; -; mRNA.
DR EMBL; AK315902; BAH14273.1; -; mRNA.
DR EMBL; AC008817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC034222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009001; AAH09001.1; -; mRNA.
DR CCDS; CCDS3937.1; -. [P55809-1]
DR RefSeq; NP_000427.1; NM_000436.3. [P55809-1]
DR PDB; 3DLX; X-ray; 2.20 A; A/B/C/D=40-520.
DR PDBsum; 3DLX; -.
DR AlphaFoldDB; P55809; -.
DR SMR; P55809; -.
DR BioGRID; 111059; 113.
DR IntAct; P55809; 28.
DR MINT; P55809; -.
DR STRING; 9606.ENSP00000196371; -.
DR DrugBank; DB02731; Ethylmercurithiosalicylic acid.
DR DrugBank; DB00139; Succinic acid.
DR GlyGen; P55809; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55809; -.
DR PhosphoSitePlus; P55809; -.
DR SwissPalm; P55809; -.
DR BioMuta; OXCT1; -.
DR DMDM; 2492998; -.
DR UCD-2DPAGE; P55809; -.
DR EPD; P55809; -.
DR jPOST; P55809; -.
DR MassIVE; P55809; -.
DR MaxQB; P55809; -.
DR PaxDb; P55809; -.
DR PeptideAtlas; P55809; -.
DR PRIDE; P55809; -.
DR ProteomicsDB; 56871; -. [P55809-1]
DR ProteomicsDB; 6656; -.
DR Antibodypedia; 1558; 192 antibodies from 26 providers.
DR DNASU; 5019; -.
DR Ensembl; ENST00000196371.10; ENSP00000196371.5; ENSG00000083720.13. [P55809-1]
DR Ensembl; ENST00000510634.5; ENSP00000423144.1; ENSG00000083720.13. [P55809-2]
DR Ensembl; ENST00000512084.5; ENSP00000421143.1; ENSG00000083720.13. [P55809-2]
DR GeneID; 5019; -.
DR KEGG; hsa:5019; -.
DR MANE-Select; ENST00000196371.10; ENSP00000196371.5; NM_000436.4; NP_000427.1.
DR UCSC; uc003jmn.4; human. [P55809-1]
DR CTD; 5019; -.
DR DisGeNET; 5019; -.
DR GeneCards; OXCT1; -.
DR HGNC; HGNC:8527; OXCT1.
DR HPA; ENSG00000083720; Tissue enhanced (heart).
DR MalaCards; OXCT1; -.
DR MIM; 245050; phenotype.
DR MIM; 601424; gene.
DR neXtProt; NX_P55809; -.
DR OpenTargets; ENSG00000083720; -.
DR Orphanet; 832; Succinyl-CoA:3-oxoacid CoA transferase deficiency.
DR PharmGKB; PA32855; -.
DR VEuPathDB; HostDB:ENSG00000083720; -.
DR eggNOG; KOG3822; Eukaryota.
DR GeneTree; ENSGT00390000009130; -.
DR HOGENOM; CLU_019942_1_3_1; -.
DR InParanoid; P55809; -.
DR OMA; GTDYNKR; -.
DR OrthoDB; 1076134at2759; -.
DR PhylomeDB; P55809; -.
DR TreeFam; TF313991; -.
DR BioCyc; MetaCyc:HS01447-MON; -.
DR BRENDA; 2.8.3.5; 2681.
DR PathwayCommons; P55809; -.
DR Reactome; R-HSA-77108; Utilization of Ketone Bodies.
DR SignaLink; P55809; -.
DR UniPathway; UPA00929; UER00894.
DR BioGRID-ORCS; 5019; 15 hits in 1081 CRISPR screens.
DR ChiTaRS; OXCT1; human.
DR EvolutionaryTrace; P55809; -.
DR GeneWiki; OXCT1; -.
DR GenomeRNAi; 5019; -.
DR Pharos; P55809; Tbio.
DR PRO; PR:P55809; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P55809; protein.
DR Bgee; ENSG00000083720; Expressed in left ventricle myocardium and 203 other tissues.
DR ExpressionAtlas; P55809; baseline and differential.
DR Genevisible; P55809; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0008260; F:3-oxoacid CoA-transferase activity; IMP:UniProtKB.
DR GO; GO:0008410; F:CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0046952; P:ketone body catabolic process; IEA:Ensembl.
DR GO; GO:0042182; P:ketone catabolic process; IEA:Ensembl.
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; IEA:Ensembl.
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 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disease variant; Lipid metabolism; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 40..520
FT /note="Succinyl-CoA:3-ketoacid coenzyme A transferase 1,
FT mitochondrial"
FT /id="PRO_0000002413"
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:0007744|PubMed:20068231"
FT MOD_RES 185
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0K2"
FT MOD_RES 418
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0K2"
FT MOD_RES 421
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0K2"
FT MOD_RES 455
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0K2"
FT VAR_SEQ 1..397
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056310"
FT VARIANT 58
FT /note="T -> M (in dbSNP:rs75134564)"
FT /evidence="ECO:0000269|PubMed:21296660,
FT ECO:0000269|PubMed:9671268"
FT /id="VAR_000695"
FT VARIANT 124..520
FT /note="Missing (in SCOTD)"
FT /evidence="ECO:0000269|PubMed:33596448"
FT /id="VAR_085802"
FT VARIANT 133
FT /note="V -> E (in SCOTD; dbSNP:rs267606930)"
FT /evidence="ECO:0000269|PubMed:9671268"
FT /id="VAR_000696"
FT VARIANT 215
FT /note="A -> V (in SCOTD; partial loss of activity;
FT dbSNP:rs201752548)"
FT /evidence="ECO:0000269|PubMed:21296660"
FT /id="VAR_065564"
FT VARIANT 219
FT /note="G -> E (in SCOTD; dbSNP:rs121909302)"
FT /evidence="ECO:0000269|PubMed:10964512"
FT /id="VAR_010337"
FT VARIANT 221
FT /note="V -> M (in SCOTD; dbSNP:rs121909303)"
FT /evidence="ECO:0000269|PubMed:10964512"
FT /id="VAR_010338"
FT VARIANT 226
FT /note="S -> N (in SCOTD; loss of activity;
FT dbSNP:rs368841359)"
FT /evidence="ECO:0000269|PubMed:21296660"
FT /id="VAR_065565"
FT VARIANT 245
FT /note="V -> F (in SCOTD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31073471"
FT /id="VAR_085803"
FT VARIANT 270
FT /note="I -> K (in SCOTD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33596448"
FT /id="VAR_085804"
FT VARIANT 280
FT /note="E -> A (in SCOTD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33596448"
FT /id="VAR_085805"
FT VARIANT 324
FT /note="G -> E (in SCOTD; dbSNP:rs121909301)"
FT /evidence="ECO:0000269|PubMed:10964512"
FT /id="VAR_010339"
FT VARIANT 327
FT /note="L -> P (in SCOTD; partial loss of activity)"
FT /evidence="ECO:0000269|PubMed:21296660"
FT /id="VAR_065566"
FT VARIANT 404
FT /note="V -> F (in SCOTD; loss of activity)"
FT /evidence="ECO:0000269|PubMed:21296660"
FT /id="VAR_065567"
FT VARIANT 405
FT /note="S -> P (in SCOTD; loss of activity)"
FT /evidence="ECO:0000269|PubMed:21296660"
FT /id="VAR_065568"
FT VARIANT 437
FT /note="V -> M (in SCOTD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33596448"
FT /id="VAR_085806"
FT VARIANT 456
FT /note="C -> F (in SCOTD; dbSNP:rs121909300)"
FT /evidence="ECO:0000269|PubMed:9671268"
FT /id="VAR_000697"
FT VARIANT 468
FT /note="R -> C (in SCOTD; partial loss of activity; the
FT mutant retains half of the activity of the wild-type at 30
FT degrees; dbSNP:rs1327401976)"
FT /evidence="ECO:0000269|PubMed:21296660"
FT /id="VAR_065569"
FT CONFLICT 95
FT /note="D -> G (in Ref. 4; BAG35249)"
FT /evidence="ECO:0000305"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:3DLX"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 237..249
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 325..329
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:3DLX"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 382..390
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:3DLX"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 472..479
FT /evidence="ECO:0007829|PDB:3DLX"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 483..489
FT /evidence="ECO:0007829|PDB:3DLX"
FT HELIX 495..499
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:3DLX"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:3DLX"
SQ SEQUENCE 520 AA; 56158 MW; 54DA790FB8EDA546 CRC64;
MAALKLLSSG LRLCASARGS GATWYKGCVC SFSTSAHRHT KFYTDPVEAV KDIPDGATVL
VGGFGLCGIP ENLIDALLKT GVKGLTAVSN NAGVDNFGLG LLLRSKQIKR MVSSYVGENA
EFERQYLSGE LEVELTPQGT LAERIRAGGA GVPAFYTPTG YGTLVQEGGS PIKYNKDGSV
AIASKPREVR EFNGQHFILE EAITGDFALV KAWKADRAGN VIFRKSARNF NLPMCKAAET
TVVEVEEIVD IGAFAPEDIH IPQIYVHRLI KGEKYEKRIE RLSIRKEGDG EAKSAKPGDD
VRERIIKRAA LEFEDGMYAN LGIGIPLLAS NFISPNITVH LQSENGVLGL GPYPRQHEAD
ADLINAGKET VTILPGASFF SSDESFAMIR GGHVDLTMLG AMQVSKYGDL ANWMIPGKMV
KGMGGAMDLV SSAKTKVVVT MEHSAKGNAH KIMEKCTLPL TGKQCVNRII TEKAVFDVDK
KKGLTLIELW EGLTVDDVQK STGCDFAVSP KLMPMQQIAN