位置:首页 > 蛋白库 > SCOT1_HUMAN
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025