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P55809 (SCOT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial

EC=2.8.3.5
Alternative name(s):
3-oxoacid CoA-transferase 1
Somatic-type succinyl-CoA:3-oxoacid CoA-transferase
Short name=SCOT-s
Gene names
Name:OXCT1
Synonyms:OXCT, SCOT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.

Catalytic activity

Succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA.

Pathway

Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA from succinyl-CoA: step 1/1.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion matrix.

Tissue specificity

Abundant in heart, followed in order by kidney, brain, and muscle, whereas in liver it is undetectable; also detectable in leukocytes and fibroblasts.

Involvement in disease

Succinyl-CoA-3-ketoacid-CoA transferase deficiency (SCOTD) [MIM:245050]: A disorder of ketone body metabolism, characterized by episodic ketoacidosis. Patients are usually asymptomatic between episodes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.11 Ref.12

Sequence similarities

Belongs to the 3-oxoacid CoA-transferase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   Molecular functionTransferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadipose tissue development

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

cellular ketone body metabolic process

Inferred from mutant phenotype Ref.11. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular response to acid

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

ketone body catabolic process

Traceable author statement. Source: Reactome

ketone catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

response to activity

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to hormone

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay PubMed 11756565. Source: UniProtKB

   Molecular_function3-oxoacid CoA-transferase activity

Inferred from mutant phenotype Ref.2Ref.1. Source: UniProtKB

protein homodimerization activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion Ref.5
Chain40 – 520481Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
PRO_0000002413

Sites

Active site34415-glutamyl coenzyme A thioester intermediate By similarity

Amino acid modifications

Modified residue1701Phosphoserine Ref.8
Modified residue1851N6-succinyllysine By similarity
Modified residue4181N6-succinyllysine By similarity
Modified residue4211N6-succinyllysine By similarity
Modified residue4551N6-succinyllysine By similarity

Natural variations

Natural variant581T → M. Ref.11 Ref.12
Corresponds to variant rs75134564 [ dbSNP | Ensembl ].
VAR_000695
Natural variant1331V → E in SCOTD. Ref.11
VAR_000696
Natural variant2151A → V in SCOTD; partial loss of activity. Ref.12
Corresponds to variant rs201752548 [ dbSNP | Ensembl ].
VAR_065564
Natural variant2191G → E in SCOTD. Ref.2
VAR_010337
Natural variant2211V → M in SCOTD. Ref.2
VAR_010338
Natural variant2261S → N in SCOTD; loss of activity. Ref.12
VAR_065565
Natural variant3241G → E in SCOTD. Ref.2
VAR_010339
Natural variant3271L → P in SCOTD; partial loss of activity. Ref.12
VAR_065566
Natural variant4041V → F in SCOTD; loss of activity. Ref.12
VAR_065567
Natural variant4051S → P in SCOTD; loss of activity. Ref.12
VAR_065568
Natural variant4561C → F in SCOTD. Ref.11
VAR_000697
Natural variant4681R → C in SCOTD; partial loss of activity; the mutant retains half of the activity of the wild-type at 30 degrees. Ref.12
VAR_065569

Experimental info

Sequence conflict951D → G in BAG35249. Ref.3

Secondary structure

................................................................................................... 520
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55809 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 54DA790FB8EDA546

FASTA52056,158
        10         20         30         40         50         60 
MAALKLLSSG LRLCASARGS GATWYKGCVC SFSTSAHRHT KFYTDPVEAV KDIPDGATVL 

        70         80         90        100        110        120 
VGGFGLCGIP ENLIDALLKT GVKGLTAVSN NAGVDNFGLG LLLRSKQIKR MVSSYVGENA 

       130        140        150        160        170        180 
EFERQYLSGE LEVELTPQGT LAERIRAGGA GVPAFYTPTG YGTLVQEGGS PIKYNKDGSV 

       190        200        210        220        230        240 
AIASKPREVR EFNGQHFILE EAITGDFALV KAWKADRAGN VIFRKSARNF NLPMCKAAET 

       250        260        270        280        290        300 
TVVEVEEIVD IGAFAPEDIH IPQIYVHRLI KGEKYEKRIE RLSIRKEGDG EAKSAKPGDD 

       310        320        330        340        350        360 
VRERIIKRAA LEFEDGMYAN LGIGIPLLAS NFISPNITVH LQSENGVLGL GPYPRQHEAD 

       370        380        390        400        410        420 
ADLINAGKET VTILPGASFF SSDESFAMIR GGHVDLTMLG AMQVSKYGDL ANWMIPGKMV 

       430        440        450        460        470        480 
KGMGGAMDLV SSAKTKVVVT MEHSAKGNAH KIMEKCTLPL TGKQCVNRII TEKAVFDVDK 

       490        500        510        520 
KKGLTLIELW EGLTVDDVQK STGCDFAVSP KLMPMQQIAN 

« Hide

References

« Hide 'large scale' references
[1]"Succinyl CoA:3-oxoacid CoA transferase (SCOT): human cDNA cloning, human chromosomal mapping to 5p13, and mutation detection in a SCOT-deficient patient."
Kassovska-Bratinova S., Fukao T., Song X.-Q., Duncan A.M.V., Chen H.S., Robert M.-F., Perez-Cerda C., Ugarte M., Chartrand C., Vobecky S., Kondo N., Mitchell G.A.
Am. J. Hum. Genet. 59:519-528(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Heart.
[2]"Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human SCOT gene, tertiary structural modeling of the human SCOT monomer, and characterization of three pathogenic mutations."
Fukao T., Mitchell G.A., Song X.-Q., Nakamura H., Kassovska-Bratinova S., Orii K.E., Wraith J.E., Besley G., Wanders R.J.A., Niezen-Koning K.E., Berry G.T., Palmieri M., Kondo N.
Genomics 68:144-151(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SCOTD GLU-219; MET-221 AND GLU-324.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]Reymond M.A., Sanchez J.-C., Hughes G.J., Riese J., Tortola S., Peinado M.A., Kirchner T., Hohenberger W., Hochstrasser D.F., Kockerling F.
Submitted (FEB-1997) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 40-50.
Tissue: Colon.
[6]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 84-104; 111-124; 147-173; 191-211; 391-418; 422-434 AND 501-511, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Crystal structure of human 3-oxoacid CoA transferase 1."
Structural genomics consortium (SGC)
Submitted (AUG-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 40-520.
[11]"Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency: two pathogenic mutations, V133E and C456F, in Japanese siblings."
Song X.-Q., Fukao T., Watanabe H., Shintaku H., Hirayama K., Kassovska-Bratinova S., Kondo N., Mitchell G.A.
Hum. Mutat. 12:83-88(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SCOTD GLU-133 AND PHE-456, VARIANT MET-58.
[12]"Clinical and molecular characterization of five patients with succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency."
Fukao T., Sass J.O., Kursula P., Thimm E., Wendel U., Ficicioglu C., Monastiri K., Guffon N., Baric I., Zabot M.T., Kondo N.
Biochim. Biophys. Acta 1812:619-624(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SCOTD VAL-215; ASN-226; PRO-327; PHE-404; PRO-405 AND CYS-468, VARIANT MET-58, CHARACTERIZATION OF VARIANTS SCOTD VAL-215; ASN-226; PRO-327; PHE-404; PRO-405 AND CYS-468.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U62961 mRNA. Translation: AAB07366.1.
AB029576 Genomic DNA. Translation: BAB13733.1.
AK312327 mRNA. Translation: BAG35249.1.
BC009001 mRNA. Translation: AAH09001.1.
RefSeqNP_000427.1. NM_000436.3.
UniGeneHs.278277.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DLXX-ray2.20A/B/C/D40-520[»]
ProteinModelPortalP55809.
SMRP55809. Positions 40-519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111059. 42 interactions.
IntActP55809. 3 interactions.
STRING9606.ENSP00000196371.

Chemistry

DrugBankDB00139. Succinic acid.

PTM databases

PhosphoSiteP55809.

Polymorphism databases

DMDM2492998.

2D gel databases

UCD-2DPAGEP55809.

Proteomic databases

PaxDbP55809.
PeptideAtlasP55809.
PRIDEP55809.

Protocols and materials databases

DNASU5019.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000196371; ENSP00000196371; ENSG00000083720.
GeneID5019.
KEGGhsa:5019.
UCSCuc003jmn.3. human.

Organism-specific databases

CTD5019.
GeneCardsGC05M041765.
HGNCHGNC:8527. OXCT1.
HPAHPA012047.
MIM245050. phenotype.
601424. gene.
neXtProtNX_P55809.
Orphanet832. Succinyl-CoA:3-ketoacid CoA transferase deficiency.
PharmGKBPA32855.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1788.
HOGENOMHOG000221244.
HOVERGENHBG002310.
InParanoidP55809.
KOK01027.
OMAKGTEDAD.
OrthoDBEOG7XH6PR.
PhylomeDBP55809.
TreeFamTF313991.

Enzyme and pathway databases

BioCycMetaCyc:HS01447-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00929; UER00894.

Gene expression databases

ArrayExpressP55809.
BgeeP55809.
CleanExHS_OXCT1.
GenevestigatorP55809.

Family and domain databases

InterProIPR012792. 3-oxoacid_CoA-transf_A.
IPR012791. 3-oxoacid_CoA-transf_B.
IPR014388. 3-oxoacid_CoA-transferase.
IPR004165. CoA_trans_fam_I.
IPR004164. CoA_transf_AS.
IPR004163. CoA_transf_BS.
[Graphical view]
PANTHERPTHR13707. PTHR13707. 1 hit.
PfamPF01144. CoA_trans. 2 hits.
[Graphical view]
PIRSFPIRSF000858. SCOT-t. 1 hit.
SMARTSM00882. CoA_trans. 2 hits.
[Graphical view]
TIGRFAMsTIGR02429. pcaI_scoA_fam. 1 hit.
TIGR02428. pcaJ_scoB_fam. 1 hit.
PROSITEPS01273. COA_TRANSF_1. 1 hit.
PS01274. COA_TRANSF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP55809.
GeneWikiOXCT1.
GenomeRNAi5019.
NextBio19324.
PROP55809.
SOURCESearch...

Entry information

Entry nameSCOT1_HUMAN
AccessionPrimary (citable) accession number: P55809
Secondary accession number(s): B2R5V2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM