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Q9D0K2 (SCOT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 By similarity.

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 By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the 3-oxoacid CoA-transferase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionTransferase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadipose tissue development

Inferred from electronic annotation. Source: Compara

brain development

Inferred from electronic annotation. Source: Compara

cellular response to acid

Inferred from electronic annotation. Source: Compara

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Compara

heart development

Inferred from electronic annotation. Source: Compara

ketone body catabolic process

Inferred from mutant phenotype PubMed 21209089. Source: MGI

ketone catabolic process

Inferred from mutant phenotype PubMed 21209089. Source: MGI

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Compara

response to activity

Inferred from electronic annotation. Source: Compara

response to drug

Inferred from electronic annotation. Source: Compara

response to ethanol

Inferred from electronic annotation. Source: Compara

response to hormone stimulus

Inferred from electronic annotation. Source: Compara

response to nutrient

Inferred from electronic annotation. Source: Compara

response to starvation

Inferred from electronic annotation. Source: Compara

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

   Molecular_function3-oxoacid CoA-transferase activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion By similarity
Chain40 – 520481Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
PRO_0000002414

Sites

Active site3441Acyl-thioester intermediate By similarity

Amino acid modifications

Modified residue1701Phosphoserine By similarity

Experimental info

Sequence conflict4781V → G in BAB27562. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9D0K2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 6C8CB60C756FA6A9

FASTA52055,989
        10         20         30         40         50         60 
MAALKLLSSG LRLGASARSS RGALHKGCVC YFSVSTRHHT KFYTDPVEAV KDIPNGATLL 

        70         80         90        100        110        120 
VGGFGLCGIP ENLIGALLKT GVKDLTAVSN NAGVDNFGLG LLLRSKQIKR MISSYVGENA 

       130        140        150        160        170        180 
EFERQFLSGE LEVELTPQGT LAERIRAGGA GVPAFYTSTG YGTLVQEGGS PIKYNKDGSV 

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

       250        260        270        280        290        300 
TVVEVEEIVD IGSFAPEDIH IPKIYVHRLI KGEKYEKRIE RLSLRKEGDG KGKSGKPGGD 

       310        320        330        340        350        360 
VRERIIKRAA LEFEDGMYAN LGIGIPLLAS NFISPNMTVH LQSENGVLGL GPYPLKDEAD 

       370        380        390        400        410        420 
ADLINAGKET VTVLPGASFF SSDESFAMIR GGHVNLTMLG AMQVSKYGDL ANWMIPGKMV 

       430        440        450        460        470        480 
KGMGGAMDLV SSSKTKVVVT MEHSAKGNAH KIMEKCTLPL TGKQCVNRII TEKGVFDVDK 

       490        500        510        520 
KNGLTLIELW EGLTVDDIKK STGCDFAVSP NLMPMQQIST

« Hide

References

« Hide 'large scale' references
[1]"Differential expression of succinyl CoA transferase (SCOT) genes in somatic and germline cells of the mouse testis."
Tanaka H., Iguchi N., Miyagawa Y., Koga M., Kohroki J., Nishimune Y.
Int. J. Androl. 26:52-56(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow, Embryo and Tongue.
[3]"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].
[4]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 42-51; 84-104; 147-173; 191-211 AND 437-455, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB085609 mRNA. Translation: BAC05524.1.
AK009027 mRNA. Translation: BAB26035.1.
AK011354 mRNA. Translation: BAB27562.1.
AK151662 mRNA. Translation: BAE30590.1.
AK167681 mRNA. Translation: BAE39730.1.
BC003422 mRNA. Translation: AAH03422.1.
IPIIPI00132653.
PIRPD0443.
RefSeqNP_077150.1. NM_024188.6.
UniGeneMm.13445.

3D structure databases

ProteinModelPortalQ9D0K2.
SMRQ9D0K2. Positions 40-519.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9D0K2. 3 interactions.

PTM databases

PhosphoSiteQ9D0K2.

2D gel databases

REPRODUCTION-2DPAGEIPI00132653.

Proteomic databases

PaxDbQ9D0K2.
PRIDEQ9D0K2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000110690; ENSMUSP00000106318; ENSMUSG00000022186.
GeneID67041.
KEGGmmu:67041.
UCSCuc007vck.2. mouse.

Organism-specific databases

CTD5019.
MGIMGI:1914291. Oxct1.

Phylogenomic databases

eggNOGCOG1788.
GeneTreeENSGT00390000009130.
HOGENOMHOG000221244.
HOVERGENHBG002310.
InParanoidQ9D0K2.
KOK01027.
OMAASDLKVM.
OrthoDBEOG4GMTWV.

Enzyme and pathway databases

UniPathwayUPA00929; UER00894.

Gene expression databases

ArrayExpressQ9D0K2.
BgeeQ9D0K2.
CleanExMM_OXCT1.
GenevestigatorQ9D0K2.
GermOnlineENSMUSG00000022186. Mus musculus.

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

NextBio323396.
SOURCESearch...

Entry information

Entry nameSCOT1_MOUSE
AccessionPrimary (citable) accession number: Q9D0K2
Secondary accession number(s): Q3TIW6, Q9CV92
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2001
Last modified: April 3, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents