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Protein

Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial

Gene

Oxct2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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). Probably play and important roles in the energy metabolism of spermatozoa.By similarity

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei342 – 34215-glutamyl coenzyme A thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. 3-oxoacid CoA-transferase activity Source: MGI

GO - Biological processi

  1. cellular ketone body metabolic process Source: MGI
  2. ketone body catabolic process Source: InterPro
  3. succinyl-CoA metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.8.3.5. 3474.
UniPathwayiUPA00929; UER00894.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial (EC:2.8.3.5)
Alternative name(s):
3-oxoacid CoA-transferase 2A
Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 1
Short name:
SCOT-t1
Gene namesi
Name:Oxct2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1891061. Oxct2a.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939MitochondrionBy similarityAdd
BLAST
Chaini40 – 520481Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrialPRO_0000366209Add
BLAST

Proteomic databases

PaxDbiQ9JJN4.
PRIDEiQ9JJN4.

Expressioni

Gene expression databases

BgeeiQ9JJN4.
GenevestigatoriQ9JJN4.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9JJN4.
SMRiQ9JJN4. Positions 42-516.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-oxoacid CoA-transferase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1788.
GeneTreeiENSGT00390000009130.
HOGENOMiHOG000221244.
HOVERGENiHBG002310.
InParanoidiQ9JJN4.
KOiK01027.
OMAiDITQGAR.
OrthoDBiEOG7XH6PR.
PhylomeDBiQ9JJN4.
TreeFamiTF313991.

Family and domain databases

InterProiIPR012792. 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]
PANTHERiPTHR13707. PTHR13707. 1 hit.
PfamiPF01144. CoA_trans. 2 hits.
[Graphical view]
PIRSFiPIRSF000858. SCOT-t. 1 hit.
SMARTiSM00882. CoA_trans. 2 hits.
[Graphical view]
TIGRFAMsiTIGR02429. pcaI_scoA_fam. 1 hit.
TIGR02428. pcaJ_scoB_fam. 1 hit.
PROSITEiPS01273. COA_TRANSF_1. 1 hit.
PS01274. COA_TRANSF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JJN4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAALRLLAWA LPRGVSALRP PPALPHRLIR RYVSDRSGSV HFYTDPVKAV
60 70 80 90 100
EGVKDGSTVM LGGFGLCGIP ENLIGALKTK GVKDLKIVSS NVGVDDFGLG
110 120 130 140 150
ILLASKQVRR VVCSYLGENA LCEKLYLAGE LELEMTPQGT LAERIRAGGT
160 170 180 190 200
GVPAFYTPTG YGTLVQEGGS PIRYAPDGHL ITLSEPREVR EFQGRFYLLE
210 220 230 240 250
HAIRADFALI KGWKADRSGN VIFRGSARNF NVPMCKAADI SVVEVEEIVD
260 270 280 290 300
VGTFAPEDIH VPNIYVDRVI KGPKFEKRIE RLTTRDSKPA PGSKDNDPSR
310 320 330 340 350
TRIIKRAALE FQDGMYANLG IGIPVLASNY ISPKMTVYLH SENGILGLGP
360 370 380 390 400
FPLKNEVDAD VINAGKQTVT VVPGGCFFAS DDSFAMIRGG HLQLTMLGAM
410 420 430 440 450
QVSQYGDLAN WMVPGKKVKG MGGAMDLVSS KKTRVVVTME HCTKTKQPKI
460 470 480 490 500
LKKCTMPLTG KRCVDLIITE KAVFEVNHSK GLTLVELWEG SSVDDIKATT
510 520
ACSFAVSPNL KPMQQIKLDA
Length:520
Mass (Da):56,473
Last modified:March 1, 2001 - v2
Checksum:i16BAE0F546AFB993
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022180 mRNA. Translation: BAA97654.2.
AB105454 Genomic DNA. Translation: BAC87737.1.
AK077075 mRNA. Translation: BAC36595.1.
AL606917 Genomic DNA. Translation: CAM46094.1.
BC137887 mRNA. Translation: AAI37888.1.
BC137888 mRNA. Translation: AAI37889.1.
CCDSiCCDS18617.1.
RefSeqiNP_071316.1. NM_022033.4.
UniGeneiMm.270287.

Genome annotation databases

EnsembliENSMUST00000102640; ENSMUSP00000099700; ENSMUSG00000076436.
GeneIDi64059.
KEGGimmu:64059.
UCSCiuc008uph.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022180 mRNA. Translation: BAA97654.2.
AB105454 Genomic DNA. Translation: BAC87737.1.
AK077075 mRNA. Translation: BAC36595.1.
AL606917 Genomic DNA. Translation: CAM46094.1.
BC137887 mRNA. Translation: AAI37888.1.
BC137888 mRNA. Translation: AAI37889.1.
CCDSiCCDS18617.1.
RefSeqiNP_071316.1. NM_022033.4.
UniGeneiMm.270287.

3D structure databases

ProteinModelPortaliQ9JJN4.
SMRiQ9JJN4. Positions 42-516.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ9JJN4.
PRIDEiQ9JJN4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102640; ENSMUSP00000099700; ENSMUSG00000076436.
GeneIDi64059.
KEGGimmu:64059.
UCSCiuc008uph.3. mouse.

Organism-specific databases

CTDi64059.
MGIiMGI:1891061. Oxct2a.

Phylogenomic databases

eggNOGiCOG1788.
GeneTreeiENSGT00390000009130.
HOGENOMiHOG000221244.
HOVERGENiHBG002310.
InParanoidiQ9JJN4.
KOiK01027.
OMAiDITQGAR.
OrthoDBiEOG7XH6PR.
PhylomeDBiQ9JJN4.
TreeFamiTF313991.

Enzyme and pathway databases

UniPathwayiUPA00929; UER00894.
BRENDAi2.8.3.5. 3474.

Miscellaneous databases

ChiTaRSiOxct1. mouse.
NextBioi319883.
PROiQ9JJN4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJN4.
GenevestigatoriQ9JJN4.

Family and domain databases

InterProiIPR012792. 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]
PANTHERiPTHR13707. PTHR13707. 1 hit.
PfamiPF01144. CoA_trans. 2 hits.
[Graphical view]
PIRSFiPIRSF000858. SCOT-t. 1 hit.
SMARTiSM00882. CoA_trans. 2 hits.
[Graphical view]
TIGRFAMsiTIGR02429. pcaI_scoA_fam. 1 hit.
TIGR02428. pcaJ_scoB_fam. 1 hit.
PROSITEiPS01273. COA_TRANSF_1. 1 hit.
PS01274. COA_TRANSF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of haploid germ cell-specific succinyl CoA:3-oxo acid CoA transferase (scot-t1 and scot-t2)."
    Tanaka H., Koga M., Yomogida K., Iguchi N., Nozaki M., Onishi M., Egydio de Carvalho C., Nakamura Y., Miyagawa Y., Takeyama M., Matsumiya K., Okuyama A., Nishimune Y.
    (In) Robaire B., Chemes H., Morales C.R. (eds.); Andrology in the 21th Century. Proceeding of the VIIth International Congress of Andrology, pp.157-161, Medimond Press, Montreal (2001)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Testis.
  2. "Gene structure and evolution of testicular haploid germ cell-specific genes, Oxct2a and Oxct2b."
    Onishi M., Yasunaga T., Tanaka H., Nishimune Y., Nozaki M.
    Genomics 83:647-657(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. "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.
    , 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: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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.

Entry informationi

Entry nameiSCO2A_MOUSE
AccessioniPrimary (citable) accession number: Q9JJN4
Secondary accession number(s): B9EHG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: March 1, 2001
Last modified: January 7, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.