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Q9JJN4

- SCO2A_MOUSE

UniProt

Q9JJN4 - SCO2A_MOUSE

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Protein

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

Gene
Oxct2a
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei342 – 34215-glutamyl coenzyme A thioester intermediate By similarity

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 – 3939Mitochondrion By 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.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1788.
GeneTreeiENSGT00390000009130.
HOGENOMiHOG000221244.
HOVERGENiHBG002310.
InParanoidiQ9JJN4.
KOiK01027.
OMAiIRERMAQ.
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

MAALRLLAWA LPRGVSALRP PPALPHRLIR RYVSDRSGSV HFYTDPVKAV    50
EGVKDGSTVM LGGFGLCGIP ENLIGALKTK GVKDLKIVSS NVGVDDFGLG 100
ILLASKQVRR VVCSYLGENA LCEKLYLAGE LELEMTPQGT LAERIRAGGT 150
GVPAFYTPTG YGTLVQEGGS PIRYAPDGHL ITLSEPREVR EFQGRFYLLE 200
HAIRADFALI KGWKADRSGN VIFRGSARNF NVPMCKAADI SVVEVEEIVD 250
VGTFAPEDIH VPNIYVDRVI KGPKFEKRIE RLTTRDSKPA PGSKDNDPSR 300
TRIIKRAALE FQDGMYANLG IGIPVLASNY ISPKMTVYLH SENGILGLGP 350
FPLKNEVDAD VINAGKQTVT VVPGGCFFAS DDSFAMIRGG HLQLTMLGAM 400
QVSQYGDLAN WMVPGKKVKG MGGAMDLVSS KKTRVVVTME HCTKTKQPKI 450
LKKCTMPLTG KRCVDLIITE KAVFEVNHSK GLTLVELWEG SSVDDIKATT 500
ACSFAVSPNL KPMQQIKLDA 520
Length:520
Mass (Da):56,473
Last modified:March 1, 2001 - v2
Checksum:i16BAE0F546AFB993
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18617.1.
RefSeqi NP_071316.1. NM_022033.4.
UniGenei Mm.270287.

3D structure databases

ProteinModelPortali Q9JJN4.
SMRi Q9JJN4. Positions 42-516.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q9JJN4.
PRIDEi Q9JJN4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102640 ; ENSMUSP00000099700 ; ENSMUSG00000076436 .
GeneIDi 64059.
KEGGi mmu:64059.
UCSCi uc008uph.3. mouse.

Organism-specific databases

CTDi 64059.
MGIi MGI:1891061. Oxct2a.

Phylogenomic databases

eggNOGi COG1788.
GeneTreei ENSGT00390000009130.
HOGENOMi HOG000221244.
HOVERGENi HBG002310.
InParanoidi Q9JJN4.
KOi K01027.
OMAi IRERMAQ.
OrthoDBi EOG7XH6PR.
PhylomeDBi Q9JJN4.
TreeFami TF313991.

Enzyme and pathway databases

UniPathwayi UPA00929 ; UER00894 .
BRENDAi 2.8.3.5. 3474.

Miscellaneous databases

NextBioi 319883.
PROi Q9JJN4.
SOURCEi Search...

Gene expression databases

Bgeei Q9JJN4.
Genevestigatori Q9JJN4.

Family and domain databases

InterProi IPR012792. 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 ]
PANTHERi PTHR13707. PTHR13707. 1 hit.
Pfami PF01144. CoA_trans. 2 hits.
[Graphical view ]
PIRSFi PIRSF000858. SCOT-t. 1 hit.
SMARTi SM00882. CoA_trans. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR02429. pcaI_scoA_fam. 1 hit.
TIGR02428. pcaJ_scoB_fam. 1 hit.
PROSITEi PS01273. COA_TRANSF_1. 1 hit.
PS01274. COA_TRANSF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 97 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

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