SCO2A_MOUSE
ID SCO2A_MOUSE Reviewed; 520 AA.
AC Q9JJN4; B9EHG5;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial;
DE EC=2.8.3.5;
DE AltName: Full=3-oxoacid CoA-transferase 2A;
DE AltName: Full=Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 1;
DE Short=SCOT-t1;
DE Flags: Precursor;
GN Name=Oxct2a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RA Tanaka H., Koga M., Yomogida K., Iguchi N., Nozaki M., Onishi M.,
RA Egydio de Carvalho C., Nakamura Y., Miyagawa Y., Takeyama M., Matsumiya K.,
RA Okuyama A., Nishimune Y.;
RT "Isolation and characterization of haploid germ cell-specific succinyl
RT CoA:3-oxo acid CoA transferase (scot-t1 and scot-t2).";
RL (In) Robaire B., Chemes H., Morales C.R. (eds.);
RL Andrology in the 21th Century. Proceeding of the VIIth International
RL Congress of Andrology, pp.157-161, Medimond Press, Montreal (2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=15028287; DOI=10.1016/j.ygeno.2003.09.018;
RA Onishi M., Yasunaga T., Tanaka H., Nishimune Y., Nozaki M.;
RT "Gene structure and evolution of testicular haploid germ cell-specific
RT genes, Oxct2a and Oxct2b.";
RL Genomics 83:647-657(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Key enzyme for ketone body catabolism. Transfers the CoA
CC moiety from succinate to acetoacetate. Formation of the enzyme-CoA
CC intermediate proceeds via an unstable anhydride species formed between
CC the carboxylate groups of the enzyme and substrate (By similarity).
CC Probably play and important roles in the energy metabolism of
CC spermatozoa. {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU10034};
CC -!- PATHWAY: Ketone metabolism; succinyl-CoA degradation; acetoacetyl-CoA
CC from succinyl-CoA: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000305}.
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DR EMBL; AB022180; BAA97654.2; -; mRNA.
DR EMBL; AB105454; BAC87737.1; -; Genomic_DNA.
DR EMBL; AK077075; BAC36595.1; -; mRNA.
DR EMBL; AL606917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137887; AAI37888.1; -; mRNA.
DR EMBL; BC137888; AAI37889.1; -; mRNA.
DR CCDS; CCDS18617.1; -.
DR RefSeq; NP_071316.1; NM_022033.4.
DR AlphaFoldDB; Q9JJN4; -.
DR SMR; Q9JJN4; -.
DR IntAct; Q9JJN4; 2.
DR MINT; Q9JJN4; -.
DR STRING; 10090.ENSMUSP00000099700; -.
DR PhosphoSitePlus; Q9JJN4; -.
DR jPOST; Q9JJN4; -.
DR PaxDb; Q9JJN4; -.
DR PeptideAtlas; Q9JJN4; -.
DR PRIDE; Q9JJN4; -.
DR ProteomicsDB; 253425; -.
DR DNASU; 64059; -.
DR Ensembl; ENSMUST00000102640; ENSMUSP00000099700; ENSMUSG00000076436.
DR GeneID; 64059; -.
DR KEGG; mmu:64059; -.
DR UCSC; uc008uph.3; mouse.
DR CTD; 64059; -.
DR MGI; MGI:1891061; Oxct2a.
DR VEuPathDB; HostDB:ENSMUSG00000076436; -.
DR eggNOG; KOG3822; Eukaryota.
DR GeneTree; ENSGT00390000009130; -.
DR HOGENOM; CLU_019942_1_3_1; -.
DR InParanoid; Q9JJN4; -.
DR OMA; MQVNQFG; -.
DR OrthoDB; 460209at2759; -.
DR PhylomeDB; Q9JJN4; -.
DR TreeFam; TF313991; -.
DR BRENDA; 2.8.3.5; 3474.
DR UniPathway; UPA00929; UER00894.
DR BioGRID-ORCS; 64059; 0 hits in 52 CRISPR screens.
DR ChiTaRS; Oxct1; mouse.
DR PRO; PR:Q9JJN4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JJN4; protein.
DR Bgee; ENSMUSG00000076436; Expressed in testis and 18 other tissues.
DR Genevisible; Q9JJN4; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008260; F:3-oxoacid CoA-transferase activity; IDA:MGI.
DR GO; GO:0008410; F:CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0046950; P:cellular ketone body metabolic process; IDA:MGI.
DR GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; ISA:MGI.
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 2: Evidence at transcript level;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 40..520
FT /note="Succinyl-CoA:3-ketoacid coenzyme A transferase 2A,
FT mitochondrial"
FT /id="PRO_0000366209"
FT REGION 280..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 342
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
SQ SEQUENCE 520 AA; 56473 MW; 16BAE0F546AFB993 CRC64;
MAALRLLAWA LPRGVSALRP PPALPHRLIR RYVSDRSGSV HFYTDPVKAV EGVKDGSTVM
LGGFGLCGIP ENLIGALKTK GVKDLKIVSS NVGVDDFGLG ILLASKQVRR VVCSYLGENA
LCEKLYLAGE LELEMTPQGT LAERIRAGGT GVPAFYTPTG YGTLVQEGGS PIRYAPDGHL
ITLSEPREVR EFQGRFYLLE HAIRADFALI KGWKADRSGN VIFRGSARNF NVPMCKAADI
SVVEVEEIVD VGTFAPEDIH VPNIYVDRVI KGPKFEKRIE RLTTRDSKPA PGSKDNDPSR
TRIIKRAALE FQDGMYANLG IGIPVLASNY ISPKMTVYLH SENGILGLGP FPLKNEVDAD
VINAGKQTVT VVPGGCFFAS DDSFAMIRGG HLQLTMLGAM QVSQYGDLAN WMVPGKKVKG
MGGAMDLVSS KKTRVVVTME HCTKTKQPKI LKKCTMPLTG KRCVDLIITE KAVFEVNHSK
GLTLVELWEG SSVDDIKATT ACSFAVSPNL KPMQQIKLDA
