SCOT2_HUMAN
ID SCOT2_HUMAN Reviewed; 517 AA.
AC Q9BYC2; B2RBB4; Q5QPK4; Q8NHR1; Q9H1I4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Succinyl-CoA:3-ketoacid coenzyme A transferase 2, 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;
DE Short=SCOT-t;
DE Flags: Precursor;
GN Name=OXCT2; ORFNames=FKSG25;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11756565; DOI=10.1093/molehr/8.1.16;
RA Tanaka H., Kohroki J., Iguchi N., Onishi M., Nishimune Y.;
RT "Cloning and characterization of a human orthologue of testis-specific
RT succinyl CoA:3-oxo acid CoA transferase (Scot-t) cDNA.";
RL Mol. Hum. Reprod. 8:16-23(2002).
RN [2]
RP SEQUENCE REVISION TO 352.
RA Kohroki J., Tanaka H.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang Y.-G., Gong L.;
RT "Cloning and characterization of FKSG25, a novel gene located on human
RT chromosome 1p34.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 {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:0000269|PubMed:11756565}.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11756565}.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase family.
CC {ECO:0000305}.
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DR EMBL; AB050193; BAB40810.2; -; mRNA.
DR EMBL; AY013700; AAG33922.1; -; mRNA.
DR EMBL; AK314586; BAG37161.1; -; mRNA.
DR EMBL; AL033527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS445.1; -.
DR RefSeq; NP_071403.1; NM_022120.1.
DR AlphaFoldDB; Q9BYC2; -.
DR SMR; Q9BYC2; -.
DR BioGRID; 122037; 41.
DR IntAct; Q9BYC2; 17.
DR STRING; 9606.ENSP00000361914; -.
DR iPTMnet; Q9BYC2; -.
DR PhosphoSitePlus; Q9BYC2; -.
DR BioMuta; OXCT2; -.
DR DMDM; 48428678; -.
DR EPD; Q9BYC2; -.
DR jPOST; Q9BYC2; -.
DR MassIVE; Q9BYC2; -.
DR MaxQB; Q9BYC2; -.
DR PaxDb; Q9BYC2; -.
DR PeptideAtlas; Q9BYC2; -.
DR PRIDE; Q9BYC2; -.
DR ProteomicsDB; 79610; -.
DR Antibodypedia; 31956; 95 antibodies from 24 providers.
DR DNASU; 64064; -.
DR Ensembl; ENST00000327582.5; ENSP00000361914.1; ENSG00000198754.5.
DR GeneID; 64064; -.
DR KEGG; hsa:64064; -.
DR MANE-Select; ENST00000327582.5; ENSP00000361914.1; NM_022120.2; NP_071403.1.
DR UCSC; uc001ceb.2; human.
DR CTD; 64064; -.
DR GeneCards; OXCT2; -.
DR HGNC; HGNC:18606; OXCT2.
DR HPA; ENSG00000198754; Tissue enriched (testis).
DR MIM; 610289; gene.
DR neXtProt; NX_Q9BYC2; -.
DR OpenTargets; ENSG00000198754; -.
DR PharmGKB; PA38360; -.
DR VEuPathDB; HostDB:ENSG00000198754; -.
DR eggNOG; KOG3822; Eukaryota.
DR GeneTree; ENSGT00390000009130; -.
DR HOGENOM; CLU_019942_1_3_1; -.
DR InParanoid; Q9BYC2; -.
DR OMA; MQVNQFG; -.
DR OrthoDB; 460209at2759; -.
DR PhylomeDB; Q9BYC2; -.
DR TreeFam; TF313991; -.
DR BRENDA; 2.8.3.5; 2681.
DR PathwayCommons; Q9BYC2; -.
DR Reactome; R-HSA-77108; Utilization of Ketone Bodies.
DR SignaLink; Q9BYC2; -.
DR UniPathway; UPA00929; UER00894.
DR BioGRID-ORCS; 64064; 43 hits in 1034 CRISPR screens.
DR GenomeRNAi; 64064; -.
DR Pharos; Q9BYC2; Tbio.
DR PRO; PR:Q9BYC2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BYC2; protein.
DR Bgee; ENSG00000198754; Expressed in right testis and 92 other tissues.
DR Genevisible; Q9BYC2; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0008260; F:3-oxoacid CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0008410; F:CoA-transferase activity; IBA:GO_Central.
DR GO; GO:0046950; P:cellular ketone body metabolic process; IBA:GO_Central.
DR GO; GO:0046952; P:ketone body catabolic process; IEA:InterPro.
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..517
FT /note="Succinyl-CoA:3-ketoacid coenzyme A transferase 2,
FT mitochondrial"
FT /id="PRO_0000002416"
FT ACT_SITE 341
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
FT VARIANT 250
FT /note="E -> D (in dbSNP:rs7542609)"
FT /id="VAR_059134"
FT VARIANT 285
FT /note="L -> R (in dbSNP:rs230321)"
FT /id="VAR_059135"
FT CONFLICT 38
FT /note="L -> P (in Ref. 4; BAG37161)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="E -> G (in Ref. 4; BAG37161)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="E -> G (in Ref. 4; BAG37161)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="E -> G (in Ref. 4; BAG37161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 56140 MW; 50EB94A755839B91 CRC64;
MAALRLLASV LGRGVPAGGS GLALSQGCAR CFATSPRLRA KFYADPVEMV KDISDGATVM
IGGFGLCGIP ENLIAALLRT RVKDLQVVSS NVGVEDFGLG LLLAARQVRR IVCSYVGENT
LCESQYLAGE LELELTPQGT LAERIRAGGA GVPAFYTPTG YGTLVQEGGA PIRYTPDGHL
ALMSQPREVR EFNGDHFLLE RAIRADFALV KGWKADRAGN VVFRRSARNF NVPMCKAADV
TAVEVEEIVE VGAFPPEDIH VPNIYVDRVI KGQKYEKRIE RLTILKEEDG DAGKEEDART
RIIRRAALEF EDGMYANLGI GIPLLASNFI SPSMTVHLHS ENGILGLGPF PTEDEVDADL
INAGKQTVTV LPGGCFFASD DSFAMIRGGH IQLTMLGAMQ VSKYGDLANW MIPGKKVKGM
GGAMDLVSSQ KTRVVVTMQH CTKDNTPKIM EKCTMPLTGK RCVDRIITEK AVFDVHRKKE
LTLRELWEGL TVDDIKKSTG CAFAVSPNLR PMQQVAP
