Q9BYC2 (SCOT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial
EC=2.8.3.5

Alternative name(s):
3-oxoacid CoA-transferase 2A
Testis-specific succinyl-CoA:3-oxoacid CoA-transferase
Short name=SCOT-t

Gene names

Name:	OXCT2
ORF Names:	FKSG25

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 Ref.1.
Tissue specificity	Testis specific. Ref.1
Sequence similarities	Belongs to the 3-oxoacid CoA-transferase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ketone body catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrion Inferred from direct assay Ref.1. Source: MGI motile cilium Inferred from direct assay Ref.1. Source: MGI
Molecular_function	3-oxoacid CoA-transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 39	39	Mitochondrion By similarity
	Chain	40 – 517	478	Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial		PRO_0000002416
Sites
	Active site	341	1	Acyl-thioester intermediate By similarity
Natural variations
	Natural variant	250	1	E → D. Corresponds to variant rs7542609 [ dbSNP | Ensembl ].		VAR_059134
	Natural variant	285	1	L → R. Corresponds to variant rs230321 [ dbSNP | Ensembl ].		VAR_059135
Experimental info
	Sequence conflict	38	1	L → P in BAG37161. Ref.4
	Sequence conflict	355	1	E → G in BAG37161. Ref.4
	Sequence conflict	480	1	E → G in BAG37161. Ref.4
	Sequence conflict	488	1	E → G in BAG37161. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9BYC2 [UniParc]. Last modified June 7, 2004. Version 2. Checksum: 50EB94A755839B91	FASTA	517	56,140
	10 20 30 40 50 60 MAALRLLASV LGRGVPAGGS GLALSQGCAR CFATSPRLRA KFYADPVEMV KDISDGATVM 70 80 90 100 110 120 IGGFGLCGIP ENLIAALLRT RVKDLQVVSS NVGVEDFGLG LLLAARQVRR IVCSYVGENT 130 140 150 160 170 180 LCESQYLAGE LELELTPQGT LAERIRAGGA GVPAFYTPTG YGTLVQEGGA PIRYTPDGHL 190 200 210 220 230 240 ALMSQPREVR EFNGDHFLLE RAIRADFALV KGWKADRAGN VVFRRSARNF NVPMCKAADV 250 260 270 280 290 300 TAVEVEEIVE VGAFPPEDIH VPNIYVDRVI KGQKYEKRIE RLTILKEEDG DAGKEEDART 310 320 330 340 350 360 RIIRRAALEF EDGMYANLGI GIPLLASNFI SPSMTVHLHS ENGILGLGPF PTEDEVDADL 370 380 390 400 410 420 INAGKQTVTV LPGGCFFASD DSFAMIRGGH IQLTMLGAMQ VSKYGDLANW MIPGKKVKGM 430 440 450 460 470 480 GGAMDLVSSQ KTRVVVTMQH CTKDNTPKIM EKCTMPLTGK RCVDRIITEK AVFDVHRKKE 490 500 510 LTLRELWEGL TVDDIKKSTG CAFAVSPNLR PMQQVAP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a human orthologue of testis-specific succinyl CoA:3-oxo acid CoA transferase (Scot-t) cDNA." Tanaka H., Kohroki J., Iguchi N., Onishi M., Nishimune Y. Mol. Hum. Reprod. 8:16-23(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	Kohroki J., Tanaka H. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 352.
[3]	"Cloning and characterization of FKSG25, a novel gene located on human chromosome 1p34." Wang Y.-G., Gong L. Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB050193 mRNA. Translation: BAB40810.2. AY013700 mRNA. Translation: AAG33922.1. AK314586 mRNA. Translation: BAG37161.1. AL033527 Genomic DNA. Translation: CAI19402.1.
IPI	IPI00307395.
RefSeq	NP_071403.1. NM_022120.1.
UniGene	Hs.472491.
3D structure databases
ProteinModelPortal	Q9BYC2.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000361914.
PTM databases
PhosphoSite	Q9BYC2.
Polymorphism databases
DMDM	48428678.
Proteomic databases
PaxDb	Q9BYC2.
PRIDE	Q9BYC2.
Protocols and materials databases
DNASU	64064.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000327582; ENSP00000361914; ENSG00000198754.
GeneID	64064.
KEGG	hsa:64064.
UCSC	uc001ceb.1. human.
Organism-specific databases
CTD	64064.
GeneCards	GC01M040235.
H-InvDB	HIX0199835.
HGNC	HGNC:18606. OXCT2.
HPA	HPA053950.
MIM	610289. gene.
neXtProt	NX_Q9BYC2.
PharmGKB	PA38360.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1788.
HOGENOM	HOG000221244.
HOVERGEN	HBG002310.
InParanoid	Q9BYC2.
KO	K01027.
OMA	HVPNIYV.
OrthoDB	EOG4S4PG7.
PhylomeDB	Q9BYC2.
Enzyme and pathway databases
UniPathway	UPA00929; UER00894.
Gene expression databases
Bgee	Q9BYC2.
CleanEx	HS_OXCT2.
Genevestigator	Q9BYC2.
GermOnline	ENSG00000198754. Homo sapiens.
Family and domain databases
InterPro	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]
PANTHER	PTHR13707. PTHR13707. 1 hit.
Pfam	PF01144. CoA_trans. 2 hits. [Graphical view]
PIRSF	PIRSF000858. SCOT-t. 1 hit.
SMART	SM00882. CoA_trans. 2 hits. [Graphical view]
TIGRFAMs	TIGR02429. pcaI_scoA_fam. 1 hit. TIGR02428. pcaJ_scoB_fam. 1 hit.
PROSITE	PS01273. COA_TRANSF_1. 1 hit. PS01274. COA_TRANSF_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00139. Succinic acid.
GenomeRNAi	64064.
NextBio	65830.
SOURCE	Search...

Entry information

Entry name

SCOT2_HUMAN

Accession

Primary (citable) accession number: Q9BYC2
Secondary accession number(s): B2RBB4 , Q5QPK4, Q8NHR1, Q9H1I4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.