Q9UKG9 (OCTC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxisomal carnitine O-octanoyltransferase
Short name=COT
EC=2.3.1.137

Gene names

Name:	CROT
Synonyms:	COT

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	612 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate. Converts the end product of pristanic acid beta oxidation, 4,8-dimethylnonanoyl-CoA, to its corresponding carnitine ester. Ref.1
Catalytic activity	Octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine.
Pathway	Lipid metabolism; fatty acid beta-oxidation.
Subunit structure	Monomer Probable. Ref.1
Subcellular location	Peroxisome Potential.
Sequence similarities	Belongs to the carnitine/choline acetyltransferase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism Transport
Cellular component	Peroxisome
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation using acyl-CoA oxidase Traceable author statement. Source: Reactome generation of precursor metabolites and energy Inferred from direct assay Ref.1. Source: UniProtKB medium-chain fatty acid metabolic process Inferred from direct assay Ref.1. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	peroxisomal matrix Traceable author statement. Source: Reactome
Molecular_function	carnitine O-octanoyltransferase activity Inferred from direct assay Ref.1PubMed 21619872. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UKG9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UKG9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     81-87: LEEWWLN → VFVVIIE
     88-612: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 612	612	Peroxisomal carnitine O-octanoyltransferase		PRO_0000210169
Regions
	Region	405 – 417	13	Coenzyme A binding By similarity
	Motif	610 – 612	3	Microbody targeting signal Potential
	Compositional bias	534 – 537	4	Poly-Gly
Sites
	Active site	327	1	Proton acceptor By similarity
	Binding site	439	1	Carnitine By similarity
	Binding site	442	1	Coenzyme A By similarity
	Binding site	452	1	Carnitine By similarity
	Binding site	505	1	Carnitine By similarity
Amino acid modifications
	Modified residue	495	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	81 – 87	7	LEEWWLN → VFVVIIE in isoform 2.		VSP_045213
	Alternative sequence	88 – 612	525	Missing in isoform 2.		VSP_045214
	Natural variant	94	1	R → H. Corresponds to variant rs3827653 [ dbSNP | Ensembl ].		VAR_048612
	Natural variant	474	1	V → L. Corresponds to variant rs7785206 [ dbSNP | Ensembl ].		VAR_048613
Experimental info
	Sequence conflict	144	1	V → L in AAF03234. Ref.1
	Sequence conflict	168	1	V → G in AAD41654. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 7, 2004. Version 2. Checksum: BFC4E0A09B191038	FASTA	612	70,178
	10 20 30 40 50 60 MENQLAKSTE ERTFQYQDSL PSLPVPSLEE SLKKYLESVK PFANQEEYKK TEEIVQKFQS 70 80 90 100 110 120 GIGEKLHQKL LERAKGKRNW LEEWWLNVAY LDVRIPSQLN VNFAGPAAHF EHYWPPKEGT 130 140 150 160 170 180 QLERGSITLW HNLNYWQLLR KEKVPVHKVG NTPLDMNQFR MLFSTCKVPG ITRDSIMNYF 190 200 210 220 230 240 RTESEGRSPN HIVVLCRGRA FVFDVIHEGC LVTPPELLRQ LTYIHKKCHS EPDGPGIAAL 250 260 270 280 290 300 TSEERTRWAK AREYLIGLDP ENLALLEKIQ SSLLVYSMED SSPHVTPEDY SEIIAAILIG 310 320 330 340 350 360 DPTVRWGDKS YNLISFSNGV FGCNCDHAPF DAMIMVNISY YVDEKIFQNE GRWKGSEKVR 370 380 390 400 410 420 DIPLPEELIF IVDEKVLNDI NQAKAQYLRE ASDLQIAAYA FTSFGKKLTK NKMLHPDTFI 430 440 450 460 470 480 QLALQLAYYR LHGHPGCCYE TAMTRHFYHG RTETMRSCTV EAVRWCQSMQ DPSVNLRERQ 490 500 510 520 530 540 QKMLQAFAKH NKMMKDCSAG KGFDRHLLGL LLIAKEEGLP VPELFTDPLF SKSGGGGNFV 550 560 570 580 590 600 LSTSLVGYLR VQGVVVPMVH NGYGFFYHIR DDRFVVACSA WKSCPETDAE KLVQLTFCAF 610 HDMIQLMNST HL
	Isoform 2 [UniParc]. Checksum: 9806EC31C962CE35	FASTA	87	10,214
	10 20 30 40 50 60 MENQLAKSTE ERTFQYQDSL PSLPVPSLEE SLKKYLESVK PFANQEEYKK TEEIVQKFQS 70 80 GIGEKLHQKL LERAKGKRNW VFVVIIE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of human carnitine octanoyltransferase: evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids." Ferdinandusse S., Mulders J., Ijlst L., Denis S., Dacremont G., Waterham H.R., Wanders R.J.A. Biochem. Biophys. Res. Commun. 263:213-218(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT. Tissue: Skin.
[2]	"Cloning of the human gene for carnitine octanoyltransferase." Kim D.G., Hlubb C.W., Yun J., Mihalik S.J. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 2). Tissue: Brain and Skin.
[6]	"Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: mutational analysis of a malonyl-CoA affinity domain." Morillas M., Gomez-Puertas P., Rubi B., Clotet J., Arino J., Valencia A., Hegardt F.G., Serra D., Asins G. J. Biol. Chem. 277:11473-11480(2002) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF168793 mRNA. Translation: AAF03234.1. AF073770 mRNA. Translation: AAD41654.1. AC005045 Genomic DNA. No translation available. CH236949 Genomic DNA. Translation: EAL24177.1. CH471091 Genomic DNA. Translation: EAW76954.1. BC039004 mRNA. Translation: AAH39004.1. BC051874 mRNA. Translation: AAH51874.1.
IPI	IPI00292763.
PIR	JC7101.
RefSeq	NP_001230674.1. NM_001243745.1. NP_066974.2. NM_021151.3.
UniGene	Hs.125039.
3D structure databases
ProteinModelPortal	Q9UKG9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UKG9. 1 interaction.
STRING	9606.ENSP00000413575.
Protein family/group databases
TCDB	4.C.2.1.2. carnitine O-acyl transferase (CrAT) family.
PTM databases
PhosphoSite	Q9UKG9.
Polymorphism databases
DMDM	48429265.
Proteomic databases
PaxDb	Q9UKG9.
PeptideAtlas	Q9UKG9.
PRIDE	Q9UKG9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000331536; ENSP00000331981; ENSG00000005469. ENST00000412227; ENSP00000404867; ENSG00000005469.
GeneID	54677.
KEGG	hsa:54677.
UCSC	uc003uis.3. human. uc003uit.3. human.
Organism-specific databases
CTD	54677.
GeneCards	GC07P086974.
HGNC	HGNC:2366. CROT.
HPA	HPA019052. HPA019364. HPA019365.
MIM	606090. gene.
neXtProt	NX_Q9UKG9.
PharmGKB	PA26887.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG70127.
HOGENOM	HOG000233845.
HOVERGEN	HBG104403.
InParanoid	Q9UKG9.
KO	K05940.
PhylomeDB	Q9UKG9.
Enzyme and pathway databases
BRENDA	2.3.1.137. 2681.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00659.
Gene expression databases
ArrayExpress	Q9UKG9.
Bgee	Q9UKG9.
CleanEx	HS_CROT.
Genevestigator	Q9UKG9.
GermOnline	ENSG00000005469. Homo sapiens.
Family and domain databases
InterPro	IPR000542. Carn_acyl_trans. [Graphical view]
PANTHER	PTHR22589. PTHR22589. 1 hit.
Pfam	PF00755. Carn_acyltransf. 1 hit. [Graphical view]
PROSITE	PS00439. ACYLTRANSF_C_1. 1 hit. PS00440. ACYLTRANSF_C_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9UKG9.
ChEMBL	CHEMBL2206.
DrugBank	DB00583. L-Carnitine.
GenomeRNAi	54677.
NextBio	57236.
SOURCE	Search...

Entry information

Entry name

OCTC_HUMAN

Accession

Primary (citable) accession number: Q9UKG9
Secondary accession number(s): A4D1D6 , Q86V17, Q8IUW9, Q9Y6I2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	June 7, 2004
Last modified:	May 29, 2013
This is version 110 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.