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Q9UKG9 (OCTC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal carnitine O-octanoyltransferase

Short name=COT
EC=2.3.1.137
Gene names
Name:CROT
Synonyms:COT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length612 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processFatty acid metabolism
Lipid metabolism
Transport
   Cellular componentPeroxisome
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarnitine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

coenzyme A metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid beta-oxidation

Inferred from direct assay PubMed 21619872. Source: UniProtKB

fatty acid beta-oxidation using acyl-CoA oxidase

Traceable author statement. Source: Reactome

fatty acid metabolic process

Inferred from mutant phenotype PubMed 21619872. Source: UniProtKB

fatty acid transport

Inferred from electronic annotation. Source: Ensembl

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

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentintracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Traceable author statement. Source: Reactome

peroxisome

Inferred from direct assay PubMed 21619872. Source: UniProtKB

   Molecular_functioncarnitine O-octanoyltransferase activity

Inferred from direct assay Ref.1PubMed 21619872. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 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.
Isoform 3 (identifier: Q9UKG9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     38-38: S → SVTRTCYQIRGLDPDAKRGFLDLTREGIQ
Note: No experimental confirmation available. Gene prediction based on cDNA data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 612612Peroxisomal carnitine O-octanoyltransferase
PRO_0000210169

Regions

Region410 – 4178Coenzyme A binding By similarity
Motif610 – 6123Microbody targeting signal Potential
Compositional bias534 – 5374Poly-Gly

Sites

Active site3271Proton acceptor By similarity
Binding site4061Coenzyme A By similarity
Binding site4391Carnitine By similarity
Binding site4411Carnitine; via carbonyl oxygen By similarity
Binding site4521Carnitine By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7
Modified residue401N6-succinyllysine By similarity
Modified residue571N6-succinyllysine By similarity
Modified residue4061N6-acetyllysine; alternate By similarity
Modified residue4061N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence381S → SVTRTCYQIRGLDPDAKRGF LDLTREGIQ in isoform 3.
VSP_046953
Alternative sequence81 – 877LEEWWLN → VFVVIIE in isoform 2.
VSP_045213
Alternative sequence88 – 612525Missing in isoform 2.
VSP_045214
Natural variant941R → H.
Corresponds to variant rs3827653 [ dbSNP | Ensembl ].
VAR_048612
Natural variant4741V → L.
Corresponds to variant rs7785206 [ dbSNP | Ensembl ].
VAR_048613

Experimental info

Sequence conflict1441V → L in AAF03234. Ref.1
Sequence conflict1681V → G in AAD41654. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: BFC4E0A09B191038

FASTA61270,178
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 9806EC31C962CE35
Show »

FASTA8710,214
Isoform 3 [UniParc].

Checksum: 3215B8DD2DBB1F65
Show »

FASTA64073,383

References

« Hide '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]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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. expand/collapse author list , 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].
[5]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. expand/collapse author list , 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].
[6]"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.
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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.
CCDSCCDS47634.1. [Q9UKG9-3]
CCDS5604.1. [Q9UKG9-1]
CCDS59062.1. [Q9UKG9-2]
PIRJC7101.
RefSeqNP_001137407.1. NM_001143935.1. [Q9UKG9-3]
NP_001230674.1. NM_001243745.1. [Q9UKG9-2]
NP_066974.2. NM_021151.3. [Q9UKG9-1]
UniGeneHs.125039.

3D structure databases

ProteinModelPortalQ9UKG9.
SMRQ9UKG9. Positions 11-609.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120098. 3 interactions.
IntActQ9UKG9. 1 interaction.
STRING9606.ENSP00000413575.

Chemistry

BindingDBQ9UKG9.
ChEMBLCHEMBL2206.
DrugBankDB00583. L-Carnitine.

Protein family/group databases

TCDB4.C.2.1.2. the carnitine o-acyl transferase (crat) family.

PTM databases

PhosphoSiteQ9UKG9.

Polymorphism databases

DMDM48429265.

Proteomic databases

MaxQBQ9UKG9.
PaxDbQ9UKG9.
PeptideAtlasQ9UKG9.
PRIDEQ9UKG9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331536; ENSP00000331981; ENSG00000005469. [Q9UKG9-1]
ENST00000412227; ENSP00000404867; ENSG00000005469. [Q9UKG9-2]
ENST00000419147; ENSP00000413575; ENSG00000005469. [Q9UKG9-3]
GeneID54677.
KEGGhsa:54677.
UCSCuc003uis.3. human.
uc003uit.3. human. [Q9UKG9-1]

Organism-specific databases

CTD54677.
GeneCardsGC07P086974.
HGNCHGNC:2366. CROT.
HPAHPA019052.
HPA019364.
HPA019365.
MIM606090. gene.
neXtProtNX_Q9UKG9.
PharmGKBPA26887.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70127.
HOGENOMHOG000233845.
HOVERGENHBG104403.
InParanoidQ9UKG9.
KOK05940.
OMADSIMNYF.
OrthoDBEOG7BGHKN.
PhylomeDBQ9UKG9.
TreeFamTF313836.

Enzyme and pathway databases

BRENDA2.3.1.137. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00659.

Gene expression databases

ArrayExpressQ9UKG9.
BgeeQ9UKG9.
CleanExHS_CROT.
GenevestigatorQ9UKG9.

Family and domain databases

InterProIPR000542. Carn_acyl_trans.
[Graphical view]
PANTHERPTHR22589. PTHR22589. 1 hit.
PfamPF00755. Carn_acyltransf. 1 hit.
[Graphical view]
PROSITEPS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCROT_(gene).
GenomeRNAi54677.
NextBio57236.
PROQ9UKG9.
SOURCESearch...

Entry information

Entry nameOCTC_HUMAN
AccessionPrimary (citable) accession number: Q9UKG9
Secondary accession number(s): A4D1D6 expand/collapse secondary AC list , E7EQF2, Q86V17, Q8IUW9, Q9Y6I2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 7, 2004
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM