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Q9UKG9

- OCTC_HUMAN

UniProt

Q9UKG9 - OCTC_HUMAN

Protein

Peroxisomal carnitine O-octanoyltransferase

Gene

CROT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    Octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei327 – 3271Proton acceptorBy similarity
    Binding sitei406 – 4061Coenzyme ABy similarity
    Binding sitei439 – 4391CarnitineBy similarity
    Binding sitei441 – 4411Carnitine; via carbonyl oxygenBy similarity
    Binding sitei452 – 4521CarnitineBy similarity

    GO - Molecular functioni

    1. carnitine O-octanoyltransferase activity Source: UniProtKB
    2. receptor binding Source: UniProtKB

    GO - Biological processi

    1. carnitine metabolic process Source: UniProtKB
    2. cellular lipid metabolic process Source: Reactome
    3. coenzyme A metabolic process Source: UniProtKB
    4. fatty acid beta-oxidation Source: UniProtKB
    5. fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
    6. fatty acid metabolic process Source: UniProtKB
    7. fatty acid transport Source: Ensembl
    8. generation of precursor metabolites and energy Source: UniProtKB
    9. medium-chain fatty acid metabolic process Source: UniProtKB
    10. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism, Transport

    Enzyme and pathway databases

    BRENDAi2.3.1.137. 2681.
    ReactomeiREACT_17017. Beta-oxidation of pristanoyl-CoA.
    UniPathwayiUPA00659.

    Protein family/group databases

    TCDBi4.C.2.1.2. the carnitine o-acyl transferase (crat) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal carnitine O-octanoyltransferase (EC:2.3.1.137)
    Short name:
    COT
    Gene namesi
    Name:CROT
    Synonyms:COT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:2366. CROT.

    Subcellular locationi

    Peroxisome Curated

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: HPA
    2. mitochondrion Source: Ensembl
    3. peroxisomal matrix Source: Reactome
    4. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26887.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 612612Peroxisomal carnitine O-octanoyltransferasePRO_0000210169Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei40 – 401N6-succinyllysineBy similarity
    Modified residuei57 – 571N6-succinyllysineBy similarity
    Modified residuei406 – 4061N6-acetyllysine; alternateBy similarity
    Modified residuei406 – 4061N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UKG9.
    PaxDbiQ9UKG9.
    PeptideAtlasiQ9UKG9.
    PRIDEiQ9UKG9.

    PTM databases

    PhosphoSiteiQ9UKG9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UKG9.
    BgeeiQ9UKG9.
    CleanExiHS_CROT.
    GenevestigatoriQ9UKG9.

    Organism-specific databases

    HPAiHPA019052.
    HPA019364.
    HPA019365.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi120098. 4 interactions.
    IntActiQ9UKG9. 1 interaction.
    STRINGi9606.ENSP00000413575.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UKG9.
    SMRiQ9UKG9. Positions 11-609.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni410 – 4178Coenzyme A bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi610 – 6123Microbody targeting signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi534 – 5374Poly-Gly

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG70127.
    HOGENOMiHOG000233845.
    HOVERGENiHBG104403.
    InParanoidiQ9UKG9.
    KOiK05940.
    OMAiDSIMNYF.
    OrthoDBiEOG7BGHKN.
    PhylomeDBiQ9UKG9.
    TreeFamiTF313836.

    Family and domain databases

    InterProiIPR000542. Carn_acyl_trans.
    [Graphical view]
    PANTHERiPTHR22589. PTHR22589. 1 hit.
    PfamiPF00755. Carn_acyltransf. 1 hit.
    [Graphical view]
    PROSITEiPS00439. ACYLTRANSF_C_1. 1 hit.
    PS00440. ACYLTRANSF_C_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UKG9-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MENQLAKSTE ERTFQYQDSL PSLPVPSLEE SLKKYLESVK PFANQEEYKK    50
    TEEIVQKFQS GIGEKLHQKL LERAKGKRNW LEEWWLNVAY LDVRIPSQLN 100
    VNFAGPAAHF EHYWPPKEGT QLERGSITLW HNLNYWQLLR KEKVPVHKVG 150
    NTPLDMNQFR MLFSTCKVPG ITRDSIMNYF RTESEGRSPN HIVVLCRGRA 200
    FVFDVIHEGC LVTPPELLRQ LTYIHKKCHS EPDGPGIAAL TSEERTRWAK 250
    AREYLIGLDP ENLALLEKIQ SSLLVYSMED SSPHVTPEDY SEIIAAILIG 300
    DPTVRWGDKS YNLISFSNGV FGCNCDHAPF DAMIMVNISY YVDEKIFQNE 350
    GRWKGSEKVR DIPLPEELIF IVDEKVLNDI NQAKAQYLRE ASDLQIAAYA 400
    FTSFGKKLTK NKMLHPDTFI QLALQLAYYR LHGHPGCCYE TAMTRHFYHG 450
    RTETMRSCTV EAVRWCQSMQ DPSVNLRERQ QKMLQAFAKH NKMMKDCSAG 500
    KGFDRHLLGL LLIAKEEGLP VPELFTDPLF SKSGGGGNFV LSTSLVGYLR 550
    VQGVVVPMVH NGYGFFYHIR DDRFVVACSA WKSCPETDAE KLVQLTFCAF 600
    HDMIQLMNST HL 612
    Length:612
    Mass (Da):70,178
    Last modified:June 7, 2004 - v2
    Checksum:iBFC4E0A09B191038
    GO
    Isoform 2 (identifier: Q9UKG9-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:87
    Mass (Da):10,214
    Checksum:i9806EC31C962CE35
    GO
    Isoform 3 (identifier: Q9UKG9-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:640
    Mass (Da):73,383
    Checksum:i3215B8DD2DBB1F65
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1441V → L in AAF03234. (PubMed:10486279)Curated
    Sequence conflicti168 – 1681V → G in AAD41654. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti94 – 941R → H.
    Corresponds to variant rs3827653 [ dbSNP | Ensembl ].
    VAR_048612
    Natural varianti474 – 4741V → L.
    Corresponds to variant rs7785206 [ dbSNP | Ensembl ].
    VAR_048613

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei38 – 381S → SVTRTCYQIRGLDPDAKRGF LDLTREGIQ in isoform 3. CuratedVSP_046953
    Alternative sequencei81 – 877LEEWWLN → VFVVIIE in isoform 2. 1 PublicationVSP_045213
    Alternative sequencei88 – 612525Missing in isoform 2. 1 PublicationVSP_045214Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS47634.1. [Q9UKG9-3]
    CCDS5604.1. [Q9UKG9-1]
    CCDS59062.1. [Q9UKG9-2]
    PIRiJC7101.
    RefSeqiNP_001137407.1. NM_001143935.1. [Q9UKG9-3]
    NP_001230674.1. NM_001243745.1. [Q9UKG9-2]
    NP_066974.2. NM_021151.3. [Q9UKG9-1]
    UniGeneiHs.125039.

    Genome annotation databases

    EnsembliENST00000331536; ENSP00000331981; ENSG00000005469. [Q9UKG9-1]
    ENST00000412227; ENSP00000404867; ENSG00000005469. [Q9UKG9-2]
    ENST00000419147; ENSP00000413575; ENSG00000005469. [Q9UKG9-3]
    GeneIDi54677.
    KEGGihsa:54677.
    UCSCiuc003uis.3. human.
    uc003uit.3. human. [Q9UKG9-1]

    Polymorphism databases

    DMDMi48429265.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS47634.1. [Q9UKG9-3 ]
    CCDS5604.1. [Q9UKG9-1 ]
    CCDS59062.1. [Q9UKG9-2 ]
    PIRi JC7101.
    RefSeqi NP_001137407.1. NM_001143935.1. [Q9UKG9-3 ]
    NP_001230674.1. NM_001243745.1. [Q9UKG9-2 ]
    NP_066974.2. NM_021151.3. [Q9UKG9-1 ]
    UniGenei Hs.125039.

    3D structure databases

    ProteinModelPortali Q9UKG9.
    SMRi Q9UKG9. Positions 11-609.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120098. 4 interactions.
    IntActi Q9UKG9. 1 interaction.
    STRINGi 9606.ENSP00000413575.

    Chemistry

    BindingDBi Q9UKG9.
    ChEMBLi CHEMBL2206.
    DrugBanki DB00583. L-Carnitine.

    Protein family/group databases

    TCDBi 4.C.2.1.2. the carnitine o-acyl transferase (crat) family.

    PTM databases

    PhosphoSitei Q9UKG9.

    Polymorphism databases

    DMDMi 48429265.

    Proteomic databases

    MaxQBi Q9UKG9.
    PaxDbi Q9UKG9.
    PeptideAtlasi Q9UKG9.
    PRIDEi Q9UKG9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331536 ; ENSP00000331981 ; ENSG00000005469 . [Q9UKG9-1 ]
    ENST00000412227 ; ENSP00000404867 ; ENSG00000005469 . [Q9UKG9-2 ]
    ENST00000419147 ; ENSP00000413575 ; ENSG00000005469 . [Q9UKG9-3 ]
    GeneIDi 54677.
    KEGGi hsa:54677.
    UCSCi uc003uis.3. human.
    uc003uit.3. human. [Q9UKG9-1 ]

    Organism-specific databases

    CTDi 54677.
    GeneCardsi GC07P086974.
    HGNCi HGNC:2366. CROT.
    HPAi HPA019052.
    HPA019364.
    HPA019365.
    MIMi 606090. gene.
    neXtProti NX_Q9UKG9.
    PharmGKBi PA26887.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70127.
    HOGENOMi HOG000233845.
    HOVERGENi HBG104403.
    InParanoidi Q9UKG9.
    KOi K05940.
    OMAi DSIMNYF.
    OrthoDBi EOG7BGHKN.
    PhylomeDBi Q9UKG9.
    TreeFami TF313836.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BRENDAi 2.3.1.137. 2681.
    Reactomei REACT_17017. Beta-oxidation of pristanoyl-CoA.

    Miscellaneous databases

    GeneWikii CROT_(gene).
    GenomeRNAii 54677.
    NextBioi 57236.
    PROi Q9UKG9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKG9.
    Bgeei Q9UKG9.
    CleanExi HS_CROT.
    Genevestigatori Q9UKG9.

    Family and domain databases

    InterProi IPR000542. Carn_acyl_trans.
    [Graphical view ]
    PANTHERi PTHR22589. PTHR22589. 1 hit.
    Pfami PF00755. Carn_acyltransf. 1 hit.
    [Graphical view ]
    PROSITEi PS00439. ACYLTRANSF_C_1. 1 hit.
    PS00440. ACYLTRANSF_C_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiOCTC_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKG9
    Secondary accession number(s): A4D1D6
    , E7EQF2, Q86V17, Q8IUW9, Q9Y6I2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3