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Q9UKG9

- OCTC_HUMAN

UniProt

Q9UKG9 - OCTC_HUMAN

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Protein

Peroxisomal carnitine O-octanoyltransferase

Gene

CROT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9UKG9.
CleanExiHS_CROT.
ExpressionAtlasiQ9UKG9. baseline and differential.
GenevestigatoriQ9UKG9.

Organism-specific databases

HPAiHPA019052.
HPA019364.
HPA019365.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi120098. 8 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.
GeneTreeiENSGT00760000119220.
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

        10         20         30         40         50
MENQLAKSTE ERTFQYQDSL PSLPVPSLEE SLKKYLESVK PFANQEEYKK
60 70 80 90 100
TEEIVQKFQS GIGEKLHQKL LERAKGKRNW LEEWWLNVAY LDVRIPSQLN
110 120 130 140 150
VNFAGPAAHF EHYWPPKEGT QLERGSITLW HNLNYWQLLR KEKVPVHKVG
160 170 180 190 200
NTPLDMNQFR MLFSTCKVPG ITRDSIMNYF RTESEGRSPN HIVVLCRGRA
210 220 230 240 250
FVFDVIHEGC LVTPPELLRQ LTYIHKKCHS EPDGPGIAAL TSEERTRWAK
260 270 280 290 300
AREYLIGLDP ENLALLEKIQ SSLLVYSMED SSPHVTPEDY SEIIAAILIG
310 320 330 340 350
DPTVRWGDKS YNLISFSNGV FGCNCDHAPF DAMIMVNISY YVDEKIFQNE
360 370 380 390 400
GRWKGSEKVR DIPLPEELIF IVDEKVLNDI NQAKAQYLRE ASDLQIAAYA
410 420 430 440 450
FTSFGKKLTK NKMLHPDTFI QLALQLAYYR LHGHPGCCYE TAMTRHFYHG
460 470 480 490 500
RTETMRSCTV EAVRWCQSMQ DPSVNLRERQ QKMLQAFAKH NKMMKDCSAG
510 520 530 540 550
KGFDRHLLGL LLIAKEEGLP VPELFTDPLF SKSGGGGNFV LSTSLVGYLR
560 570 580 590 600
VQGVVVPMVH NGYGFFYHIR DDRFVVACSA WKSCPETDAE KLVQLTFCAF
610
HDMIQLMNST HL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 8 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.
GeneTreei ENSGT00760000119220.
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

Bgeei Q9UKG9.
CleanExi HS_CROT.
ExpressionAtlasi Q9UKG9. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 125 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