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Protein

Peroxisomal carnitine O-octanoyltransferase

Gene

Crot

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.1 Publication

Catalytic activityi

Octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine.1 Publication

Pathwayi: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei327 – 3271Proton acceptor1 Publication
Binding sitei406 – 4061Coenzyme ABy similarity
Binding sitei439 – 4391Carnitine
Binding sitei441 – 4411Carnitine; via carbonyl oxygen
Binding sitei452 – 4521Carnitine

GO - Molecular functioni

  • carnitine O-octanoyltransferase activity Source: UniProtKB
  • receptor binding Source: MGI

GO - Biological processi

  • carnitine metabolic process Source: UniProtKB
  • coenzyme A metabolic process Source: UniProtKB
  • fatty acid beta-oxidation Source: MGI
  • fatty acid metabolic process Source: UniProtKB
  • fatty acid transport Source: MGI
  • generation of precursor metabolites and energy Source: MGI
  • medium-chain fatty acid metabolic process Source: MGI
  • response to drug Source: Ensembl
  • response to organonitrogen compound Source: Ensembl
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. 3474.
ReactomeiR-MMU-389887. Beta-oxidation of pristanoyl-CoA.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal carnitine O-octanoyltransferase (EC:2.3.1.137)
Short name:
COT
Gene namesi
Name:Crot
Synonyms:Cot
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1921364. Crot.

Subcellular locationi

GO - Cellular componenti

  • intracellular membrane-bounded organelle Source: MGI
  • mitochondrion Source: MGI
  • peroxisome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi323 – 3231C → M: Increases activity with octanoyl-CoA. 1 Publication
Mutagenesisi335 – 3351M → A: Slightly decreases activity with octanoyl-CoA. 1 Publication
Mutagenesisi335 – 3351M → A: Strongly decreases activity with octanoyl-CoA. 1 Publication
Mutagenesisi553 – 5531G → M: Loss of activity with octanoyl-CoA and myristoyl-CoA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 612612Peroxisomal carnitine O-octanoyltransferasePRO_0000210170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei40 – 401N6-succinyllysineCombined sources
Modified residuei57 – 571N6-succinyllysineCombined sources
Modified residuei406 – 4061N6-acetyllysine; alternateCombined sources
Modified residuei406 – 4061N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9DC50.
MaxQBiQ9DC50.
PaxDbiQ9DC50.
PRIDEiQ9DC50.

PTM databases

iPTMnetiQ9DC50.
PhosphoSiteiQ9DC50.
SwissPalmiQ9DC50.

Expressioni

Gene expression databases

BgeeiQ9DC50.
CleanExiMM_CROT.
GenevisibleiQ9DC50. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9DC50. 3 interactions.
MINTiMINT-1850094.
STRINGi10090.ENSMUSP00000003720.

Structurei

Secondary structure

1
612
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni13 – 164Combined sources
Helixi17 – 193Combined sources
Helixi28 – 3912Combined sources
Helixi40 – 423Combined sources
Helixi45 – 6016Combined sources
Helixi62 – 7615Combined sources
Beta strandi78 – 814Combined sources
Helixi82 – 898Combined sources
Helixi97 – 1004Combined sources
Beta strandi103 – 1064Combined sources
Helixi108 – 1114Combined sources
Helixi121 – 14020Combined sources
Helixi157 – 1615Combined sources
Beta strandi162 – 1687Combined sources
Beta strandi175 – 1784Combined sources
Turni183 – 1853Combined sources
Beta strandi191 – 1966Combined sources
Beta strandi199 – 2079Combined sources
Helixi214 – 22916Combined sources
Helixi237 – 2426Combined sources
Helixi245 – 25814Combined sources
Helixi260 – 27112Combined sources
Beta strandi275 – 2784Combined sources
Helixi291 – 2988Combined sources
Helixi302 – 3043Combined sources
Beta strandi312 – 3154Combined sources
Beta strandi321 – 3255Combined sources
Beta strandi327 – 3293Combined sources
Helixi333 – 34816Combined sources
Turni349 – 3513Combined sources
Beta strandi366 – 3683Combined sources
Helixi374 – 39219Combined sources
Beta strandi394 – 4018Combined sources
Helixi406 – 4094Combined sources
Helixi410 – 4123Combined sources
Helixi416 – 43217Combined sources
Beta strandi438 – 4436Combined sources
Beta strandi452 – 4565Combined sources
Helixi460 – 47011Combined sources
Helixi476 – 49823Combined sources
Turni499 – 5013Combined sources
Helixi504 – 51613Combined sources
Helixi523 – 5253Combined sources
Helixi528 – 5325Combined sources
Turni533 – 5375Combined sources
Beta strandi540 – 5456Combined sources
Beta strandi548 – 5503Combined sources
Beta strandi563 – 5708Combined sources
Beta strandi573 – 5819Combined sources
Helixi589 – 61123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XL7X-ray2.00A/B1-612[»]
1XL8X-ray2.20A/B1-612[»]
1XMCX-ray2.00A/B1-612[»]
1XMDX-ray2.10A/B1-612[»]
ProteinModelPortaliQ9DC50.
SMRiQ9DC50. Positions 11-610.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DC50.

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

eggNOGiKOG3718. Eukaryota.
ENOG410ZE4S. LUCA.
GeneTreeiENSGT00760000119220.
HOGENOMiHOG000233845.
HOVERGENiHBG104403.
InParanoidiQ9DC50.
KOiK05940.
OMAiDSIMNYF.
OrthoDBiEOG7BGHKN.
PhylomeDBiQ9DC50.
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]

Sequencei

Sequence statusi: Complete.

Q9DC50-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENQLTKSVE ERTFQYQDSL PSLPVPALEE SLKKYLESVK PFANEDEYKK
60 70 80 90 100
TEEIVQKFQE GAGKRLHQKL LERARGKRNW LEEWWLNVAY LDVRIPSQLN
110 120 130 140 150
VNFVGPCPHF EHYWPAREGT QLERGSMMLW HNLNYWQLLR REKLPVHKSG
160 170 180 190 200
NTPLDMNQFR MLFSTCKVPG ITRDSIMNYF KTESEGHCPT HIAVLCRGRA
210 220 230 240 250
FVFDVLHEGC LITPPELLRQ LTYIHKKCSN EPVGPSIAAL TSEERTRWAK
260 270 280 290 300
AREYLISLDP ENLTLLEKIQ TSLFVYSIED SSPHATPEEY SQVFEMLLGG
310 320 330 340 350
DPSVRWGDKS YNLISFANGI FGCCCDHAPY DAMVMVNIAH YVDERVLETE
360 370 380 390 400
GRWKGSEKVR DIPLPEELVF TVDEKILNDV SQAKAQHLKA ASDLQIAAST
410 420 430 440 450
FTSFGKKLTK EEALHPDTFI QLALQLAYYR LHGRPGCCYE TAMTRYFYHG
460 470 480 490 500
RTETVRSCTV EAVRWCQSMQ DPSASLLERQ QKMLEAFAKH NKMMKDCSHG
510 520 530 540 550
KGFDRHLLGL LLIAKEEGLP VPELFEDPLF SRSGGGGNFV LSTSLVGYLR
560 570 580 590 600
VQGVVVPMVH NGYGFFYHIR DDRFVVACSS WRSCPETDAE KLVQMIFHAF
610
HDMIQLMNTA HL
Length:612
Mass (Da):70,264
Last modified:June 1, 2001 - v1
Checksum:i1C045A419A75C8B6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti459 – 4591T → A in AAH12308 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004567 mRNA. Translation: BAB23378.1.
BC006593 mRNA. Translation: AAH06593.1.
BC012308 mRNA. Translation: AAH12308.1.
CCDSiCCDS19087.1.
RefSeqiNP_076222.1. NM_023733.3.
UniGeneiMm.28197.

Genome annotation databases

EnsembliENSMUST00000003720; ENSMUSP00000003720; ENSMUSG00000003623.
GeneIDi74114.
KEGGimmu:74114.
UCSCiuc008wkt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004567 mRNA. Translation: BAB23378.1.
BC006593 mRNA. Translation: AAH06593.1.
BC012308 mRNA. Translation: AAH12308.1.
CCDSiCCDS19087.1.
RefSeqiNP_076222.1. NM_023733.3.
UniGeneiMm.28197.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XL7X-ray2.00A/B1-612[»]
1XL8X-ray2.20A/B1-612[»]
1XMCX-ray2.00A/B1-612[»]
1XMDX-ray2.10A/B1-612[»]
ProteinModelPortaliQ9DC50.
SMRiQ9DC50. Positions 11-610.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DC50. 3 interactions.
MINTiMINT-1850094.
STRINGi10090.ENSMUSP00000003720.

PTM databases

iPTMnetiQ9DC50.
PhosphoSiteiQ9DC50.
SwissPalmiQ9DC50.

Proteomic databases

EPDiQ9DC50.
MaxQBiQ9DC50.
PaxDbiQ9DC50.
PRIDEiQ9DC50.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003720; ENSMUSP00000003720; ENSMUSG00000003623.
GeneIDi74114.
KEGGimmu:74114.
UCSCiuc008wkt.1. mouse.

Organism-specific databases

CTDi54677.
MGIiMGI:1921364. Crot.

Phylogenomic databases

eggNOGiKOG3718. Eukaryota.
ENOG410ZE4S. LUCA.
GeneTreeiENSGT00760000119220.
HOGENOMiHOG000233845.
HOVERGENiHBG104403.
InParanoidiQ9DC50.
KOiK05940.
OMAiDSIMNYF.
OrthoDBiEOG7BGHKN.
PhylomeDBiQ9DC50.
TreeFamiTF313836.

Enzyme and pathway databases

UniPathwayiUPA00659.
BRENDAi2.3.1.137. 3474.
ReactomeiR-MMU-389887. Beta-oxidation of pristanoyl-CoA.

Miscellaneous databases

ChiTaRSiCrot. mouse.
EvolutionaryTraceiQ9DC50.
PROiQ9DC50.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DC50.
CleanExiMM_CROT.
GenevisibleiQ9DC50. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung.
  2. "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].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Pancreas, Spleen and Testis.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-57 AND LYS-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivity."
    Jogl G., Hsiao Y.S., Tong L.
    J. Biol. Chem. 280:738-744(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH CARNITINE AND OCTANOYLCARNITINE, ACTIVE SITE, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF CYS-323; MET-335 AND GLY-553.

Entry informationi

Entry nameiOCTC_MOUSE
AccessioniPrimary (citable) accession number: Q9DC50
Secondary accession number(s): Q921I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.