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Protein

Carnitine O-acetyltransferase

Gene

Crat

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.

Catalytic activityi

Acetyl-CoA + carnitine = CoA + O-acetylcarnitine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei343 – 3431Proton acceptor
Binding sitei419 – 4191Coenzyme A2 Publications
Binding sitei452 – 4521Carnitine2 Publications
Binding sitei454 – 4541Carnitine2 Publications
Binding sitei456 – 4561Coenzyme A; via amide nitrogen2 Publications
Binding sitei465 – 4651Carnitine2 Publications
Binding sitei504 – 5041Coenzyme A2 Publications
Binding sitei555 – 5551Coenzyme A; via carbonyl oxygen2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism, Transport

Enzyme and pathway databases

BRENDAi2.3.1.7. 3474.
ReactomeiR-MMU-389887. Beta-oxidation of pristanoyl-CoA.
R-MMU-390247. Beta-oxidation of very long chain fatty acids.

Names & Taxonomyi

Protein namesi
Recommended name:
Carnitine O-acetyltransferase (EC:2.3.1.7)
Short name:
Carnitine acetylase
Alternative name(s):
Carnitine acetyltransferase
Short name:
CAT
Short name:
CrAT
Gene namesi
Name:Crat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:109501. Crat.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB-SubCell
  • mitochondrial inner membrane Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • peroxisome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion inner membrane, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi564 – 5641M → A: Lowers activity towards short-chain fatty acids.
Mutagenesisi564 – 5641M → G: Lowers activity towards short-chain fatty acids. Strong increase in activity towards medium chain fatty acids.
Mutagenesisi565 – 5651F → A: Increases activity towards short-chain fatty acids.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 626626Carnitine O-acetyltransferasePRO_0000210173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931N6-succinyllysineCombined sources
Modified residuei261 – 2611N6-acetyllysine; alternateBy similarity
Modified residuei261 – 2611N6-succinyllysine; alternateCombined sources
Modified residuei268 – 2681N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP47934.
MaxQBiP47934.
PaxDbiP47934.
PRIDEiP47934.

PTM databases

iPTMnetiP47934.
PhosphoSiteiP47934.

Expressioni

Gene expression databases

BgeeiP47934.
CleanExiMM_CRAT.
ExpressionAtlasiP47934. baseline and differential.
GenevisibleiP47934. MM.

Interactioni

Subunit structurei

Monomer.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

IntActiP47934. 2 interactions.
MINTiMINT-4089666.
STRINGi10090.ENSMUSP00000028207.

Structurei

Secondary structure

1
626
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 343Combined sources
Helixi43 – 5412Combined sources
Turni55 – 573Combined sources
Helixi60 – 7314Combined sources
Helixi79 – 9315Combined sources
Helixi99 – 1068Combined sources
Turni107 – 1093Combined sources
Turni116 – 1183Combined sources
Beta strandi121 – 1244Combined sources
Helixi132 – 15423Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi166 – 1683Combined sources
Helixi171 – 1744Combined sources
Beta strandi176 – 1827Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi202 – 2076Combined sources
Beta strandi210 – 2156Combined sources
Beta strandi219 – 2213Combined sources
Helixi226 – 23813Combined sources
Helixi248 – 2536Combined sources
Helixi256 – 26611Combined sources
Helixi270 – 28112Combined sources
Beta strandi285 – 2884Combined sources
Turni297 – 2993Combined sources
Helixi300 – 30910Combined sources
Turni314 – 3196Combined sources
Beta strandi325 – 3317Combined sources
Beta strandi333 – 3353Combined sources
Beta strandi337 – 3415Combined sources
Turni343 – 3453Combined sources
Helixi348 – 36114Combined sources
Beta strandi379 – 3813Combined sources
Helixi387 – 40519Combined sources
Beta strandi407 – 4148Combined sources
Helixi420 – 4245Combined sources
Helixi429 – 44517Combined sources
Beta strandi451 – 4566Combined sources
Beta strandi465 – 4695Combined sources
Helixi473 – 48311Combined sources
Beta strandi485 – 4873Combined sources
Helixi489 – 51123Combined sources
Helixi517 – 52913Combined sources
Helixi536 – 5394Combined sources
Helixi541 – 5466Combined sources
Beta strandi550 – 5556Combined sources
Beta strandi559 – 5613Combined sources
Beta strandi563 – 5653Combined sources
Beta strandi574 – 5807Combined sources
Beta strandi585 – 5928Combined sources
Helixi600 – 61920Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NDBX-ray1.80A/B30-625[»]
1NDFX-ray1.90A/B30-625[»]
1NDIX-ray2.30A/B30-625[»]
1T7NX-ray1.90A30-626[»]
1T7OX-ray2.30A30-626[»]
1T7QX-ray1.80A/B30-626[»]
2H3PX-ray2.20A/B30-625[»]
2H3UX-ray1.90A/B30-625[»]
2H3WX-ray2.10A/B30-625[»]
ProteinModelPortaliP47934.
SMRiP47934. Positions 30-625.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47934.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni423 – 4308Coenzyme A binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi624 – 6263Microbody targeting signalSequence analysis

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
GeneTreeiENSGT00760000119220.
HOGENOMiHOG000233845.
HOVERGENiHBG107717.
InParanoidiP47934.
KOiK00624.
OMAiDHIVEYT.
OrthoDBiEOG7WHH90.
PhylomeDBiP47934.
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.

P47934-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAFAARTVV KPLGLLKPSS LMKVSGRFKA HQDALPRLPV PPLQQSLDYY
60 70 80 90 100
LKALQPIVSE EEWAHTKQLV DEFQTSGGVG ERLQKGLERR AKKMENWLSE
110 120 130 140 150
WWLKTAYLQF RQPVVIYSSP GVILPKQDFV DLQGQLRFAA KLIEGVLDFK
160 170 180 190 200
SMIDNETLPV EFLGGQPLCM NQYYQILSSC RVPGPKQDSV VNFLKSKRPP
210 220 230 240 250
THITVVHNYQ FFELDVYHSD GTPLTSDQIF VQLEKIWNSS LQSNKEPVGI
260 270 280 290 300
LTSNHRNTWA KAYNNLIKDK VNRESVNSIQ KSIFTVCLDK QVPRVSDDVY
310 320 330 340 350
RNHVAGQMLH GGGSKFNSGN RWFDKTLQFI VAEDGSCGMV YEHAAAEGPP
360 370 380 390 400
IVALVDHVME YTKKPELVRS PMVPLPMPKK LRFNITPEIK NDIEKAKQNL
410 420 430 440 450
SIMIQDLDIM MLTFHHFGKD FPKSEKLSPD AFIQVALQLA YYRIYGQACA
460 470 480 490 500
TYESASLRMF HLGRTDTIRS ASIDSLAFVK GMGDSTVPEQ QKVELLRKAV
510 520 530 540 550
QAHRAYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD TSYAIAMHFN
560 570 580 590 600
LSTSQVPAKT DCVMFFGPVV PDGYGICYNP MEAHINFSVS AYNSCAETNA
610 620
ARMAHYLEKA LLDMRTLLQN HPRAKL
Length:626
Mass (Da):70,840
Last modified:January 11, 2011 - v3
Checksum:i975EA04403A4F3D9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391P → S in BAE41993 (PubMed:16141072).Curated
Sequence conflicti110 – 1123FRQ → LPDK in CAA59971 (PubMed:9065756).Curated
Sequence conflicti182 – 1821V → E in CAA59971 (PubMed:9065756).Curated
Sequence conflicti217 – 2171Y → H in BAE41993 (PubMed:16141072).Curated
Sequence conflicti218 – 2181H → N in CAA59971 (PubMed:9065756).Curated
Sequence conflicti587 – 5871F → L in CAA59971 (PubMed:9065756).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85983 mRNA. Translation: CAA59971.1.
AK132179 mRNA. Translation: BAE21016.1.
AK170740 mRNA. Translation: BAE41993.1.
AL954388, AL954299 Genomic DNA. Translation: CAM23162.1.
AL954299, AL954388 Genomic DNA. Translation: CAM23291.1.
BC006668 mRNA. Translation: AAH06668.1.
CCDSiCCDS15882.1.
PIRiS52782.
RefSeqiNP_031786.2. NM_007760.3.
UniGeneiMm.20396.

Genome annotation databases

EnsembliENSMUST00000028207; ENSMUSP00000028207; ENSMUSG00000026853.
ENSMUST00000102855; ENSMUSP00000099919; ENSMUSG00000026853.
GeneIDi12908.
KEGGimmu:12908.
UCSCiuc008jcl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85983 mRNA. Translation: CAA59971.1.
AK132179 mRNA. Translation: BAE21016.1.
AK170740 mRNA. Translation: BAE41993.1.
AL954388, AL954299 Genomic DNA. Translation: CAM23162.1.
AL954299, AL954388 Genomic DNA. Translation: CAM23291.1.
BC006668 mRNA. Translation: AAH06668.1.
CCDSiCCDS15882.1.
PIRiS52782.
RefSeqiNP_031786.2. NM_007760.3.
UniGeneiMm.20396.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NDBX-ray1.80A/B30-625[»]
1NDFX-ray1.90A/B30-625[»]
1NDIX-ray2.30A/B30-625[»]
1T7NX-ray1.90A30-626[»]
1T7OX-ray2.30A30-626[»]
1T7QX-ray1.80A/B30-626[»]
2H3PX-ray2.20A/B30-625[»]
2H3UX-ray1.90A/B30-625[»]
2H3WX-ray2.10A/B30-625[»]
ProteinModelPortaliP47934.
SMRiP47934. Positions 30-625.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP47934. 2 interactions.
MINTiMINT-4089666.
STRINGi10090.ENSMUSP00000028207.

PTM databases

iPTMnetiP47934.
PhosphoSiteiP47934.

Proteomic databases

EPDiP47934.
MaxQBiP47934.
PaxDbiP47934.
PRIDEiP47934.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028207; ENSMUSP00000028207; ENSMUSG00000026853.
ENSMUST00000102855; ENSMUSP00000099919; ENSMUSG00000026853.
GeneIDi12908.
KEGGimmu:12908.
UCSCiuc008jcl.1. mouse.

Organism-specific databases

CTDi1384.
MGIiMGI:109501. Crat.

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
GeneTreeiENSGT00760000119220.
HOGENOMiHOG000233845.
HOVERGENiHBG107717.
InParanoidiP47934.
KOiK00624.
OMAiDHIVEYT.
OrthoDBiEOG7WHH90.
PhylomeDBiP47934.
TreeFamiTF313836.

Enzyme and pathway databases

BRENDAi2.3.1.7. 3474.
ReactomeiR-MMU-389887. Beta-oxidation of pristanoyl-CoA.
R-MMU-390247. Beta-oxidation of very long chain fatty acids.

Miscellaneous databases

EvolutionaryTraceiP47934.
PROiP47934.
SOURCEiSearch...

Gene expression databases

BgeeiP47934.
CleanExiMM_CRAT.
ExpressionAtlasiP47934. baseline and differential.
GenevisibleiP47934. 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. "Cloning and characterization of murine carnitine acetyltransferase: evidence for a requirement during cell cycle progression."
    Brunner S., Kramar K., Denhardt D.T., Hofbauer R.
    Biochem. J. 322:403-410(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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 and NOD.
    Tissue: Head.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "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-93 AND LYS-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport."
    Jogl G., Tong L.
    Cell 112:113-122(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-626 IN COMPLEX WITH CARNITINE AND COENZYME A.
  8. "Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase."
    Hsiao Y.-S., Jogl G., Tong L.
    J. Biol. Chem. 279:31584-31589(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-626 OF MUTANTS GLY-564 AND ALA-565 IN COMPLEX WITH CARNITINE AND COENZYME A.

Entry informationi

Entry nameiCACP_MOUSE
AccessioniPrimary (citable) accession number: P47934
Secondary accession number(s): Q3TCG3, Q3V1Y3, Q923A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 11, 2011
Last modified: June 8, 2016
This is version 131 of the entry and version 3 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.