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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)DescriptionActionsGraphical viewLength
Active sitei343Proton acceptor1
Binding sitei419Coenzyme A2 Publications1
Binding sitei452Carnitine2 Publications1
Binding sitei454Carnitine2 Publications1
Binding sitei456Coenzyme A; via amide nitrogen2 Publications1
Binding sitei465Carnitine2 Publications1
Binding sitei504Coenzyme A2 Publications1
Binding sitei555Coenzyme A; via carbonyl oxygen2 Publications1

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)DescriptionActionsGraphical viewLength
Mutagenesisi564M → A: Lowers activity towards short-chain fatty acids. 1
Mutagenesisi564M → G: Lowers activity towards short-chain fatty acids. Strong increase in activity towards medium chain fatty acids. 1
Mutagenesisi565F → A: Increases activity towards short-chain fatty acids. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002101731 – 626Carnitine O-acetyltransferaseAdd BLAST626

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei93N6-succinyllysineCombined sources1
Modified residuei261N6-acetyllysine; alternateBy similarity1
Modified residuei261N6-succinyllysine; alternateCombined sources1
Modified residuei268N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP47934.
PaxDbiP47934.
PRIDEiP47934.

PTM databases

iPTMnetiP47934.
PhosphoSitePlusiP47934.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026853.
CleanExiMM_CRAT.
ExpressionAtlasiP47934. baseline and differential.
GenevisibleiP47934. MM.

Interactioni

Subunit structurei

Monomer.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1626
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 34Combined sources3
Helixi43 – 54Combined sources12
Turni55 – 57Combined sources3
Helixi60 – 73Combined sources14
Helixi79 – 93Combined sources15
Helixi99 – 106Combined sources8
Turni107 – 109Combined sources3
Turni116 – 118Combined sources3
Beta strandi121 – 124Combined sources4
Helixi132 – 154Combined sources23
Beta strandi163 – 165Combined sources3
Beta strandi166 – 168Combined sources3
Helixi171 – 174Combined sources4
Beta strandi176 – 182Combined sources7
Beta strandi185 – 187Combined sources3
Beta strandi189 – 192Combined sources4
Beta strandi196 – 198Combined sources3
Beta strandi202 – 207Combined sources6
Beta strandi210 – 215Combined sources6
Beta strandi219 – 221Combined sources3
Helixi226 – 238Combined sources13
Helixi248 – 253Combined sources6
Helixi256 – 266Combined sources11
Helixi270 – 281Combined sources12
Beta strandi285 – 288Combined sources4
Turni297 – 299Combined sources3
Helixi300 – 309Combined sources10
Turni314 – 319Combined sources6
Beta strandi325 – 331Combined sources7
Beta strandi333 – 335Combined sources3
Beta strandi337 – 341Combined sources5
Turni343 – 345Combined sources3
Helixi348 – 361Combined sources14
Beta strandi379 – 381Combined sources3
Helixi387 – 405Combined sources19
Beta strandi407 – 414Combined sources8
Helixi420 – 424Combined sources5
Helixi429 – 445Combined sources17
Beta strandi451 – 456Combined sources6
Beta strandi465 – 469Combined sources5
Helixi473 – 483Combined sources11
Beta strandi485 – 487Combined sources3
Helixi489 – 511Combined sources23
Helixi517 – 529Combined sources13
Helixi536 – 539Combined sources4
Helixi541 – 546Combined sources6
Beta strandi550 – 555Combined sources6
Beta strandi559 – 561Combined sources3
Beta strandi563 – 565Combined sources3
Beta strandi574 – 580Combined sources7
Beta strandi585 – 592Combined sources8
Helixi600 – 619Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47934.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni423 – 430Coenzyme A binding8

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi624 – 626Microbody targeting signalSequence analysis3

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
GeneTreeiENSGT00760000119220.
HOGENOMiHOG000233845.
HOVERGENiHBG107717.
InParanoidiP47934.
KOiK00624.
OMAiAHINFSL.
OrthoDBiEOG091G038F.
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)DescriptionActionsGraphical viewLength
Sequence conflicti39P → S in BAE41993 (PubMed:16141072).Curated1
Sequence conflicti110 – 112FRQ → LPDK in CAA59971 (PubMed:9065756).Curated3
Sequence conflicti182V → E in CAA59971 (PubMed:9065756).Curated1
Sequence conflicti217Y → H in BAE41993 (PubMed:16141072).Curated1
Sequence conflicti218H → N in CAA59971 (PubMed:9065756).Curated1
Sequence conflicti587F → L in CAA59971 (PubMed:9065756).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP47934.
PhosphoSitePlusiP47934.

Proteomic databases

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.
OMAiAHINFSL.
OrthoDBiEOG091G038F.
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

BgeeiENSMUSG00000026853.
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...

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: November 2, 2016
This is version 133 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.