UniProtKB - P43155 (CACP_HUMAN)
Carnitine O-acetyltransferase
CRAT
Functioni
Catalyzes the reversible transfer of acyl groups from carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio. Also plays a crucial role in the transport of fatty acids for beta-oxidation (PubMed:15099582, PubMed:29395073).
Responsible for the synthesis of short- and branched-chain acylcarnitines (PubMed:23485643).
Active towards some branched-chain amino acid oxidation pathway (BCAAO) intermediates (PubMed:23485643).
Trans-2-enoyl-CoAs and 2-methylacyl-CoAs are poor substrates (PubMed:23485643).
3 PublicationsCatalytic activityi
- EC:2.3.1.71 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- EC:2.3.1.1371 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- (R)-carnitine + 2,6-dimethylheptanoyl-CoA = CoA + O-2,6-dimethylheptanoyl-(R)-carnitine1 PublicationThis reaction proceeds in the forward1 Publication direction.
Kineticsi
- KM=240 µM for acetyl-CoA1 Publication
- KM=499 µM for butyryl-CoA1 Publication
- KM=590 µM for trans-2-butenoyl-CoA1 Publication
- Vmax=2.5 nmol/min/µg enzyme towards acetyl-CoA1 Publication
- Vmax=10.7 nmol/min/µg enzyme towards butyryl-CoA1 Publication
- Vmax=0.13 nmol/min/µg enzyme towards trans-2-butenoyl-CoA1 Publication
- KM=78 µM for acetyl-CoA1 Publication
- Vmax=4.4 nmol/min/µg enzyme towards acetyl-CoA1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 343 | Proton acceptorCurated | 1 | |
Binding sitei | 419 | Coenzyme ABy similarity | 1 | |
Binding sitei | 452 | Carnitine1 Publication | 1 | |
Binding sitei | 454 | Carnitine1 Publication | 1 | |
Binding sitei | 456 | Coenzyme A; via amide nitrogenBy similarity | 1 | |
Binding sitei | 465 | Carnitine1 Publication | 1 | |
Binding sitei | 504 | Coenzyme ABy similarity | 1 | |
Binding sitei | 555 | Coenzyme A; via carbonyl oxygenBy similarity | 1 |
GO - Molecular functioni
- acyl-CoA oxidase activity Source: UniProtKB
- carnitine O-acetyltransferase activity Source: UniProtKB
- carnitine O-octanoyltransferase activity Source: UniProtKB-EC
GO - Biological processi
- carnitine metabolic process, CoA-linked Source: UniProtKB
- fatty acid beta-oxidation using acyl-CoA oxidase Source: UniProtKB
- medium-chain fatty acid metabolic process Source: UniProtKB
- short-chain fatty acid metabolic process Source: UniProtKB
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Fatty acid metabolism, Lipid metabolism, Transport |
Enzyme and pathway databases
BRENDAi | 2.3.1.7, 2681 |
PathwayCommonsi | P43155 |
Reactomei | R-HSA-389887, Beta-oxidation of pristanoyl-CoA R-HSA-9033241, Peroxisomal protein import |
SABIO-RKi | P43155 |
SignaLinki | P43155 |
Protein family/group databases
TCDBi | 4.C.2.1.1, the carnitine o-acyl transferase (carat) family |
Chemistry databases
SwissLipidsi | SLP:000001053 SLP:000001057 [P43155-1] SLP:000001058 [P43155-2] |
Names & Taxonomyi
Protein namesi | |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:2342, CRAT |
MIMi | 600184, gene |
neXtProti | NX_P43155 |
VEuPathDBi | HostDB:ENSG00000095321 |
Subcellular locationi
Mitochondrion
- Mitochondrion inner membrane Curated; Peripheral membrane protein Curated; Matrix side Curated
Peroxisome
- Peroxisome Curated
Endoplasmic reticulum
- Endoplasmic reticulum Curated
Mitochondrion
- Mitochondrion 1 Publication
Peroxisome
- Peroxisome 1 Publication
Cytosol
- cytosol Source: Reactome
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB-SubCell
Mitochondrion
- mitochondrial inner membrane Source: UniProtKB-SubCell
- mitochondrion Source: UniProtKB
Peroxisome
- peroxisomal matrix Source: Reactome
- peroxisome Source: UniProtKB
Keywords - Cellular componenti
Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion inner membrane, PeroxisomePathology & Biotechi
Involvement in diseasei
Neurodegeneration with brain iron accumulation 8 (NBIA8)1 Publication
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_080636 | 321 | R → H in NBIA8; unknown pathological significance; loss of expression at the protein level and drastic decrease in beta-oxidation of palmitate in homozygous patient's primary fibroblasts as compared to wild-type cells; primary fibroblasts from a homozygous patient show much higher intracellular iron content than fibroblasts from control individuals and abnormally elevated levels of transferrin receptor 1/TFRC at the cell surface. 1 PublicationCorresponds to variant dbSNP:rs138665095EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 452 | Y → A: Increases the KM for carnitine 100-fold. 1 Publication | 1 | |
Mutagenesisi | 452 | Y → F: Increases the KM for carnitine 320-fold and reduces enzyme activity 10000-fold. 1 Publication | 1 | |
Mutagenesisi | 465 | T → A: Increases the KM for carnitine almost 70-fold and reduces enzyme activity 450-fold. 1 Publication | 1 | |
Mutagenesisi | 518 | R → Q: Increases the KM for carnitine 230-fold and reduces enzyme activity almost 100-fold. 1 Publication | 1 | |
Mutagenesisi | 566 | F → A: Increases the KM for carnitine 18-fold and reduces enzyme activity 100-fold. 1 Publication | 1 | |
Mutagenesisi | 566 | F → Y: No effect. 1 Publication | 1 |
Keywords - Diseasei
NeurodegenerationOrganism-specific databases
DisGeNETi | 1384 |
MalaCardsi | CRAT |
MIMi | 617917, phenotype |
OpenTargetsi | ENSG00000095321 |
PharmGKBi | PA26862 |
Miscellaneous databases
Pharosi | P43155, Tbio |
Chemistry databases
ChEMBLi | CHEMBL3184 |
DrugBanki | DB02648, (3-Carboxy-2-(R)-Hydroxy-Propyl)-Trimethyl-Ammonium DB01992, Coenzyme A DB00583, Levocarnitine |
Genetic variation databases
BioMutai | CRAT |
DMDMi | 215274265 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000210172 | 1 – 626 | Carnitine O-acetyltransferaseAdd BLAST | 626 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 93 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 261 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 261 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 268 | N6-acetyllysineCombined sources | 1 |
Keywords - PTMi
AcetylationProteomic databases
CPTACi | CPTAC-341 CPTAC-342 |
EPDi | P43155 |
jPOSTi | P43155 |
MassIVEi | P43155 |
MaxQBi | P43155 |
PaxDbi | P43155 |
PeptideAtlasi | P43155 |
PRIDEi | P43155 |
ProteomicsDBi | 55592 [P43155-1] 55593 [P43155-2] 55594 [P43155-3] |
PTM databases
GlyConnecti | 1073, 4 N-Linked glycans (2 sites) |
GlyGeni | P43155, 2 sites, 5 N-linked glycans (2 sites) |
iPTMneti | P43155 |
PhosphoSitePlusi | P43155 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000095321, Expressed in sperm and 244 other tissues |
ExpressionAtlasi | P43155, baseline and differential |
Genevisiblei | P43155, HS |
Organism-specific databases
HPAi | ENSG00000095321, Tissue enhanced (skeletal muscle, tongue) |
Interactioni
Subunit structurei
Monomer.
2 PublicationsProtein-protein interaction databases
BioGRIDi | 107774, 42 interactors |
IntActi | P43155, 15 interactors |
STRINGi | 9606.ENSP00000315013 |
Chemistry databases
BindingDBi | P43155 |
Miscellaneous databases
RNActi | P43155, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P43155 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P43155 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 423 – 430 | Coenzyme A bindingBy similarity | 8 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 624 – 626 | Microbody targeting signalSequence analysis | 3 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG3717, Eukaryota |
GeneTreei | ENSGT01040000240407 |
HOGENOMi | CLU_013513_5_0_1 |
InParanoidi | P43155 |
OMAi | FNSCAET |
OrthoDBi | 559299at2759 |
PhylomeDBi | P43155 |
TreeFami | TF313836 |
Family and domain databases
Gene3Di | 3.30.559.10, 1 hit 3.30.559.70, 1 hit |
InterProi | View protein in InterPro IPR000542, Carn_acyl_trans IPR023213, CAT-like_dom_sf IPR039551, Cho/carn_acyl_trans IPR042231, Cho/carn_acyl_trans_2 |
PANTHERi | PTHR22589, PTHR22589, 1 hit |
Pfami | View protein in Pfam PF00755, Carn_acyltransf, 1 hit |
PROSITEi | View protein in PROSITE PS00439, ACYLTRANSF_C_1, 1 hit PS00440, ACYLTRANSF_C_2, 1 hit |
s (3+)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 3 described isoforms and 9 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY
60 70 80 90 100
LKALQPIVSE EEWAHTKQLV DEFQASGGVG ERLQKGLERR ARKTENWLSE
110 120 130 140 150
WWLKTAYLQY RQPVVIYSSP GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK
160 170 180 190 200
VMIDNETLPV EYLGGKPLCM NQYYQILSSC RVPGPKQDTV SNFSKTKKPP
210 220 230 240 250
THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS LQTNKEPVGI
260 270 280 290 300
LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY
310 320 330 340 350
RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGPP
360 370 380 390 400
IVTLLDYVIE YTKKPELVRS PLVPLPMPKK LRFNITPEIK SDIEKAKQNL
410 420 430 440 450
SIMIQDLDIT VMVFHHFGKD FPKSEKLSPD AFIQMALQLA YYRIYGQACA
460 470 480 490 500
TYESASLRMF HLGRTDTIRS ASMDSLTFVK AMDDSSVTEH QKVELLRKAV
510 520 530 540 550
QAHRGYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD TSYAIAMHFH
560 570 580 590 600
LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA
610 620
ARLAHYLEKA LLDMRALLQS HPRAKL
Computationally mapped potential isoform sequencesi
There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketH0Y4Z7 | H0Y4Z7_HUMAN | Carnitine O-acetyltransferase | CRAT | 586 | Annotation score: | ||
A0A7P0T9E7 | A0A7P0T9E7_HUMAN | Carnitine O-acetyltransferase | CRAT | 590 | Annotation score: | ||
A0A7P0T9R9 | A0A7P0T9R9_HUMAN | Carnitine O-acetyltransferase | CRAT | 572 | Annotation score: | ||
A6PVN3 | A6PVN3_HUMAN | Carnitine O-acetyltransferase | CRAT | 161 | Annotation score: | ||
B7ZBP5 | B7ZBP5_HUMAN | Carnitine O-acetyltransferase | CRAT | 98 | Annotation score: | ||
A0A7P0TAR1 | A0A7P0TAR1_HUMAN | Carnitine O-acetyltransferase | CRAT | 602 | Annotation score: | ||
A0A7P0TBF3 | A0A7P0TBF3_HUMAN | Carnitine O-acetyltransferase | CRAT | 551 | Annotation score: | ||
A0A7P0TAQ4 | A0A7P0TAQ4_HUMAN | Carnitine O-acetyltransferase | CRAT | 212 | Annotation score: | ||
F2Z2C5 | F2Z2C5_HUMAN | Carnitine O-acetyltransferase | CRAT | 40 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 88 | E → G in CAA55359 (PubMed:7829107).Curated | 1 | |
Sequence conflicti | 349 | P → F in CAA55359 (PubMed:7829107).Curated | 1 | |
Sequence conflicti | 517 | D → G in CAA55359 (PubMed:7829107).Curated | 1 | |
Sequence conflicti | 534 | M → T in CAA55359 (PubMed:7829107).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_080636 | 321 | R → H in NBIA8; unknown pathological significance; loss of expression at the protein level and drastic decrease in beta-oxidation of palmitate in homozygous patient's primary fibroblasts as compared to wild-type cells; primary fibroblasts from a homozygous patient show much higher intracellular iron content than fibroblasts from control individuals and abnormally elevated levels of transferrin receptor 1/TFRC at the cell surface. 1 PublicationCorresponds to variant dbSNP:rs138665095EnsemblClinVar. | 1 | |
Natural variantiVAR_047780 | 372 | L → M3 PublicationsCorresponds to variant dbSNP:rs3118635Ensembl. | 1 | |
Natural variantiVAR_047781 | 624 | A → P. Corresponds to variant dbSNP:rs17459086Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_000792 | 1 – 21 | Missing in isoform 2. CuratedAdd BLAST | 21 | |
Alternative sequenceiVSP_012798 | 282 – 363 | Missing in isoform 3. 2 PublicationsAdd BLAST | 82 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BT006801 mRNA Translation: AAP35447.1 AL158151 Genomic DNA No translation available. BC000723 mRNA Translation: AAH00723.1 X79825 Genomic DNA No translation available. X79827 Genomic DNA No translation available. X78706 mRNA Translation: CAA55359.1 |
CCDSi | CCDS6919.1 [P43155-1] |
PIRi | A55720 |
RefSeqi | XP_005251765.1, XM_005251708.3 [P43155-2] |
Genome annotation databases
Ensembli | ENST00000318080; ENSP00000315013; ENSG00000095321 |
GeneIDi | 1384 |
MANE-Selecti | ENST00000318080.7; ENSP00000315013.2; NM_000755.5; NP_000746.3 |
UCSCi | uc004bxh.4, human [P43155-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BT006801 mRNA Translation: AAP35447.1 AL158151 Genomic DNA No translation available. BC000723 mRNA Translation: AAH00723.1 X79825 Genomic DNA No translation available. X79827 Genomic DNA No translation available. X78706 mRNA Translation: CAA55359.1 |
CCDSi | CCDS6919.1 [P43155-1] |
PIRi | A55720 |
RefSeqi | XP_005251765.1, XM_005251708.3 [P43155-2] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1NM8 | X-ray | 1.60 | A | 35-626 | [»] | |
1S5O | X-ray | 1.80 | A | 35-626 | [»] | |
SMRi | P43155 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 107774, 42 interactors |
IntActi | P43155, 15 interactors |
STRINGi | 9606.ENSP00000315013 |
Chemistry databases
BindingDBi | P43155 |
ChEMBLi | CHEMBL3184 |
DrugBanki | DB02648, (3-Carboxy-2-(R)-Hydroxy-Propyl)-Trimethyl-Ammonium DB01992, Coenzyme A DB00583, Levocarnitine |
SwissLipidsi | SLP:000001053 SLP:000001057 [P43155-1] SLP:000001058 [P43155-2] |
Protein family/group databases
TCDBi | 4.C.2.1.1, the carnitine o-acyl transferase (carat) family |
PTM databases
GlyConnecti | 1073, 4 N-Linked glycans (2 sites) |
GlyGeni | P43155, 2 sites, 5 N-linked glycans (2 sites) |
iPTMneti | P43155 |
PhosphoSitePlusi | P43155 |
Genetic variation databases
BioMutai | CRAT |
DMDMi | 215274265 |
Proteomic databases
CPTACi | CPTAC-341 CPTAC-342 |
EPDi | P43155 |
jPOSTi | P43155 |
MassIVEi | P43155 |
MaxQBi | P43155 |
PaxDbi | P43155 |
PeptideAtlasi | P43155 |
PRIDEi | P43155 |
ProteomicsDBi | 55592 [P43155-1] 55593 [P43155-2] 55594 [P43155-3] |
Protocols and materials databases
Antibodypediai | 17825, 237 antibodies from 30 providers |
DNASUi | 1384 |
Genome annotation databases
Ensembli | ENST00000318080; ENSP00000315013; ENSG00000095321 |
GeneIDi | 1384 |
MANE-Selecti | ENST00000318080.7; ENSP00000315013.2; NM_000755.5; NP_000746.3 |
UCSCi | uc004bxh.4, human [P43155-1] |
Organism-specific databases
CTDi | 1384 |
DisGeNETi | 1384 |
GeneCardsi | CRAT |
HGNCi | HGNC:2342, CRAT |
HPAi | ENSG00000095321, Tissue enhanced (skeletal muscle, tongue) |
MalaCardsi | CRAT |
MIMi | 600184, gene 617917, phenotype |
neXtProti | NX_P43155 |
OpenTargetsi | ENSG00000095321 |
PharmGKBi | PA26862 |
VEuPathDBi | HostDB:ENSG00000095321 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3717, Eukaryota |
GeneTreei | ENSGT01040000240407 |
HOGENOMi | CLU_013513_5_0_1 |
InParanoidi | P43155 |
OMAi | FNSCAET |
OrthoDBi | 559299at2759 |
PhylomeDBi | P43155 |
TreeFami | TF313836 |
Enzyme and pathway databases
BRENDAi | 2.3.1.7, 2681 |
PathwayCommonsi | P43155 |
Reactomei | R-HSA-389887, Beta-oxidation of pristanoyl-CoA R-HSA-9033241, Peroxisomal protein import |
SABIO-RKi | P43155 |
SignaLinki | P43155 |
Miscellaneous databases
BioGRID-ORCSi | 1384, 7 hits in 1045 CRISPR screens |
ChiTaRSi | CRAT, human |
EvolutionaryTracei | P43155 |
GeneWikii | CRAT_(gene) |
GenomeRNAii | 1384 |
Pharosi | P43155, Tbio |
PROi | PR:P43155 |
RNActi | P43155, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000095321, Expressed in sperm and 244 other tissues |
ExpressionAtlasi | P43155, baseline and differential |
Genevisiblei | P43155, HS |
Family and domain databases
Gene3Di | 3.30.559.10, 1 hit 3.30.559.70, 1 hit |
InterProi | View protein in InterPro IPR000542, Carn_acyl_trans IPR023213, CAT-like_dom_sf IPR039551, Cho/carn_acyl_trans IPR042231, Cho/carn_acyl_trans_2 |
PANTHERi | PTHR22589, PTHR22589, 1 hit |
Pfami | View protein in Pfam PF00755, Carn_acyltransf, 1 hit |
PROSITEi | View protein in PROSITE PS00439, ACYLTRANSF_C_1, 1 hit PS00440, ACYLTRANSF_C_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CACP_HUMAN | |
Accessioni | P43155Primary (citable) accession number: P43155 Secondary accession number(s): Q5T952, Q9BW16 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | November 25, 2008 | |
Last modified: | February 23, 2022 | |
This is version 199 of the entry and version 5 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families