UniProtKB - P43155 (CACP_HUMAN)
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Protein
Carnitine O-acetyltransferase
Gene
CRAT
Organism
Homo sapiens (Human)
Status
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 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
- carnitine O-acetyltransferase activity Source: UniProtKB
- receptor binding Source: UniProtKB
GO - Biological processi
- carnitine metabolic process, CoA-linked Source: UniProtKB
- fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
- transport Source: UniProtKB-KW
Keywordsi
| Molecular function | Acyltransferase, Transferase |
| Biological process | Fatty acid metabolism, Lipid metabolism, Transport |
Enzyme and pathway databases
| BioCyci | MetaCyc:HS01816-MONOMER. |
| BRENDAi | 2.3.1.7. 2681. |
| Reactomei | R-HSA-389887. Beta-oxidation of pristanoyl-CoA. R-HSA-390247. Beta-oxidation of very long chain fatty acids. |
| SABIO-RKi | P43155. |
Protein family/group databases
| TCDBi | 4.C.2.1.1. the carnitine o-acyl transferase (crat) family. |
Chemistry databases
| SwissLipidsi | SLP:000001053. SLP:000001057. [P43155-1] SLP:000001058. [P43155-2] |
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 Synonyms:CAT1 |
| 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. |
Subcellular locationi
- Endoplasmic reticulum Curated
- Peroxisome Curated
- Mitochondrion inner membrane Curated; Peripheral membrane protein Curated; Matrix side Curated
Isoform 1 :
- Mitochondrion Curated
Isoform 2 :
- Peroxisome Curated
GO - Cellular componenti
- endoplasmic reticulum Source: UniProtKB-SubCell
- mitochondrial inner membrane Source: UniProtKB-SubCell
- mitochondrion Source: UniProtKB
- peroxisomal matrix Source: Reactome
- peroxisome Source: UniProtKB
Keywords - Cellular componenti
Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion inner membrane, PeroxisomePathology & Biotechi
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 |
Organism-specific databases
| DisGeNETi | 1384. |
| MalaCardsi | CRAT. |
| OpenTargetsi | ENSG00000095321. |
| PharmGKBi | PA26862. |
Chemistry databases
| ChEMBLi | CHEMBL3184. |
| DrugBanki | DB02648. (3-Carboxy-2-(R)-Hydroxy-Propyl)-Trimethyl-Ammonium. DB01992. Coenzyme A. DB00583. L-Carnitine. |
Polymorphism and mutation 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
| EPDi | P43155. |
| MaxQBi | P43155. |
| PaxDbi | P43155. |
| PeptideAtlasi | P43155. |
| PRIDEi | P43155. |
PTM databases
| iPTMneti | P43155. |
| PhosphoSitePlusi | P43155. |
Expressioni
Tissue specificityi
Mostly in skeletal muscle, less in heart, liver and pancreas, only weakly detectable in brain, placenta, lung and kidney.
Gene expression databases
| Bgeei | ENSG00000095321. |
| CleanExi | HS_CRAT. |
| ExpressionAtlasi | P43155. baseline and differential. |
| Genevisiblei | P43155. HS. |
Organism-specific databases
| HPAi | HPA019230. HPA020260. HPA022815. |
Interactioni
Subunit structurei
Monomer.2 Publications
GO - Molecular functioni
- receptor binding Source: UniProtKB
Protein-protein interaction databases
| BioGridi | 107774. 4 interactors. |
| IntActi | P43155. 10 interactors. |
| STRINGi | 9606.ENSP00000315013. |
Chemistry databases
| BindingDBi | P43155. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Helixi | 43 – 54 | Combined sources | 12 | |
| Turni | 55 – 57 | Combined sources | 3 | |
| Helixi | 60 – 74 | Combined sources | 15 | |
| Helixi | 79 – 93 | Combined sources | 15 | |
| Beta strandi | 94 – 96 | Combined sources | 3 | |
| Helixi | 99 – 106 | Combined sources | 8 | |
| Turni | 107 – 109 | Combined sources | 3 | |
| Turni | 116 – 118 | Combined sources | 3 | |
| Beta strandi | 121 – 123 | Combined sources | 3 | |
| Helixi | 132 – 154 | Combined sources | 23 | |
| Helixi | 171 – 175 | Combined sources | 5 | |
| Beta strandi | 179 – 182 | Combined sources | 4 | |
| Beta strandi | 185 – 187 | Combined sources | 3 | |
| Beta strandi | 189 – 192 | Combined sources | 4 | |
| Beta strandi | 196 – 198 | Combined sources | 3 | |
| Beta strandi | 202 – 207 | Combined sources | 6 | |
| Beta strandi | 210 – 215 | Combined sources | 6 | |
| Helixi | 226 – 238 | Combined sources | 13 | |
| Helixi | 248 – 253 | Combined sources | 6 | |
| Helixi | 256 – 266 | Combined sources | 11 | |
| Helixi | 270 – 281 | Combined sources | 12 | |
| Beta strandi | 285 – 289 | Combined sources | 5 | |
| Beta strandi | 297 – 299 | Combined sources | 3 | |
| Helixi | 300 – 310 | Combined sources | 11 | |
| Turni | 314 – 319 | Combined sources | 6 | |
| Beta strandi | 325 – 332 | Combined sources | 8 | |
| Beta strandi | 337 – 341 | Combined sources | 5 | |
| Helixi | 348 – 363 | Combined sources | 16 | |
| Beta strandi | 379 – 381 | Combined sources | 3 | |
| Helixi | 387 – 406 | Combined sources | 20 | |
| Beta strandi | 407 – 414 | Combined sources | 8 | |
| Helixi | 420 – 424 | Combined sources | 5 | |
| Helixi | 429 – 445 | Combined sources | 17 | |
| Beta strandi | 451 – 456 | Combined sources | 6 | |
| Beta strandi | 465 – 469 | Combined sources | 5 | |
| Helixi | 473 – 482 | Combined sources | 10 | |
| Helixi | 489 – 511 | Combined sources | 23 | |
| Helixi | 517 – 529 | Combined sources | 13 | |
| Helixi | 536 – 539 | Combined sources | 4 | |
| Helixi | 541 – 546 | Combined sources | 6 | |
| Beta strandi | 550 – 555 | Combined sources | 6 | |
| Beta strandi | 559 – 561 | Combined sources | 3 | |
| Beta strandi | 563 – 565 | Combined sources | 3 | |
| Beta strandi | 574 – 580 | Combined sources | 7 | |
| Beta strandi | 585 – 592 | Combined sources | 8 | |
| Helixi | 600 – 619 | Combined sources | 20 |
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 | [»] | |
| DisProti | DP00305. | |||||
| ProteinModelPortali | P43155. | |||||
| SMRi | P43155. | |||||
| ModBasei | Search... | |||||
| MobiDBi | 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
Belongs to the carnitine/choline acetyltransferase family.Curated
Phylogenomic databases
| eggNOGi | KOG3717. Eukaryota. ENOG410XNZ9. LUCA. |
| GeneTreei | ENSGT00760000119220. |
| HOGENOMi | HOG000233845. |
| HOVERGENi | HBG107717. |
| InParanoidi | P43155. |
| OMAi | WWNDAAY. |
| OrthoDBi | EOG091G038F. |
| PhylomeDBi | P43155. |
| TreeFami | TF313836. |
Family and domain databases
| InterProi | View protein in InterPro IPR000542. Carn_acyl_trans. |
| 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. |
Sequences (3)i
Sequence statusi: Complete.
This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P43155-1) [UniParc]FASTAAdd to basket
Also known as: SM-1400
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.
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
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_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. Translation: CAI12869.1. 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] |
| UniGenei | Hs.12068. |
Genome annotation databases
| Ensembli | ENST00000318080; ENSP00000315013; ENSG00000095321. [P43155-1] |
| GeneIDi | 1384. |
| UCSCi | uc004bxh.4. human. [P43155-1] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismSimilar 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. |
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: | June 7, 2017 | |
| This is version 170 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, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - 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
