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Protein

Carnitine O-acetyltransferase

Gene

CRAT

Organism
Homo sapiens (Human)
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 acceptorCurated1
Binding sitei419Coenzyme ABy similarity1
Binding sitei452Carnitine1 Publication1
Binding sitei454Carnitine1 Publication1
Binding sitei456Coenzyme A; via amide nitrogenBy similarity1
Binding sitei465Carnitine1 Publication1
Binding sitei504Coenzyme ABy similarity1
Binding sitei555Coenzyme A; via carbonyl oxygenBy similarity1

GO - Molecular functioni

  • carnitine O-acetyltransferase activity Source: UniProtKB
  • receptor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism, Transport

Enzyme and pathway databases

BioCyciMetaCyc:HS01816-MONOMER.
ZFISH:HS01816-MONOMER.
BRENDAi2.3.1.7. 2681.
ReactomeiR-HSA-389887. Beta-oxidation of pristanoyl-CoA.
R-HSA-390247. Beta-oxidation of very long chain fatty acids.
SABIO-RKP43155.

Protein family/group databases

TCDBi4.C.2.1.1. the carnitine o-acyl transferase (crat) family.

Chemistry databases

SwissLipidsiSLP: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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:2342. CRAT.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi452Y → A: Increases the KM for carnitine 100-fold. 1 Publication1
Mutagenesisi452Y → F: Increases the KM for carnitine 320-fold and reduces enzyme activity 10000-fold. 1 Publication1
Mutagenesisi465T → A: Increases the KM for carnitine almost 70-fold and reduces enzyme activity 450-fold. 1 Publication1
Mutagenesisi518R → Q: Increases the KM for carnitine 230-fold and reduces enzyme activity almost 100-fold. 1 Publication1
Mutagenesisi566F → A: Increases the KM for carnitine 18-fold and reduces enzyme activity 100-fold. 1 Publication1
Mutagenesisi566F → Y: No effect. 1 Publication1

Organism-specific databases

DisGeNETi1384.
MalaCardsiCRAT.
OpenTargetsiENSG00000095321.
PharmGKBiPA26862.

Chemistry databases

ChEMBLiCHEMBL3184.
DrugBankiDB00583. L-Carnitine.

Polymorphism and mutation databases

BioMutaiCRAT.
DMDMi215274265.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002101721 – 626Carnitine O-acetyltransferaseAdd BLAST626

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP43155.
MaxQBiP43155.
PaxDbiP43155.
PeptideAtlasiP43155.
PRIDEiP43155.

PTM databases

iPTMnetiP43155.
PhosphoSitePlusiP43155.

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

BgeeiENSG00000095321.
CleanExiHS_CRAT.
ExpressionAtlasiP43155. baseline and differential.
GenevisibleiP43155. HS.

Organism-specific databases

HPAiHPA019230.
HPA020260.
HPA022815.

Interactioni

Subunit structurei

Monomer.2 Publications

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107774. 4 interactors.
IntActiP43155. 10 interactors.
STRINGi9606.ENSP00000315013.

Chemistry databases

BindingDBiP43155.

Structurei

Secondary structure

1626
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 54Combined sources12
Turni55 – 57Combined sources3
Helixi60 – 74Combined sources15
Helixi79 – 93Combined sources15
Beta strandi94 – 96Combined sources3
Helixi99 – 106Combined sources8
Turni107 – 109Combined sources3
Turni116 – 118Combined sources3
Beta strandi121 – 123Combined sources3
Helixi132 – 154Combined sources23
Helixi171 – 175Combined sources5
Beta strandi179 – 182Combined sources4
Beta strandi185 – 187Combined sources3
Beta strandi189 – 192Combined sources4
Beta strandi196 – 198Combined sources3
Beta strandi202 – 207Combined sources6
Beta strandi210 – 215Combined sources6
Helixi226 – 238Combined sources13
Helixi248 – 253Combined sources6
Helixi256 – 266Combined sources11
Helixi270 – 281Combined sources12
Beta strandi285 – 289Combined sources5
Beta strandi297 – 299Combined sources3
Helixi300 – 310Combined sources11
Turni314 – 319Combined sources6
Beta strandi325 – 332Combined sources8
Beta strandi337 – 341Combined sources5
Helixi348 – 363Combined sources16
Beta strandi379 – 381Combined sources3
Helixi387 – 406Combined sources20
Beta strandi407 – 414Combined sources8
Helixi420 – 424Combined sources5
Helixi429 – 445Combined sources17
Beta strandi451 – 456Combined sources6
Beta strandi465 – 469Combined sources5
Helixi473 – 482Combined sources10
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
1NM8X-ray1.60A35-626[»]
1S5OX-ray1.80A35-626[»]
DisProtiDP00305.
ProteinModelPortaliP43155.
SMRiP43155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43155.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni423 – 430Coenzyme A bindingBy similarity8

Motif

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
GeneTreeiENSGT00760000119220.
HOGENOMiHOG000233845.
HOVERGENiHBG107717.
InParanoidiP43155.
KOiK00624.
OMAiAHINFSL.
OrthoDBiEOG091G038F.
PhylomeDBiP43155.
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]

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.

« Hide

        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
Length:626
Mass (Da):70,858
Last modified:November 25, 2008 - v5
Checksum:i51B65E7C94E458D7
GO
Isoform 2 (identifier: P43155-2) [UniParc]FASTAAdd to basket
Also known as: SM-1200

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Note: No experimental confirmation available.
Show »
Length:605
Mass (Da):68,569
Checksum:i915540218D46D9C7
GO
Isoform 3 (identifier: P43155-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     282-363: Missing.

Show »
Length:544
Mass (Da):61,870
Checksum:i2AD5B9AA49773E5C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti88E → G in CAA55359 (PubMed:7829107).Curated1
Sequence conflicti349P → F in CAA55359 (PubMed:7829107).Curated1
Sequence conflicti517D → G in CAA55359 (PubMed:7829107).Curated1
Sequence conflicti534M → T in CAA55359 (PubMed:7829107).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_047780372L → M.3 PublicationsCorresponds to variant rs3118635dbSNPEnsembl.1
Natural variantiVAR_047781624A → P.Corresponds to variant rs17459086dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0007921 – 21Missing in isoform 2. CuratedAdd BLAST21
Alternative sequenceiVSP_012798282 – 363Missing in isoform 3. 2 PublicationsAdd BLAST82

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.
CCDSiCCDS6919.1. [P43155-1]
PIRiA55720.
RefSeqiNP_000746.2. NM_000755.3.
NP_001244292.1. NM_001257363.1.
XP_005251765.1. XM_005251708.3. [P43155-2]
UniGeneiHs.12068.

Genome annotation databases

EnsembliENST00000318080; ENSP00000315013; ENSG00000095321. [P43155-1]
GeneIDi1384.
KEGGihsa:1384.
UCSCiuc004bxh.4. human. [P43155-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

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.
CCDSiCCDS6919.1. [P43155-1]
PIRiA55720.
RefSeqiNP_000746.2. NM_000755.3.
NP_001244292.1. NM_001257363.1.
XP_005251765.1. XM_005251708.3. [P43155-2]
UniGeneiHs.12068.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NM8X-ray1.60A35-626[»]
1S5OX-ray1.80A35-626[»]
DisProtiDP00305.
ProteinModelPortaliP43155.
SMRiP43155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107774. 4 interactors.
IntActiP43155. 10 interactors.
STRINGi9606.ENSP00000315013.

Chemistry databases

BindingDBiP43155.
ChEMBLiCHEMBL3184.
DrugBankiDB00583. L-Carnitine.
SwissLipidsiSLP:000001053.
SLP:000001057. [P43155-1]
SLP:000001058. [P43155-2]

Protein family/group databases

TCDBi4.C.2.1.1. the carnitine o-acyl transferase (crat) family.

PTM databases

iPTMnetiP43155.
PhosphoSitePlusiP43155.

Polymorphism and mutation databases

BioMutaiCRAT.
DMDMi215274265.

Proteomic databases

EPDiP43155.
MaxQBiP43155.
PaxDbiP43155.
PeptideAtlasiP43155.
PRIDEiP43155.

Protocols and materials databases

DNASUi1384.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318080; ENSP00000315013; ENSG00000095321. [P43155-1]
GeneIDi1384.
KEGGihsa:1384.
UCSCiuc004bxh.4. human. [P43155-1]

Organism-specific databases

CTDi1384.
DisGeNETi1384.
GeneCardsiCRAT.
H-InvDBHIX0169130.
HGNCiHGNC:2342. CRAT.
HPAiHPA019230.
HPA020260.
HPA022815.
MalaCardsiCRAT.
MIMi600184. gene.
neXtProtiNX_P43155.
OpenTargetsiENSG00000095321.
PharmGKBiPA26862.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
GeneTreeiENSGT00760000119220.
HOGENOMiHOG000233845.
HOVERGENiHBG107717.
InParanoidiP43155.
KOiK00624.
OMAiAHINFSL.
OrthoDBiEOG091G038F.
PhylomeDBiP43155.
TreeFamiTF313836.

Enzyme and pathway databases

BioCyciMetaCyc:HS01816-MONOMER.
ZFISH:HS01816-MONOMER.
BRENDAi2.3.1.7. 2681.
ReactomeiR-HSA-389887. Beta-oxidation of pristanoyl-CoA.
R-HSA-390247. Beta-oxidation of very long chain fatty acids.
SABIO-RKP43155.

Miscellaneous databases

ChiTaRSiCRAT. human.
EvolutionaryTraceiP43155.
GeneWikiiCRAT_(gene).
GenomeRNAii1384.
PROiP43155.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000095321.
CleanExiHS_CRAT.
ExpressionAtlasiP43155. baseline and differential.
GenevisibleiP43155. HS.

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_HUMAN
AccessioniPrimary (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: November 2, 2016
This is version 164 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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 proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.