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Carnitine O-acetyltransferase (Carnitine acetylase) (EC 2.3.1.7) (Carnitine acetyltransferase) (CAT) (CrAT)

 CACP_HUMAN              Reviewed;         626 AA.
P43155; Q5T952; Q9BW16;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 5.
27-SEP-2017, entry version 172.
RecName: Full=Carnitine O-acetyltransferase;
Short=Carnitine acetylase;
EC=2.3.1.7;
AltName: Full=Carnitine acetyltransferase;
Short=CAT;
Short=CrAT;
Name=CRAT; Synonyms=CAT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
MET-372.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
MET-372.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 (ISOFORMS 1 AND 2), AND
ALTERNATIVE SPLICING.
PubMed=7945262; DOI=10.1042/bj3030037;
Corti O., DiDonato S., Finocchiaro G.;
"Divergent sequences in the 5' region of cDNA suggest alternative
splicing as a mechanism for the generation of carnitine
acetyltransferases with different subcellular localizations.";
Biochem. J. 303:37-41(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-626 (ISOFORM 1), PARTIAL PROTEIN
SEQUENCE, AND VARIANT MET-372.
PubMed=7829107; DOI=10.1006/geno.1994.1463;
Corti O., Finocchiaro G., Rossi E., Zuffardi O., Didonato S.;
"Molecular cloning of cDNAs encoding human carnitine acetyltransferase
and mapping of the corresponding gene to chromosome 9q34.1.";
Genomics 23:94-99(1994).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-261 AND LYS-268, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[9]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 35-626, AND SUBUNIT.
PubMed=12562770; DOI=10.1074/jbc.M212356200;
Wu D., Govindasamy L., Lian W., Gu Y., Kukar T., Agbandje-McKenna M.,
McKenna R.;
"Structure of human carnitine acetyltransferase. Molecular basis for
fatty acyl transfer.";
J. Biol. Chem. 278:13159-13165(2003).
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 35-626 IN COMPLEX WITH
CARNITINE, AND MUTAGENESIS OF TYR-452; THR-465; ARG-518 AND PHE-566.
PubMed=15099582; DOI=10.1016/j.jsb.2004.01.011;
Govindasamy L., Kukar T., Lian W., Pedersen B., Gu Y.,
Agbandje-McKenna M., Jin S., McKenna R., Wu D.;
"Structural and mutational characterization of L-carnitine binding to
human carnitine acetyltransferase.";
J. Struct. Biol. 146:416-424(2004).
-!- FUNCTION: 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 ACTIVITY: Acetyl-CoA + carnitine = CoA + O-
acetylcarnitine.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12562770,
ECO:0000269|PubMed:15099582}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000305}.
Peroxisome {ECO:0000305}. Mitochondrion inner membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Matrix
side {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 2: Peroxisome {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=SM-1400;
IsoId=P43155-1; Sequence=Displayed;
Name=2; Synonyms=SM-1200;
IsoId=P43155-2; Sequence=VSP_000792;
Note=No experimental confirmation available.;
Name=3;
IsoId=P43155-3; Sequence=VSP_012798;
-!- TISSUE SPECIFICITY: Mostly in skeletal muscle, less in heart,
liver and pancreas, only weakly detectable in brain, placenta,
lung and kidney.
-!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BT006801; AAP35447.1; -; mRNA.
EMBL; AL158151; CAI12869.1; -; Genomic_DNA.
EMBL; BC000723; AAH00723.1; -; mRNA.
EMBL; X79825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X79827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X78706; CAA55359.1; -; mRNA.
CCDS; CCDS6919.1; -. [P43155-1]
PIR; A55720; A55720.
RefSeq; XP_005251765.1; XM_005251708.3. [P43155-2]
UniGene; Hs.12068; -.
PDB; 1NM8; X-ray; 1.60 A; A=35-626.
PDB; 1S5O; X-ray; 1.80 A; A=35-626.
PDBsum; 1NM8; -.
PDBsum; 1S5O; -.
DisProt; DP00305; -.
ProteinModelPortal; P43155; -.
SMR; P43155; -.
BioGrid; 107774; 7.
IntAct; P43155; 10.
STRING; 9606.ENSP00000315013; -.
BindingDB; P43155; -.
ChEMBL; CHEMBL3184; -.
DrugBank; DB02648; (3-Carboxy-2-(R)-Hydroxy-Propyl)-Trimethyl-Ammonium.
DrugBank; DB01992; Coenzyme A.
DrugBank; DB00583; L-Carnitine.
SwissLipids; SLP:000001053; -.
SwissLipids; SLP:000001057; -. [P43155-1]
SwissLipids; SLP:000001058; -. [P43155-2]
TCDB; 4.C.2.1.1; the carnitine o-acyl transferase (crat) family.
iPTMnet; P43155; -.
PhosphoSitePlus; P43155; -.
BioMuta; CRAT; -.
DMDM; 215274265; -.
EPD; P43155; -.
MaxQB; P43155; -.
PaxDb; P43155; -.
PeptideAtlas; P43155; -.
PRIDE; P43155; -.
DNASU; 1384; -.
Ensembl; ENST00000318080; ENSP00000315013; ENSG00000095321. [P43155-1]
GeneID; 1384; -.
UCSC; uc004bxh.4; human. [P43155-1]
CTD; 1384; -.
DisGeNET; 1384; -.
EuPathDB; HostDB:ENSG00000095321.16; -.
GeneCards; CRAT; -.
H-InvDB; HIX0169130; -.
HGNC; HGNC:2342; CRAT.
HPA; HPA019230; -.
HPA; HPA020260; -.
HPA; HPA022815; -.
MalaCards; CRAT; -.
MIM; 600184; gene.
neXtProt; NX_P43155; -.
OpenTargets; ENSG00000095321; -.
PharmGKB; PA26862; -.
eggNOG; KOG3717; Eukaryota.
eggNOG; ENOG410XNZ9; LUCA.
GeneTree; ENSGT00760000119220; -.
HOGENOM; HOG000233845; -.
HOVERGEN; HBG107717; -.
InParanoid; P43155; -.
OMA; WWNDAAY; -.
OrthoDB; EOG091G038F; -.
PhylomeDB; P43155; -.
TreeFam; TF313836; -.
BioCyc; MetaCyc:HS01816-MONOMER; -.
BRENDA; 2.3.1.7; 2681.
Reactome; R-HSA-389887; Beta-oxidation of pristanoyl-CoA.
SABIO-RK; P43155; -.
ChiTaRS; CRAT; human.
EvolutionaryTrace; P43155; -.
GeneWiki; CRAT_(gene); -.
GenomeRNAi; 1384; -.
PRO; PR:P43155; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000095321; -.
CleanEx; HS_CRAT; -.
ExpressionAtlas; P43155; baseline and differential.
Genevisible; P43155; HS.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0004092; F:carnitine O-acetyltransferase activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0019254; P:carnitine metabolic process, CoA-linked; IDA:UniProtKB.
GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome.
GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
InterPro; IPR000542; Carn_acyl_trans.
PANTHER; PTHR22589; PTHR22589; 1.
Pfam; PF00755; Carn_acyltransf; 1.
PROSITE; PS00439; ACYLTRANSF_C_1; 1.
PROSITE; PS00440; ACYLTRANSF_C_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Acyltransferase; Alternative splicing;
Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion;
Mitochondrion inner membrane; Peroxisome; Polymorphism;
Reference proteome; Transferase; Transport.
CHAIN 1 626 Carnitine O-acetyltransferase.
/FTId=PRO_0000210172.
REGION 423 430 Coenzyme A binding. {ECO:0000250}.
MOTIF 624 626 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 343 343 Proton acceptor. {ECO:0000305}.
BINDING 419 419 Coenzyme A. {ECO:0000250}.
BINDING 452 452 Carnitine. {ECO:0000269|PubMed:15099582}.
BINDING 454 454 Carnitine. {ECO:0000269|PubMed:15099582}.
BINDING 456 456 Coenzyme A; via amide nitrogen.
{ECO:0000250}.
BINDING 465 465 Carnitine. {ECO:0000269|PubMed:15099582}.
BINDING 504 504 Coenzyme A. {ECO:0000250}.
BINDING 555 555 Coenzyme A; via carbonyl oxygen.
{ECO:0000250}.
MOD_RES 93 93 N6-succinyllysine.
{ECO:0000250|UniProtKB:P47934}.
MOD_RES 261 261 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 261 261 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P47934}.
MOD_RES 268 268 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 21 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_000792.
VAR_SEQ 282 363 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.1}.
/FTId=VSP_012798.
VARIANT 372 372 L -> M (in dbSNP:rs3118635).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7829107,
ECO:0000269|Ref.1}.
/FTId=VAR_047780.
VARIANT 624 624 A -> P (in dbSNP:rs17459086).
/FTId=VAR_047781.
MUTAGEN 452 452 Y->A: Increases the KM for carnitine 100-
fold. {ECO:0000269|PubMed:15099582}.
MUTAGEN 452 452 Y->F: Increases the KM for carnitine 320-
fold and reduces enzyme activity 10000-
fold. {ECO:0000269|PubMed:15099582}.
MUTAGEN 465 465 T->A: Increases the KM for carnitine
almost 70-fold and reduces enzyme
activity 450-fold.
{ECO:0000269|PubMed:15099582}.
MUTAGEN 518 518 R->Q: Increases the KM for carnitine 230-
fold and reduces enzyme activity almost
100-fold. {ECO:0000269|PubMed:15099582}.
MUTAGEN 566 566 F->A: Increases the KM for carnitine 18-
fold and reduces enzyme activity 100-
fold. {ECO:0000269|PubMed:15099582}.
MUTAGEN 566 566 F->Y: No effect.
{ECO:0000269|PubMed:15099582}.
CONFLICT 88 88 E -> G (in Ref. 5; CAA55359).
{ECO:0000305}.
CONFLICT 349 349 P -> F (in Ref. 5; CAA55359).
{ECO:0000305}.
CONFLICT 517 517 D -> G (in Ref. 5; CAA55359).
{ECO:0000305}.
CONFLICT 534 534 M -> T (in Ref. 5; CAA55359).
{ECO:0000305}.
HELIX 43 54 {ECO:0000244|PDB:1NM8}.
TURN 55 57 {ECO:0000244|PDB:1NM8}.
HELIX 60 74 {ECO:0000244|PDB:1NM8}.
HELIX 79 93 {ECO:0000244|PDB:1NM8}.
STRAND 94 96 {ECO:0000244|PDB:1NM8}.
HELIX 99 106 {ECO:0000244|PDB:1NM8}.
TURN 107 109 {ECO:0000244|PDB:1NM8}.
TURN 116 118 {ECO:0000244|PDB:1NM8}.
STRAND 121 123 {ECO:0000244|PDB:1NM8}.
HELIX 132 154 {ECO:0000244|PDB:1NM8}.
HELIX 171 175 {ECO:0000244|PDB:1NM8}.
STRAND 179 182 {ECO:0000244|PDB:1NM8}.
STRAND 185 187 {ECO:0000244|PDB:1NM8}.
STRAND 189 192 {ECO:0000244|PDB:1NM8}.
STRAND 196 198 {ECO:0000244|PDB:1NM8}.
STRAND 202 207 {ECO:0000244|PDB:1NM8}.
STRAND 210 215 {ECO:0000244|PDB:1NM8}.
HELIX 226 238 {ECO:0000244|PDB:1NM8}.
HELIX 248 253 {ECO:0000244|PDB:1NM8}.
HELIX 256 266 {ECO:0000244|PDB:1NM8}.
HELIX 270 281 {ECO:0000244|PDB:1NM8}.
STRAND 285 289 {ECO:0000244|PDB:1NM8}.
STRAND 297 299 {ECO:0000244|PDB:1S5O}.
HELIX 300 310 {ECO:0000244|PDB:1NM8}.
TURN 314 319 {ECO:0000244|PDB:1NM8}.
STRAND 325 332 {ECO:0000244|PDB:1NM8}.
STRAND 337 341 {ECO:0000244|PDB:1NM8}.
HELIX 348 363 {ECO:0000244|PDB:1NM8}.
STRAND 379 381 {ECO:0000244|PDB:1NM8}.
HELIX 387 406 {ECO:0000244|PDB:1NM8}.
STRAND 407 414 {ECO:0000244|PDB:1NM8}.
HELIX 420 424 {ECO:0000244|PDB:1NM8}.
HELIX 429 445 {ECO:0000244|PDB:1NM8}.
STRAND 451 456 {ECO:0000244|PDB:1NM8}.
STRAND 465 469 {ECO:0000244|PDB:1NM8}.
HELIX 473 482 {ECO:0000244|PDB:1NM8}.
HELIX 489 511 {ECO:0000244|PDB:1NM8}.
HELIX 517 529 {ECO:0000244|PDB:1NM8}.
HELIX 536 539 {ECO:0000244|PDB:1NM8}.
HELIX 541 546 {ECO:0000244|PDB:1NM8}.
STRAND 550 555 {ECO:0000244|PDB:1NM8}.
STRAND 559 561 {ECO:0000244|PDB:1NM8}.
STRAND 563 565 {ECO:0000244|PDB:1NM8}.
STRAND 574 580 {ECO:0000244|PDB:1NM8}.
STRAND 585 592 {ECO:0000244|PDB:1NM8}.
HELIX 600 619 {ECO:0000244|PDB:1NM8}.
SEQUENCE 626 AA; 70858 MW; 51B65E7C94E458D7 CRC64;
MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE
EEWAHTKQLV DEFQASGGVG ERLQKGLERR ARKTENWLSE WWLKTAYLQY RQPVVIYSSP
GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK VMIDNETLPV EYLGGKPLCM NQYYQILSSC
RVPGPKQDTV SNFSKTKKPP THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS
LQTNKEPVGI LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY
RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGPP IVTLLDYVIE
YTKKPELVRS PLVPLPMPKK LRFNITPEIK SDIEKAKQNL SIMIQDLDIT VMVFHHFGKD
FPKSEKLSPD AFIQMALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASMDSLTFVK
AMDDSSVTEH QKVELLRKAV QAHRGYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD
TSYAIAMHFH LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA
ARLAHYLEKA LLDMRALLQS HPRAKL


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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