Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Choline O-acetyltransferase (CHOACTase) (ChAT) (Choline acetylase) (EC 2.3.1.6)

 CLAT_HUMAN              Reviewed;         748 AA.
P28329; A2BDF4; A2BDF5; Q16488; Q9BQ23; Q9BQ35; Q9BQE1;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
15-DEC-2009, sequence version 4.
27-SEP-2017, entry version 170.
RecName: Full=Choline O-acetyltransferase;
Short=CHOACTase;
Short=ChAT;
Short=Choline acetylase;
EC=2.3.1.6 {ECO:0000269|PubMed:17144655};
Name=CHAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M), AND VARIANTS GLY-392 AND
MET-461.
TISSUE=Spinal cord;
PubMed=1337937; DOI=10.1016/0169-328X(92)90237-6;
Oda Y., Nakanishi I., Deguchi T.;
"A complementary DNA for human choline acetyltransferase induces two
forms of enzyme with different molecular weights in cultured cells.";
Brain Res. Mol. Brain Res. 16:287-294(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS M; R AND S),
ALTERNATIVE SPLICING, VARIANTS CMS6 PRO-210; ALA-211; THR-305;
CYS-420; LYS-441; GLY-482; LEU-498; LEU-506 AND HIS-560, AND VARIANTS
THR-120; GLY-392 AND MET-461.
PubMed=11172068; DOI=10.1073/pnas.98.4.2017;
Ohno K., Tsujino A., Brengman J.M., Harper C.M., Bajzer Z., Udd B.,
Beyring R., Robb S., Kirkham F.J., Engel A.G.;
"Choline acetyltransferase mutations cause myasthenic syndrome
associated with episodic apnea in humans.";
Proc. Natl. Acad. Sci. U.S.A. 98:2017-2022(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM R), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 108-748 (ISOFORM M), AND VARIANTS
THR-120 AND MET-461.
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 111-669, AND VARIANTS THR-120 AND
MET-461.
PubMed=1388731; DOI=10.1089/dna.1992.11.593;
Lorenzi M.V., Trinidad A.C., Zhang R., Strauss W.L.;
"Two mRNAs are transcribed from the human gene for choline
acetyltransferase.";
DNA Cell Biol. 11:593-603(1992).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-232.
PubMed=1339386; DOI=10.1016/0888-7543(92)90395-9;
Toussaint J.L., Geoffroy V., Schmitt M., Werner A., Garnier J.-M.,
Simoni P., Kempf J.;
"Human choline acetyltransferase (CHAT): partial gene sequence and
potential control regions.";
Genomics 12:412-416(1992).
[8]
PROTEIN SEQUENCE OF 161-182; 271-295; 340-352; 376-382; 404-415;
550-559; 572-583; 620-632; 644-648; 650-662 AND 739-748.
TISSUE=Placenta;
PubMed=3183663; DOI=10.1111/j.1471-4159.1988.tb01166.x;
Hersh L.B., Takane K., Gylys K., Moomaw C., Slaughter C.;
"Conservation of amino acid sequences between human and porcine
choline acetyltransferase.";
J. Neurochem. 51:1843-1845(1988).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 688-738.
TISSUE=Lymphocyte;
PubMed=1784419; DOI=10.1016/0304-3940(91)90299-9;
Cervini R., Rocchi M., DiDonato S., Finocchiaro G.;
"Isolation and sub-chromosomal localization of a DNA fragment of the
human choline acetyltransferase gene.";
Neurosci. Lett. 132:191-194(1991).
[10]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 120-733 IN COMPLEXES WITH
CHOLINE AND ACETYL COENZYME A, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=17144655; DOI=10.1021/bi061536l;
Kim A.-R., Rylett R.J., Shilton B.H.;
"Substrate binding and catalytic mechanism of human choline
acetyltransferase.";
Biochemistry 45:14621-14631(2006).
[11]
VARIANT CMS6 THR-336.
PubMed=12756141; DOI=10.1001/archneur.60.5.761;
Kraner S., Laufenberg I., Strassburg H.M., Sieb J.P., Steinlein O.K.;
"Congenital myasthenic syndrome with episodic apnea in patients
homozygous for a CHAT missense mutation.";
Arch. Neurol. 60:761-763(2003).
-!- FUNCTION: Catalyzes the reversible synthesis of acetylcholine
(ACh) from acetyl CoA and choline at cholinergic synapses.
{ECO:0000269|PubMed:17144655}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + choline = CoA + O-acetylcholine.
{ECO:0000269|PubMed:17144655}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=M; Synonyms=83 kDa;
IsoId=P28329-1; Sequence=Displayed;
Name=S; Synonyms=74 kDa;
IsoId=P28329-2; Sequence=VSP_000790;
Name=R; Synonyms=70 kDa;
IsoId=P28329-3; Sequence=VSP_000791;
-!- DISEASE: Myasthenic syndrome, congenital, 6, presynaptic (CMS6)
[MIM:254210]: A form of congenital myasthenic syndrome, a group of
disorders characterized by failure of neuromuscular transmission,
including pre-synaptic, synaptic, and post-synaptic disorders that
are not of autoimmune origin. Clinical features are easy
fatigability and muscle weakness affecting the axial and limb
muscles (with hypotonia in early-onset forms), the ocular muscles
(leading to ptosis and ophthalmoplegia), and the facial and bulbar
musculature (affecting sucking and swallowing, and leading to
dysphonia). The symptoms fluctuate and worsen with physical
effort. CMS6 affected individuals have myasthenic symptoms since
birth or early infancy, negative tests for anti-AChR antibodies,
and abrupt episodic crises with increased weakness, bulbar
paralysis, and apnea precipitated by undue exertion, fever, or
excitement. CMS6 inheritance is autosomal recessive.
{ECO:0000269|PubMed:11172068, ECO:0000269|PubMed:12756141}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Choline acetyltransferase
entry;
URL="https://en.wikipedia.org/wiki/Choline_acetyltransferase";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; S56138; AAA14245.1; -; mRNA.
EMBL; AF305907; AAK08953.1; -; mRNA.
EMBL; AF305906; AAK08950.1; -; Genomic_DNA.
EMBL; AF305894; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305895; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305896; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305897; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305898; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305899; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305900; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305901; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305902; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305903; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305904; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305905; AAK08950.1; JOINED; Genomic_DNA.
EMBL; AF305908; AAK08954.1; -; mRNA.
EMBL; AF305906; AAK08951.1; -; Genomic_DNA.
EMBL; AF305894; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305895; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305896; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305897; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305898; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305899; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305900; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305901; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305902; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305903; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305904; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305905; AAK08951.1; JOINED; Genomic_DNA.
EMBL; AF305909; AAK08955.1; -; mRNA.
EMBL; AF305906; AAK08952.1; -; Genomic_DNA.
EMBL; AF305894; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AF305895; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AF305896; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AF305897; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AF305898; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AF305899; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AF305900; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AF305901; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AF305902; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AF305903; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AF305904; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AF305905; AAK08952.1; JOINED; Genomic_DNA.
EMBL; AC073366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471187; EAW93086.1; -; Genomic_DNA.
EMBL; BC130615; AAI30616.1; -; mRNA.
EMBL; BC130617; AAI30618.1; -; mRNA.
EMBL; S45018; AAB23557.2; -; mRNA.
EMBL; X56585; CAA39923.1; -; Genomic_DNA.
EMBL; X56879; CAA40201.1; -; Genomic_DNA.
CCDS; CCDS44389.1; -. [P28329-2]
CCDS; CCDS7232.1; -. [P28329-1]
CCDS; CCDS7233.1; -. [P28329-3]
PIR; I52631; A60202.
RefSeq; NP_001136401.1; NM_001142929.1.
RefSeq; NP_001136405.1; NM_001142933.1.
RefSeq; NP_001136406.1; NM_001142934.1.
RefSeq; NP_065574.3; NM_020549.4.
RefSeq; NP_066264.3; NM_020984.3.
RefSeq; NP_066265.3; NM_020985.3.
RefSeq; NP_066266.3; NM_020986.3.
UniGene; Hs.302002; -.
PDB; 2FY2; X-ray; 2.25 A; A=120-733.
PDB; 2FY3; X-ray; 2.27 A; A=120-733.
PDB; 2FY4; X-ray; 2.30 A; A=120-733.
PDB; 2FY5; X-ray; 2.60 A; A=120-733.
PDBsum; 2FY2; -.
PDBsum; 2FY3; -.
PDBsum; 2FY4; -.
PDBsum; 2FY5; -.
ProteinModelPortal; P28329; -.
SMR; P28329; -.
BioGrid; 107528; 2.
STRING; 9606.ENSP00000337103; -.
BindingDB; P28329; -.
ChEMBL; CHEMBL4039; -.
DrugBank; DB00122; Choline.
DrugBank; DB00184; Nicotine.
iPTMnet; P28329; -.
PhosphoSitePlus; P28329; -.
BioMuta; CHAT; -.
DMDM; 281185509; -.
PaxDb; P28329; -.
PeptideAtlas; P28329; -.
PRIDE; P28329; -.
DNASU; 1103; -.
Ensembl; ENST00000337653; ENSP00000337103; ENSG00000070748. [P28329-1]
Ensembl; ENST00000339797; ENSP00000343486; ENSG00000070748. [P28329-3]
Ensembl; ENST00000351556; ENSP00000345878; ENSG00000070748. [P28329-3]
Ensembl; ENST00000395559; ENSP00000378926; ENSG00000070748. [P28329-3]
Ensembl; ENST00000395562; ENSP00000378929; ENSG00000070748. [P28329-2]
GeneID; 1103; -.
KEGG; hsa:1103; -.
UCSC; uc001jhv.1; human. [P28329-1]
CTD; 1103; -.
DisGeNET; 1103; -.
EuPathDB; HostDB:ENSG00000070748.17; -.
GeneCards; CHAT; -.
GeneReviews; CHAT; -.
HGNC; HGNC:1912; CHAT.
HPA; CAB002313; -.
HPA; HPA048547; -.
MalaCards; CHAT; -.
MIM; 118490; gene.
MIM; 254210; phenotype.
neXtProt; NX_P28329; -.
OpenTargets; ENSG00000070748; -.
Orphanet; 98914; Presynaptic congenital myasthenic syndromes.
PharmGKB; PA26448; -.
eggNOG; KOG3717; Eukaryota.
eggNOG; ENOG410XNZ9; LUCA.
GeneTree; ENSGT00760000119220; -.
HOGENOM; HOG000233845; -.
HOVERGEN; HBG107717; -.
InParanoid; P28329; -.
KO; K00623; -.
OMA; DKPMQFV; -.
OrthoDB; EOG091G038F; -.
PhylomeDB; P28329; -.
TreeFam; TF313836; -.
BRENDA; 2.3.1.6; 2681.
Reactome; R-HSA-1483191; Synthesis of PC.
Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
SABIO-RK; P28329; -.
SIGNOR; P28329; -.
EvolutionaryTrace; P28329; -.
GeneWiki; Choline_acetyltransferase; -.
GenomeRNAi; 1103; -.
PRO; PR:P28329; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000070748; -.
CleanEx; HS_CHAT; -.
ExpressionAtlas; P28329; baseline and differential.
Genevisible; P28329; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0004102; F:choline O-acetyltransferase activity; TAS:Reactome.
GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0007269; P:neurotransmitter secretion; TAS:Reactome.
GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
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; Acyltransferase; Alternative splicing;
Complete proteome; Congenital myasthenic syndrome;
Direct protein sequencing; Disease mutation;
Neurotransmitter biosynthesis; Phosphoprotein; Polymorphism;
Reference proteome; Transferase.
CHAIN 1 748 Choline O-acetyltransferase.
/FTId=PRO_0000210154.
REGION 520 532 Coenzyme A binding.
ACT_SITE 442 442 Proton acceptor.
BINDING 558 558 Coenzyme A.
BINDING 659 659 Coenzyme A.
MOD_RES 125 125 Phosphoserine.
{ECO:0000250|UniProtKB:P32738}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000250|UniProtKB:P32738}.
VAR_SEQ 1 118 Missing (in isoform R).
{ECO:0000303|PubMed:11172068,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_000791.
VAR_SEQ 1 95 MGLRTAKKRGLGGGGKWKREEGGGTRGRREVRPACFLQSGG
RGDPGDVGGPAGNPGCSPHPRAATRPPPLPAHTPAHTPEWC
GAASAEAAEPRRA -> MWPECRDEALSTV (in
isoform S).
{ECO:0000303|PubMed:11172068}.
/FTId=VSP_000790.
VARIANT 47 47 D -> E (in dbSNP:rs3810948).
/FTId=VAR_046683.
VARIANT 120 120 A -> T (in dbSNP:rs3810950).
{ECO:0000269|PubMed:11172068,
ECO:0000269|PubMed:1388731,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_011675.
VARIANT 210 210 L -> P (in CMS6; impaired activity;
dbSNP:rs28930071).
{ECO:0000269|PubMed:11172068}.
/FTId=VAR_011666.
VARIANT 211 211 P -> A (in CMS6; impaired activity;
dbSNP:rs121912815).
{ECO:0000269|PubMed:11172068}.
/FTId=VAR_011667.
VARIANT 222 222 R -> P (in dbSNP:rs8178989).
/FTId=VAR_046684.
VARIANT 243 243 L -> F (in dbSNP:rs8178990).
/FTId=VAR_046685.
VARIANT 299 299 P -> L (in dbSNP:rs868749).
/FTId=VAR_046686.
VARIANT 305 305 I -> T (in CMS6; impaired activity;
dbSNP:rs28929482).
{ECO:0000269|PubMed:11172068}.
/FTId=VAR_011668.
VARIANT 336 336 I -> T (in CMS6; dbSNP:rs121912823).
{ECO:0000269|PubMed:12756141}.
/FTId=VAR_038605.
VARIANT 392 392 A -> G. {ECO:0000269|PubMed:11172068,
ECO:0000269|PubMed:1337937}.
/FTId=VAR_011676.
VARIANT 400 400 D -> N (in dbSNP:rs8178991).
/FTId=VAR_046687.
VARIANT 420 420 R -> C (in CMS6; impaired activity;
dbSNP:rs121912822).
{ECO:0000269|PubMed:11172068}.
/FTId=VAR_011669.
VARIANT 441 441 E -> K (in CMS6; completely lack
activity; dbSNP:rs28930070).
{ECO:0000269|PubMed:11172068}.
/FTId=VAR_011670.
VARIANT 461 461 V -> M (in dbSNP:rs4838544).
{ECO:0000269|PubMed:11172068,
ECO:0000269|PubMed:1337937,
ECO:0000269|PubMed:1388731,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_046688.
VARIANT 482 482 R -> G (in CMS6; impaired activity;
dbSNP:rs28929481).
{ECO:0000269|PubMed:11172068}.
/FTId=VAR_011671.
VARIANT 498 498 S -> L (in CMS6; impaired activity;
dbSNP:rs121912821).
{ECO:0000269|PubMed:11172068}.
/FTId=VAR_011672.
VARIANT 506 506 V -> L (in CMS6; impaired activity;
dbSNP:rs121912817).
{ECO:0000269|PubMed:11172068}.
/FTId=VAR_011673.
VARIANT 560 560 R -> H (in CMS6; impaired activity;
dbSNP:rs121912819).
{ECO:0000269|PubMed:11172068}.
/FTId=VAR_011674.
CONFLICT 151 151 R -> Q (in Ref. 7; CAA39923).
{ECO:0000305}.
CONFLICT 261 262 GQ -> PE (in Ref. 1; AAA14245).
{ECO:0000305}.
CONFLICT 396 396 V -> L (in Ref. 6; AAB23557).
{ECO:0000305}.
CONFLICT 434 434 G -> A (in Ref. 1; AAA14245).
{ECO:0000305}.
CONFLICT 529 529 C -> S (in Ref. 6; AAB23557).
{ECO:0000305}.
CONFLICT 567 567 V -> L (in Ref. 6; AAB23557).
{ECO:0000305}.
CONFLICT 629 630 EL -> DV (in Ref. 6; AAB23557).
{ECO:0000305}.
CONFLICT 664 664 T -> M (in Ref. 6; AAB23557).
{ECO:0000305}.
HELIX 139 150 {ECO:0000244|PDB:2FY2}.
HELIX 151 153 {ECO:0000244|PDB:2FY2}.
HELIX 156 169 {ECO:0000244|PDB:2FY2}.
HELIX 175 189 {ECO:0000244|PDB:2FY2}.
STRAND 190 192 {ECO:0000244|PDB:2FY5}.
HELIX 195 202 {ECO:0000244|PDB:2FY2}.
TURN 203 205 {ECO:0000244|PDB:2FY2}.
HELIX 210 213 {ECO:0000244|PDB:2FY2}.
STRAND 217 219 {ECO:0000244|PDB:2FY2}.
HELIX 228 250 {ECO:0000244|PDB:2FY2}.
STRAND 261 263 {ECO:0000244|PDB:2FY4}.
STRAND 265 267 {ECO:0000244|PDB:2FY4}.
HELIX 271 275 {ECO:0000244|PDB:2FY2}.
STRAND 276 282 {ECO:0000244|PDB:2FY2}.
STRAND 285 287 {ECO:0000244|PDB:2FY2}.
STRAND 289 292 {ECO:0000244|PDB:2FY2}.
STRAND 300 308 {ECO:0000244|PDB:2FY2}.
STRAND 311 319 {ECO:0000244|PDB:2FY2}.
HELIX 326 340 {ECO:0000244|PDB:2FY2}.
HELIX 343 345 {ECO:0000244|PDB:2FY2}.
HELIX 350 355 {ECO:0000244|PDB:2FY2}.
HELIX 358 369 {ECO:0000244|PDB:2FY2}.
HELIX 372 382 {ECO:0000244|PDB:2FY2}.
STRAND 387 390 {ECO:0000244|PDB:2FY2}.
HELIX 400 409 {ECO:0000244|PDB:2FY2}.
TURN 413 418 {ECO:0000244|PDB:2FY2}.
STRAND 424 430 {ECO:0000244|PDB:2FY2}.
STRAND 436 440 {ECO:0000244|PDB:2FY2}.
STRAND 442 444 {ECO:0000244|PDB:2FY3}.
HELIX 447 461 {ECO:0000244|PDB:2FY2}.
HELIX 489 508 {ECO:0000244|PDB:2FY2}.
STRAND 509 516 {ECO:0000244|PDB:2FY2}.
HELIX 521 525 {ECO:0000244|PDB:2FY2}.
TURN 526 528 {ECO:0000244|PDB:2FY2}.
HELIX 531 547 {ECO:0000244|PDB:2FY2}.
STRAND 553 558 {ECO:0000244|PDB:2FY2}.
STRAND 567 569 {ECO:0000244|PDB:2FY2}.
HELIX 575 585 {ECO:0000244|PDB:2FY2}.
HELIX 587 589 {ECO:0000244|PDB:2FY2}.
HELIX 593 615 {ECO:0000244|PDB:2FY2}.
HELIX 621 634 {ECO:0000244|PDB:2FY2}.
HELIX 640 643 {ECO:0000244|PDB:2FY2}.
HELIX 645 650 {ECO:0000244|PDB:2FY2}.
STRAND 654 659 {ECO:0000244|PDB:2FY2}.
STRAND 663 665 {ECO:0000244|PDB:2FY2}.
STRAND 667 669 {ECO:0000244|PDB:2FY2}.
STRAND 678 684 {ECO:0000244|PDB:2FY2}.
STRAND 689 696 {ECO:0000244|PDB:2FY2}.
HELIX 704 722 {ECO:0000244|PDB:2FY2}.
SEQUENCE 748 AA; 82536 MW; A902364081915391 CRC64;
MGLRTAKKRG LGGGGKWKRE EGGGTRGRRE VRPACFLQSG GRGDPGDVGG PAGNPGCSPH
PRAATRPPPL PAHTPAHTPE WCGAASAEAA EPRRAGPHLC IPAPGLTKTP ILEKVPRKMA
AKTPSSEESG LPKLPVPPLQ QTLATYLQCM RHLVSEEQFR KSQAIVQQFG APGGLGETLQ
QKLLERQEKT ANWVSEYWLN DMYLNNRLAL PVNSSPAVIF ARQHFPGTDD QLRFAASLIS
GVLSYKALLD SHSIPTDCAK GQLSGQPLCM KQYYGLFSSY RLPGHTQDTL VAQNSSIMPE
PEHVIVACCN QFFVLDVVIN FRRLSEGDLF TQLRKIVKMA SNEDERLPPI GLLTSDGRSE
WAEARTVLVK DSTNRDSLDM IERCICLVCL DAPGGVELSD THRALQLLHG GGYSKNGANR
WYDKSLQFVV GRDGTCGVVC EHSPFDGIVL VQCTEHLLKH VTQSSRKLIR ADSVSELPAP
RRLRWKCSPE IQGHLASSAE KLQRIVKNLD FIVYKFDNYG KTFIKKQKCS PDAFIQVALQ
LAFYRLHRRL VPTYESASIR RFQEGRVDNI RSATPEALAF VRAVTDHKAA VPASEKLLLL
KDAIRAQTAY TVMAITGMAI DNHLLALREL ARAMCKELPE MFMDETYLMS NRFVLSTSQV
PTTTEMFCCY GPVVPNGYGA CYNPQPETIL FCISSFHSCK ETSSSKFAKA VEESLIDMRD
LCSLLPPTES KPLATKEKAT RPSQGHQP


Related products :

Catalog number Product name Quantity
U1428h CLIA ChAT,CHAT,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Homo sapiens,Human 96T
E1428h ELISA ChAT,CHAT,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Homo sapiens,Human 96T
E1428h ELISA kit ChAT,CHAT,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Homo sapiens,Human 96T
E1428r ELISA kit ChAT,Chat,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Rat,Rattus norvegicus 96T
U1428m CLIA ChAT,Chat,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Mouse,Mus musculus 96T
E1428m ELISA kit ChAT,Chat,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Mouse,Mus musculus 96T
U1428r CLIA ChAT,Chat,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Rat,Rattus norvegicus 96T
E1428m ELISA ChAT,Chat,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Mouse,Mus musculus 96T
E1428r ELISA ChAT,Chat,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Rat,Rattus norvegicus 96T
E1428p ELISA ChAT,CHAT,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Pig,Sus scrofa 96T
E1428p ELISA kit ChAT,CHAT,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Pig,Sus scrofa 96T
U1428p CLIA ChAT,CHAT,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Pig,Sus scrofa 96T
E1428c ELISA ChAT,CHAT,Chicken,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Gallus gallus 96T
E1428c ELISA kit ChAT,CHAT,Chicken,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Gallus gallus 96T
U1428c CLIA ChAT,CHAT,Chicken,CHOACTase,Choline acetylase,Choline O-acetyltransferase,Gallus gallus 96T
DL-ChAT-Hu Human Choline Acetyltransferase (ChAT) ELISA Kit 96T
DL-ChAT-Mu Mouse Choline Acetyltransferase (ChAT) ELISA Kit 96T
DL-ChAT-Ra Rat Choline Acetyltransferase (ChAT) ELISA Kit 96T
E0725Ra Rat Choline acetyltransferase,ChAT ELISA Kit 96T
201-11-0726 Rat Choline acetyltransferase,ChAT ELISA Kit 96T
E02C0749 Rat Choline acetyltransferase ELISA, ChAT
E0724Ra Rat Choline acetyltransferase,ChAT ELISA Kit 48T
CHCHD10 CHAT Gene choline O-acetyltransferase
E91929Ra ELISA Kit for Choline Acetyltransferase (ChAT) 96T/Kit
YHB0221Ra Rat Choline acetyltransferase,ChAT ELISA Kit 48T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
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




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur