Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Choline O-acetyltransferase

Gene

Chat

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.

Catalytic activityi

Acetyl-CoA + choline = CoA + O-acetylcholine.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei334Proton acceptorBy similarity1
Binding sitei450Coenzyme ABy similarity1
Binding sitei551Coenzyme ABy similarity1

GO - Molecular functioni

  • choline binding Source: RGD
  • choline O-acetyltransferase activity Source: RGD

GO - Biological processi

  • acetylcholine biosynthetic process Source: RGD
  • antral ovarian follicle growth Source: RGD
  • memory Source: RGD
  • neurotransmitter biosynthetic process Source: RGD
  • response to drug Source: RGD
  • response to ethanol Source: RGD
  • response to hypoxia Source: RGD
  • response to nutrient Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Neurotransmitter biosynthesis

Enzyme and pathway databases

BRENDAi2.3.1.6. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Choline O-acetyltransferase (EC:2.3.1.6)
Short name:
CHOACTase
Short name:
ChAT
Short name:
Choline acetylase
Gene namesi
Name:Chat
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1304627. Chat.

Subcellular locationi

GO - Cellular componenti

  • neuron projection Source: RGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi453R → A, E or Q: Increases KM for coenzyme A and acetylcholine. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3945.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002101572 – 640Choline O-acetyltransferaseAdd BLAST639

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17PhosphoserineCombined sources1
Modified residuei365PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP32738.
PRIDEiP32738.

PTM databases

iPTMnetiP32738.
PhosphoSitePlusiP32738.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000036251.

Chemistry databases

BindingDBiP32738.

Structurei

Secondary structure

1640
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 42Combined sources12
Helixi43 – 45Combined sources3
Helixi48 – 61Combined sources14
Helixi67 – 81Combined sources15
Beta strandi82 – 84Combined sources3
Helixi87 – 94Combined sources8
Turni95 – 97Combined sources3
Helixi102 – 105Combined sources4
Beta strandi109 – 112Combined sources4
Helixi120 – 143Combined sources24
Beta strandi151 – 153Combined sources3
Beta strandi156 – 158Combined sources3
Helixi165 – 167Combined sources3
Turni168 – 170Combined sources3
Beta strandi171 – 174Combined sources4
Beta strandi177 – 179Combined sources3
Beta strandi181 – 184Combined sources4
Beta strandi188 – 191Combined sources4
Beta strandi195 – 200Combined sources6
Beta strandi203 – 211Combined sources9
Helixi218 – 232Combined sources15
Helixi235 – 237Combined sources3
Helixi242 – 247Combined sources6
Helixi250 – 260Combined sources11
Helixi264 – 274Combined sources11
Beta strandi279 – 282Combined sources4
Helixi292 – 301Combined sources10
Turni305 – 310Combined sources6
Beta strandi316 – 322Combined sources7
Beta strandi328 – 332Combined sources5
Helixi339 – 353Combined sources15
Beta strandi361 – 363Combined sources3
Helixi381 – 400Combined sources20
Beta strandi401 – 408Combined sources8
Helixi413 – 418Combined sources6
Helixi423 – 439Combined sources17
Beta strandi445 – 450Combined sources6
Beta strandi459 – 462Combined sources4
Helixi467 – 474Combined sources8
Beta strandi476 – 479Combined sources4
Beta strandi481 – 483Combined sources3
Helixi485 – 507Combined sources23
Helixi513 – 525Combined sources13
Helixi532 – 535Combined sources4
Helixi537 – 542Combined sources6
Beta strandi546 – 551Combined sources6
Beta strandi555 – 561Combined sources7
Beta strandi570 – 576Combined sources7
Beta strandi581 – 588Combined sources8
Helixi596 – 614Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q6XX-ray2.50A/B1-634[»]
1T1UX-ray1.55A2-640[»]
ProteinModelPortaliP32738.
SMRiP32738.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32738.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni412 – 424Coenzyme A bindingCuratedAdd BLAST13

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
HOGENOMiHOG000233845.
HOVERGENiHBG107717.
InParanoidiP32738.

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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32738-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPILEKAPQK MPVKASSWEE LDLPKLPVPP LQQTLATYLQ CMQHLVPEEQ
60 70 80 90 100
FRKSQAIVKR FGAPGGLGET LQEKLLERQE KTANWVSEYW LNDMYLNNRL
110 120 130 140 150
ALPVNSSPAV IFARQHFQDT NDQLRFAACL ISGVLSYKTL LDSHSLPTDW
160 170 180 190 200
AKGQLSGQPL CMKQYYRLFS SYRLPGHTQD TLVAQKSSIM PEPEHVIVAC
210 220 230 240 250
CNQFFVLDVV INFRRLSEGD LFTQLRKIVK MASNEDERLP PIGLLTSDGR
260 270 280 290 300
SEWAKARTVL LKDSTNRDSL DMIERCICLV CLDGPGTGEL SDTHRALQLL
310 320 330 340 350
HGGGCSLNGA NRWYDKSLQF VVGRDGTCGV VCEHSPFDGI VLVQCTEHLL
360 370 380 390 400
KHMMTSNKKL VRADSVSELP APRRLRLKCS PETQGHLASS AEKLQRIVKN
410 420 430 440 450
LDFIVYKFDN YGKTFIKKQK YSPDGFIQVA LQLAYYRLYQ RLVPTYESAS
460 470 480 490 500
IRRFQEGRVD NIRSATPEAL AFVQAMTDHK AAMPASEKLQ LLQTAMQAHK
510 520 530 540 550
QYTVMAITGM AIDNHLLALR ELARDLCKEP PEMFMDETYL MSNRFVLSTS
560 570 580 590 600
QVPTTMEMFC CYGPVVPNGN GACYNPQPEA ITFCISSFHS CKETSSVEFA
610 620 630 640
EAVGASLVDM RDLCSSRQPA DSKPPAPKEK ARGPSQAKQS
Length:640
Mass (Da):71,864
Last modified:January 23, 2007 - v2
Checksum:iE5FEA20EBBFA2EC6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88488 Genomic DNA. No translation available.
PIRiA48319.
UniGeneiRn.45116.

Genome annotation databases

UCSCiRGD:1304627. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88488 Genomic DNA. No translation available.
PIRiA48319.
UniGeneiRn.45116.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q6XX-ray2.50A/B1-634[»]
1T1UX-ray1.55A2-640[»]
ProteinModelPortaliP32738.
SMRiP32738.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000036251.

Chemistry databases

BindingDBiP32738.
ChEMBLiCHEMBL3945.

PTM databases

iPTMnetiP32738.
PhosphoSitePlusiP32738.

Proteomic databases

PaxDbiP32738.
PRIDEiP32738.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:1304627. rat.

Organism-specific databases

RGDi1304627. Chat.

Phylogenomic databases

eggNOGiKOG3717. Eukaryota.
ENOG410XNZ9. LUCA.
HOGENOMiHOG000233845.
HOVERGENiHBG107717.
InParanoidiP32738.

Enzyme and pathway databases

BRENDAi2.3.1.6. 5301.

Miscellaneous databases

EvolutionaryTraceiP32738.
PROiP32738.

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 nameiCLAT_RAT
AccessioniPrimary (citable) accession number: P32738
Secondary accession number(s): Q63849, Q64342
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.