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P32738

- CLAT_RAT

UniProt

P32738 - CLAT_RAT

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Protein

Choline O-acetyltransferase

Gene

Chat

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei334 – 3341Proton acceptorBy similarity
Binding sitei450 – 4501Coenzyme ABy similarity
Binding sitei551 – 5511Coenzyme ABy similarity

GO - Molecular functioni

  1. choline binding Source: RGD
  2. choline O-acetyltransferase activity Source: RGD

GO - Biological processi

  1. acetylcholine biosynthetic process Source: RGD
  2. antral ovarian follicle growth Source: RGD
  3. memory Source: RGD
  4. neurotransmitter biosynthetic process Source: RGD
  5. response to drug Source: RGD
  6. response to ethanol Source: RGD
  7. response to hypoxia Source: RGD
  8. response to nutrient Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Neurotransmitter biosynthesis

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
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1304627. Chat.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi453 – 4531R → A, E or Q: Increases KM for coenzyme A and acetylcholine. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 640639Choline O-acetyltransferasePRO_0000210157Add
BLAST

Proteomic databases

PaxDbiP32738.
PRIDEiP32738.

Expressioni

Gene expression databases

GenevestigatoriP32738.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063149.

Structurei

Secondary structure

1
640
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 4212
Helixi43 – 453
Helixi48 – 6114
Helixi67 – 8115
Beta strandi82 – 843
Helixi87 – 948
Turni95 – 973
Helixi102 – 1054
Beta strandi109 – 1124
Helixi120 – 14324
Beta strandi151 – 1533
Beta strandi156 – 1583
Helixi165 – 1673
Turni168 – 1703
Beta strandi171 – 1744
Beta strandi177 – 1793
Beta strandi181 – 1844
Beta strandi188 – 1914
Beta strandi195 – 2006
Beta strandi203 – 2119
Helixi218 – 23215
Helixi235 – 2373
Helixi242 – 2476
Helixi250 – 26011
Helixi264 – 27411
Beta strandi279 – 2824
Helixi292 – 30110
Turni305 – 3106
Beta strandi316 – 3227
Beta strandi328 – 3325
Helixi339 – 35315
Beta strandi361 – 3633
Helixi381 – 40020
Beta strandi401 – 4088
Helixi413 – 4186
Helixi423 – 43917
Beta strandi445 – 4506
Beta strandi459 – 4624
Helixi467 – 4748
Beta strandi476 – 4794
Beta strandi481 – 4833
Helixi485 – 50723
Helixi513 – 52513
Helixi532 – 5354
Helixi537 – 5426
Beta strandi546 – 5516
Beta strandi555 – 5617
Beta strandi570 – 5767
Beta strandi581 – 5888
Helixi596 – 61419

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q6XX-ray2.50A/B1-634[»]
1T1UX-ray1.55A2-640[»]
ProteinModelPortaliP32738.
SMRiP32738. Positions 20-616.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32738.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni412 – 42413Coenzyme A bindingCuratedAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG70127.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M88488 Genomic DNA. No translation available.
PIRi A48319.
UniGenei Rn.45116.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q6X X-ray 2.50 A/B 1-634 [» ]
1T1U X-ray 1.55 A 2-640 [» ]
ProteinModelPortali P32738.
SMRi P32738. Positions 20-616.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000063149.

Chemistry

BindingDBi P32738.
ChEMBLi CHEMBL3945.

Proteomic databases

PaxDbi P32738.
PRIDEi P32738.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:1304627. rat.

Organism-specific databases

RGDi 1304627. Chat.

Phylogenomic databases

eggNOGi NOG70127.
HOGENOMi HOG000233845.
HOVERGENi HBG107717.
InParanoidi P32738.

Miscellaneous databases

EvolutionaryTracei P32738.
PROi P32738.

Gene expression databases

Genevestigatori P32738.

Family and domain databases

InterProi IPR000542. Carn_acyl_trans.
[Graphical view ]
PANTHERi PTHR22589. PTHR22589. 1 hit.
Pfami PF00755. Carn_acyltransf. 1 hit.
[Graphical view ]
PROSITEi PS00439. ACYLTRANSF_C_1. 1 hit.
PS00440. ACYLTRANSF_C_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complementary DNAs for choline acetyltransferase from spinal cords of rat and mouse: nucleotide sequences, expression in mammalian cells, and in situ hybridization."
    Ishii K., Oda Y., Ichikawa T., Deguchi T.
    Brain Res. Mol. Brain Res. 7:151-159(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Spinal cord.
  2. "Multiple mRNA species of choline acetyltransferase from rat spinal cord."
    Kengaku M., Misawa H., Deguchi T.
    Brain Res. Mol. Brain Res. 18:71-76(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
    Tissue: Spinal cord.
  3. "Identification of an active site arginine in rat choline acetyltransferase by alanine scanning mutagenesis."
    Wu D., Hersh L.B.
    J. Biol. Chem. 270:29111-29116(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-453.
  4. "Structural insights and functional implications of choline acetyltransferase."
    Govindasamy L., Pedersen B., Lian W., Kukar T., Gu Y., Jin S., Agbandje-McKenna M., Wu D., McKenna R.
    J. Struct. Biol. 148:226-235(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), SUBUNIT.
  5. "Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders."
    Cai Y., Cronin C.N., Engel A.G., Ohno K., Hersh L.B., Rodgers D.W.
    EMBO J. 23:2047-2058(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-634 IN COMPLEX WITH COENZYME A.

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: October 1, 2014
This is version 99 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

External Data

Dasty 3