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P32738

- CLAT_RAT

UniProt

P32738 - CLAT_RAT

Protein

Choline O-acetyltransferase

Gene

Chat

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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

    MPILEKAPQK MPVKASSWEE LDLPKLPVPP LQQTLATYLQ CMQHLVPEEQ    50
    FRKSQAIVKR FGAPGGLGET LQEKLLERQE KTANWVSEYW LNDMYLNNRL 100
    ALPVNSSPAV IFARQHFQDT NDQLRFAACL ISGVLSYKTL LDSHSLPTDW 150
    AKGQLSGQPL CMKQYYRLFS SYRLPGHTQD TLVAQKSSIM PEPEHVIVAC 200
    CNQFFVLDVV INFRRLSEGD LFTQLRKIVK MASNEDERLP PIGLLTSDGR 250
    SEWAKARTVL LKDSTNRDSL DMIERCICLV CLDGPGTGEL SDTHRALQLL 300
    HGGGCSLNGA NRWYDKSLQF VVGRDGTCGV VCEHSPFDGI VLVQCTEHLL 350
    KHMMTSNKKL VRADSVSELP APRRLRLKCS PETQGHLASS AEKLQRIVKN 400
    LDFIVYKFDN YGKTFIKKQK YSPDGFIQVA LQLAYYRLYQ RLVPTYESAS 450
    IRRFQEGRVD NIRSATPEAL AFVQAMTDHK AAMPASEKLQ LLQTAMQAHK 500
    QYTVMAITGM AIDNHLLALR ELARDLCKEP PEMFMDETYL MSNRFVLSTS 550
    QVPTTMEMFC CYGPVVPNGN GACYNPQPEA ITFCISSFHS CKETSSVEFA 600
    EAVGASLVDM RDLCSSRQPA DSKPPAPKEK ARGPSQAKQS 640
    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