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Q29460

- PA1B3_BOVIN

UniProt

Q29460 - PA1B3_BOVIN

Protein

Platelet-activating factor acetylhydrolase IB subunit gamma

Gene

PAFAH1B3

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain.

    Catalytic activityi

    1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei47 – 471
    Active sitei192 – 1921
    Active sitei195 – 1951

    GO - Molecular functioni

    1. 1-alkyl-2-acetylglycerophosphocholine esterase activity Source: UniProtKB-EC

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW
    2. spermatogenesis Source: AgBase

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet-activating factor acetylhydrolase IB subunit gamma (EC:3.1.1.47)
    Alternative name(s):
    PAF acetylhydrolase 29 kDa subunit
    Short name:
    PAF-AH 29 kDa subunit
    PAF-AH subunit gamma
    Short name:
    PAFAH subunit gamma
    Gene namesi
    Name:PAFAH1B3
    Synonyms:PAFAHG
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 18

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: AgBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 232231Platelet-activating factor acetylhydrolase IB subunit gammaPRO_0000058154Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ29460.
    PRIDEiQ29460.

    Interactioni

    Subunit structurei

    Cytosolic PAF-AH IB is formed of three subunits of 45 kDa (alpha), 30 kDa (beta) and 29 kDa (gamma). The catalytic activity of the enzyme resides in the beta and gamma subunits, whereas the alpha subunit has regulatory activity. Trimer formation is not essential for the catalytic activity.

    Protein-protein interaction databases

    IntActiQ29460. 1 interaction.
    MINTiMINT-208804.

    Structurei

    Secondary structure

    1
    232
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 93
    Beta strandi17 – 204
    Helixi22 – 3615
    Beta strandi40 – 467
    Helixi47 – 504
    Helixi52 – 554
    Helixi58 – 614
    Helixi63 – 653
    Beta strandi67 – 715
    Helixi77 – 859
    Turni86 – 916
    Beta strandi95 – 1006
    Helixi110 – 12718
    Beta strandi132 – 1365
    Beta strandi142 – 1443
    Helixi147 – 16418
    Beta strandi169 – 1724
    Turni187 – 1893
    Beta strandi193 – 1964
    Helixi198 – 21518

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BWPX-ray2.10A1-232[»]
    1BWQX-ray2.30A1-232[»]
    1BWRX-ray2.40A1-232[»]
    1ES9X-ray1.30A1-232[»]
    1FXWX-ray2.10A1-232[»]
    1WABX-ray1.70A1-232[»]
    3DT6X-ray2.10A1-232[»]
    3DT8X-ray1.85A1-232[»]
    3DT9X-ray1.85A1-232[»]
    ProteinModelPortaliQ29460.
    SMRiQ29460. Positions 5-215.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ29460.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG69837.
    GeneTreeiENSGT00390000016520.
    HOGENOMiHOG000232143.
    HOVERGENiHBG053477.
    InParanoidiQ29460.
    KOiK16795.
    OMAiFAPLHCL.
    OrthoDBiEOG7HB5BS.
    TreeFamiTF323955.

    Family and domain databases

    Gene3Di3.40.50.1110. 1 hit.
    InterProiIPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q29460-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGDENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ    50
    LMHQCEIWRE LFSPLHALNF GIGGDSTQHV LWRLENGELE HIRPKIVVVW 100
    VGTNNHGHTA EQVTGGIKAI VQLVNERQPQ ARVVVLGLLP RGQHPNPLRE 150
    KNRRVNELVR AALAGHPRAH FLDADPGFVH SDGTISHHDM YDYLHLSRLG 200
    YTPVCRALHS LLLRLLTQDQ GQGGAPLPEP SP 232
    Length:232
    Mass (Da):25,865
    Last modified:November 1, 1996 - v1
    Checksum:i81C2CECA8E2204ED
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti79 – 791Missing AA sequence (PubMed:8083218)Curated
    Sequence conflicti150 – 1501E → L AA sequence (PubMed:8083218)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D30789 mRNA. Translation: BAA06455.1.
    BC120202 mRNA. Translation: AAI20203.1.
    PIRiA54754.
    RefSeqiNP_777090.1. NM_174665.2.
    UniGeneiBt.4040.

    Genome annotation databases

    EnsembliENSBTAT00000026366; ENSBTAP00000026366; ENSBTAG00000019787.
    GeneIDi282515.
    KEGGibta:282515.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D30789 mRNA. Translation: BAA06455.1 .
    BC120202 mRNA. Translation: AAI20203.1 .
    PIRi A54754.
    RefSeqi NP_777090.1. NM_174665.2.
    UniGenei Bt.4040.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BWP X-ray 2.10 A 1-232 [» ]
    1BWQ X-ray 2.30 A 1-232 [» ]
    1BWR X-ray 2.40 A 1-232 [» ]
    1ES9 X-ray 1.30 A 1-232 [» ]
    1FXW X-ray 2.10 A 1-232 [» ]
    1WAB X-ray 1.70 A 1-232 [» ]
    3DT6 X-ray 2.10 A 1-232 [» ]
    3DT8 X-ray 1.85 A 1-232 [» ]
    3DT9 X-ray 1.85 A 1-232 [» ]
    ProteinModelPortali Q29460.
    SMRi Q29460. Positions 5-215.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q29460. 1 interaction.
    MINTi MINT-208804.

    Proteomic databases

    PaxDbi Q29460.
    PRIDEi Q29460.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000026366 ; ENSBTAP00000026366 ; ENSBTAG00000019787 .
    GeneIDi 282515.
    KEGGi bta:282515.

    Organism-specific databases

    CTDi 5050.

    Phylogenomic databases

    eggNOGi NOG69837.
    GeneTreei ENSGT00390000016520.
    HOGENOMi HOG000232143.
    HOVERGENi HBG053477.
    InParanoidi Q29460.
    KOi K16795.
    OMAi FAPLHCL.
    OrthoDBi EOG7HB5BS.
    TreeFami TF323955.

    Miscellaneous databases

    EvolutionaryTracei Q29460.
    NextBioi 20806265.

    Family and domain databases

    Gene3Di 3.40.50.1110. 1 hit.
    InterProi IPR013831. SGNH_hydro-type_esterase_dom.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The catalytic subunit of bovine brain platelet-activating factor acetylhydrolase is a novel type of serine esterase."
      Hattori M., Adachi H., Tsujimoto M., Arai H., Inoue K.
      J. Biol. Chem. 269:23150-23155(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 38-85; 96-111 AND 119-151.
      Tissue: Brain.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Fetal brain.
    3. "Brain acetylhydrolase that inactivates platelet-activating factor is a G-protein-like trimer."
      Ho Y.S., Swenson L., Derewenda U., Serre L., Wei Y., Dauter Z., Hattori M., Adachi T., Aoki J., Arai H., Inoue K., Derewenda Z.S.
      Nature 385:89-93(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

    Entry informationi

    Entry nameiPA1B3_BOVIN
    AccessioniPrimary (citable) accession number: Q29460
    Secondary accession number(s): Q0VCF0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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