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Q5R6X1

- PA1B3_PONAB

UniProt

Q5R6X1 - PA1B3_PONAB

Protein

Platelet-activating factor acetylhydrolase IB subunit gamma

Gene

PAFAH1B3

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      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 By similarity.By similarity

    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 – 471By similarity
    Active sitei192 – 1921By similarity
    Active sitei195 – 1951By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW

    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
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 231230Platelet-activating factor acetylhydrolase IB subunit gammaPRO_0000252685Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ5R6X1.

    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 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R6X1.
    SMRiQ5R6X1. Positions 5-215.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG053477.
    KOiK16795.

    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.

    Q5R6X1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGEENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ    50
    LMHQCEIWRE LFSPLHALNF GIGGDGTQHV LWRLENGELE HIRPKIVVVW 100
    VGTNNHGHTA EQVTGGIKAI VQLVNERQPQ ARVVVLDLLP RGQHPNPLRE 150
    KNQRVNELVR AALAGHPRAH FLDADPGFVH SDGTISHHDM YDYLHLSRLG 200
    YAPVCRALHS LLLRLLAQDQ GQGAPLLDPA P 231
    Length:231
    Mass (Da):25,748
    Last modified:December 21, 2004 - v1
    Checksum:iE5A47630AFB13356
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR860358 mRNA. Translation: CAH92489.1.
    RefSeqiNP_001126468.1. NM_001132996.1.
    UniGeneiPab.5941.

    Genome annotation databases

    GeneIDi100173455.
    KEGGipon:100173455.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR860358 mRNA. Translation: CAH92489.1 .
    RefSeqi NP_001126468.1. NM_001132996.1.
    UniGenei Pab.5941.

    3D structure databases

    ProteinModelPortali Q5R6X1.
    SMRi Q5R6X1. Positions 5-215.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5R6X1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100173455.
    KEGGi pon:100173455.

    Organism-specific databases

    CTDi 5050.

    Phylogenomic databases

    HOVERGENi HBG053477.
    KOi K16795.

    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 German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain cortex.

    Entry informationi

    Entry nameiPA1B3_PONAB
    AccessioniPrimary (citable) accession number: Q5R6X1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 49 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3