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Q5R4G2

- PA1B2_PONAB

UniProt

Q5R4G2 - PA1B2_PONAB

Protein

Platelet-activating factor acetylhydrolase IB subunit beta

Gene

PAFAH1B2

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 55 (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 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 sitei48 – 481By similarity
    Active sitei193 – 1931By similarity
    Active sitei196 – 1961By 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 beta (EC:3.1.1.47)
    Alternative name(s):
    PAF acetylhydrolase 30 kDa subunit
    Short name:
    PAF-AH 30 kDa subunit
    PAF-AH subunit beta
    Short name:
    PAFAH subunit beta
    Gene namesi
    Name:PAFAH1B2
    Synonyms:PAFAHB
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Chromosome 11

    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 – 229228Platelet-activating factor acetylhydrolase IB subunit betaPRO_0000252683Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiQ5R4G2.

    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

    ProteinModelPortaliQ5R4G2.
    SMRiQ5R4G2. Positions 6-217.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00390000016520.
    HOVERGENiHBG053477.
    InParanoidiQ5R4G2.
    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.

    Q5R4G2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV    50
    QLMQQYEIWR ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV 100
    WVGTNNHENT AEEVAGGIEA IVQLINTRQP QAKIIVLGLL PRGEKPNPLR 150
    QKNAKVNQLL KVSLPKLANV QLLDTDGGFV HSDGAISCHD MFDFLHLTGG 200
    GYAKICKPLH ELIMQLLEET PEEKQTTIA 229
    Length:229
    Mass (Da):25,569
    Last modified:December 21, 2004 - v1
    Checksum:i14CF5D48621AA504
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR861287 mRNA. Translation: CAH93354.1.
    RefSeqiNP_001126974.1. NM_001133502.1.

    Genome annotation databases

    EnsembliENSPPYT00000004652; ENSPPYP00000004476; ENSPPYG00000003907.
    GeneIDi100173993.
    KEGGipon:100173993.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR861287 mRNA. Translation: CAH93354.1 .
    RefSeqi NP_001126974.1. NM_001133502.1.

    3D structure databases

    ProteinModelPortali Q5R4G2.
    SMRi Q5R4G2. Positions 6-217.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5R4G2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSPPYT00000004652 ; ENSPPYP00000004476 ; ENSPPYG00000003907 .
    GeneIDi 100173993.
    KEGGi pon:100173993.

    Organism-specific databases

    CTDi 5049.

    Phylogenomic databases

    GeneTreei ENSGT00390000016520.
    HOVERGENi HBG053477.
    InParanoidi Q5R4G2.
    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 nameiPA1B2_PONAB
    AccessioniPrimary (citable) accession number: Q5R4G2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 55 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