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Q5R6X1

- PA1B3_PONAB

UniProt

Q5R6X1 - PA1B3_PONAB

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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.
InParanoidiQ5R6X1.
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

        10         20         30         40         50
MSGEENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ
60 70 80 90 100
LMHQCEIWRE LFSPLHALNF GIGGDGTQHV LWRLENGELE HIRPKIVVVW
110 120 130 140 150
VGTNNHGHTA EQVTGGIKAI VQLVNERQPQ ARVVVLDLLP RGQHPNPLRE
160 170 180 190 200
KNQRVNELVR AALAGHPRAH FLDADPGFVH SDGTISHHDM YDYLHLSRLG
210 220 230
YAPVCRALHS LLLRLLAQDQ GQGAPLLDPA P
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.
InParanoidi Q5R6X1.
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 29, 2014
This is version 50 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