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Protein

Platelet-activating factor acetylhydrolase IB subunit gamma

Gene

PAFAH1B3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.47. 908.

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 Componenti: Chromosome 18

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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 – 93Combined sources
Beta strandi17 – 204Combined sources
Helixi22 – 3615Combined sources
Beta strandi40 – 467Combined sources
Helixi47 – 504Combined sources
Helixi52 – 554Combined sources
Helixi58 – 614Combined sources
Helixi63 – 653Combined sources
Beta strandi67 – 715Combined sources
Helixi77 – 859Combined sources
Turni86 – 916Combined sources
Beta strandi95 – 1006Combined sources
Helixi110 – 12718Combined sources
Beta strandi132 – 1365Combined sources
Beta strandi142 – 1443Combined sources
Helixi147 – 16418Combined sources
Beta strandi169 – 1724Combined sources
Turni187 – 1893Combined sources
Beta strandi193 – 1964Combined sources
Helixi198 – 21518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InterProiIPR013830. SGNH_hydro.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q29460-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGDENPASK PTPVQDVQGD GRWMSLHHRF VADSKDKEPE VVFIGDSLVQ
60 70 80 90 100
LMHQCEIWRE LFSPLHALNF GIGGDSTQHV LWRLENGELE HIRPKIVVVW
110 120 130 140 150
VGTNNHGHTA EQVTGGIKAI VQLVNERQPQ ARVVVLGLLP RGQHPNPLRE
160 170 180 190 200
KNRRVNELVR AALAGHPRAH FLDADPGFVH SDGTISHHDM YDYLHLSRLG
210 220 230
YTPVCRALHS LLLRLLTQDQ GQGGAPLPEP SP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
D30789 mRNA. Translation: BAA06455.1.
BC120202 mRNA. Translation: AAI20203.1.
PIRiA54754.
RefSeqiNP_777090.1. NM_174665.2.
UniGeneiBt.4040.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

IntActiQ29460. 1 interaction.
MINTiMINT-208804.

Proteomic databases

PaxDbiQ29460.
PRIDEiQ29460.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5050.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi3.1.1.47. 908.

Miscellaneous databases

EvolutionaryTraceiQ29460.
NextBioi20806265.

Family and domain databases

Gene3Di3.40.50.1110. 1 hit.
InterProiIPR013830. SGNH_hydro.
[Graphical view]
SUPFAMiSSF52266. SSF52266. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 111 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.