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Q29460

- PA1B3_BOVIN

UniProt

Q29460 - PA1B3_BOVIN

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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

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
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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 18

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: AgBase
  2. extracellular vesicular exosome Source: Ensembl
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 – 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

        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:
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

« 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: October 29, 2014
This is version 105 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