P68401 (PA1B2_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 67.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
| ||||
| Organism | Bos taurus (Bovine) [Reference proteome] | ||||
| Taxonomic identifier | 9913 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 229 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit. |
| Catalytic activity | 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate. |
| Subunit structure | 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. |
| Subcellular location | |
| Sequence similarities | Belongs to the 'GDSL' lipolytic enzyme family. Platelet-activating factor acetylhydrolase IB beta/gamma subunits subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation Lipid metabolism |
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase |
| PTM | Acetylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of macroautophagyInferred from electronic annotation. Source: Compara spermatogenesisInferred from electronic annotation. Source: Compara |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolusInferred from electronic annotation. Source: Compara plasma membraneInferred from electronic annotation. Source: Compara |
| Molecular_function | 1-alkyl-2-acetylglycerophosphocholine esterase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 229 | 228 | Platelet-activating factor acetylhydrolase IB subunit beta | PRO_0000058149 | |||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||||
| Active site | 48 | 1 | By similarity | ||||||||||||||||||||||||||||||||||||||||||
| Active site | 193 | 1 | By similarity | ||||||||||||||||||||||||||||||||||||||||||
| Active site | 196 | 1 | By similarity | ||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | Phosphoserine By similarity | ||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||
| Helix | 8 – 10 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 18 – 21 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 23 – 37 | 15 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 41 – 47 | 7 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 48 – 51 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 52 – 55 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 57 – 62 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 64 – 66 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 68 – 72 | 5 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 78 – 86 | 9 | |||||||||||||||||||||||||||||||||||||||||||
| Turn | 87 – 90 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 96 – 101 | 6 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 111 – 128 | 18 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 133 – 137 | 5 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 143 – 145 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 148 – 163 | 16 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 164 – 173 | 10 | |||||||||||||||||||||||||||||||||||||||||||
| Turn | 188 – 190 | 3 | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 194 – 197 | 4 | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 199 – 216 | 18 | |||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and expression of a cDNA encoding the beta-subunit (30-kDa subunit) of bovine brain platelet-activating factor acetylhydrolase." Hattori M., Adachi H., Aoki J., Tsujimoto M., Arai H., Inoue K. J. Biol. Chem. 270:31345-31352(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-53; 134-152 AND 167-196. Tissue: Brain. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Hypothalamus. |
| [3] | "Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib." Sheffield P.J., McMullen T.W., Li J., Ho Y.S., Garrard S.M., Derewenda U., Derewenda Z.S. Protein Eng. 14:513-519(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). Tissue: Brain. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | D49678 mRNA. Translation: BAA08534.1. BC103452 mRNA. Translation: AAI03453.1. | ||||||||||||
| IPI | IPI00692295. | ||||||||||||
| RefSeq | NP_777089.1. NM_174664.2. | ||||||||||||
| UniGene | Bt.49728. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P68401. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P68401. 1 interaction. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P68401. | ||||||||||||
| PRIDE | P68401. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSBTAT00000007398; ENSBTAP00000007398; ENSBTAG00000005627. | ||||||||||||
| GeneID | 282514. | ||||||||||||
| KEGG | bta:282514. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 5049. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | NOG69837. | ||||||||||||
| GeneTree | ENSGT00390000016520. | ||||||||||||
| HOGENOM | HOG000232143. | ||||||||||||
| HOVERGEN | HBG053477. | ||||||||||||
| InParanoid | P68401. | ||||||||||||
| KO | K16795. | ||||||||||||
| OMA | LQQYEIW. | ||||||||||||
| OrthoDB | EOG45QHF4. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 3.40.50.1110. 1 hit. | ||||||||||||
| InterPro | IPR013831. SGNH_hydro-type_esterase_dom. [Graphical view] | ||||||||||||
| PROSITE | PS01098. LIPASE_GDSL_SER. False negative. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P68401. | ||||||||||||
| NextBio | 20806264. | ||||||||||||
Entry information
| Entry name | PA1B2_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P68401 Secondary accession number(s): O00687, Q29459, Q3ZBB8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
