P43033 · LIS1_BOVIN
- ProteinPlatelet-activating factor acetylhydrolase IB subunit beta
- GenePAFAH1B1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids410 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in the PAF inactivation (PubMed:10542206).
Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (PubMed:10542206).
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing (By similarity).
Required for pronuclear migration during fertilization. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (By similarity).
May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity).
Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (PubMed:10542206).
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing (By similarity).
Required for pronuclear migration during fertilization. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (By similarity).
May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity).
Miscellaneous
Originally the subunits of the type I platelet-activating factor (PAF) acetylhydrolase was named alpha (PAFAH1B1), beta (PAFAH1B2) and gamma (PAFAH1B3) (By similarity).
Now these subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) and alpha1 (PAFAH1B3) respectively (By similarity).
Now these subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) and alpha1 (PAFAH1B3) respectively (By similarity).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 1-alkyl-2-acetylglycerophosphocholine esterase complex | |
Cellular Component | centrosome | |
Cellular Component | cytosol | |
Cellular Component | microtubule | |
Cellular Component | microtubule associated complex | |
Cellular Component | nuclear membrane | |
Cellular Component | spindle | |
Molecular Function | dynactin binding | |
Molecular Function | dynein complex binding | |
Molecular Function | heparin binding | |
Molecular Function | microtubule binding | |
Molecular Function | phospholipase binding | |
Molecular Function | protein heterodimerization activity | |
Biological Process | cell differentiation | |
Biological Process | cell division | |
Biological Process | establishment of mitotic spindle orientation | |
Biological Process | lipid catabolic process | |
Biological Process | microtubule sliding | |
Biological Process | nervous system development | |
Biological Process | platelet activating factor metabolic process | |
Biological Process | reelin-mediated signaling pathway |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended namePlatelet-activating factor acetylhydrolase IB subunit beta
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP43033
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the plus end of microtubules and to the centrosome. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes (By similarity).
May localize to the nuclear membrane
May localize to the nuclear membrane
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 149 | Loss of binding to the catalytic dimers. Loss of the ability to regulate PAF-AH (I) activity. | ||||
Sequence: H → R |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000051060 | 1-410 | Platelet-activating factor acetylhydrolase IB subunit beta | |||
Sequence: MVLSQRQRDELNRAIADYLRSNGYEAAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVEDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR | ||||||
Modified residue | 53 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 109 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Expression
Developmental stage
Expression increases during fertilization of the oocyte.
Interaction
Subunit
Can self-associate. Component of the cytosolic PAF-AH (I) heterotetrameric enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2 (alpha2) and PAFAH1B3 (alpha1) subunits. The catalytic activity of the enzyme resides in the alpha1 (PAFAH1B3) and alpha2 (PAFAH1B2) subunits, whereas the beta subunit (PAFAH1B1) has regulatory activity. Trimer formation is not essential for the catalytic activity (PubMed:10542206).
Interacts with the catalytic dimer of PAF-AH (I) heterotetrameric enzyme: interacts with PAFAH1B2 homodimer (alpha2/alpha2 homodimer), PAFAH1B3 homodimer (alpha1/alpha1 homodimer) and PAFAH1B2-PAFAH1B3 heterodimer (alpha2/alpha1 heterodimer) (PubMed:10940388).
Interacts with DCX, IQGAP1, KATNB1, NDEL1, NUDC and RSN. Interacts with DISC1, and this interaction is enhanced by NDEL1. Interacts with DAB1 when DAB1 is phosphorylated in response to RELN/reelin signaling (By similarity).
Interacts with dynein and NDE1 (PubMed:10940388, PubMed:11056532).
Interacts with dynactin (PubMed:11056532, PubMed:14584027).
Interacts with the catalytic dimer of PAF-AH (I) heterotetrameric enzyme: interacts with PAFAH1B2 homodimer (alpha2/alpha2 homodimer), PAFAH1B3 homodimer (alpha1/alpha1 homodimer) and PAFAH1B2-PAFAH1B3 heterodimer (alpha2/alpha1 heterodimer) (PubMed:10940388).
Interacts with DCX, IQGAP1, KATNB1, NDEL1, NUDC and RSN. Interacts with DISC1, and this interaction is enhanced by NDEL1. Interacts with DAB1 when DAB1 is phosphorylated in response to RELN/reelin signaling (By similarity).
Interacts with dynein and NDE1 (PubMed:10940388, PubMed:11056532).
Interacts with dynactin (PubMed:11056532, PubMed:14584027).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P43033 | Nde1 Q9ES39 | 2 | EBI-1007886, EBI-1007897 | |
XENO | P43033 | Pafah1b2 O35264 | 2 | EBI-1007886, EBI-915500 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, coiled coil, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-38 | Required for self-association and interaction with PAFAH1B2 and PAFAH1B3 | ||||
Sequence: MVLSQRQRDELNRAIADYLRSNGYEAAYSVFKKEAELD | ||||||
Region | 1-66 | Interaction with NDE1 | ||||
Sequence: MVLSQRQRDELNRAIADYLRSNGYEAAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVM | ||||||
Region | 1-102 | Interaction with NDEL1 | ||||
Sequence: MVLSQRQRDELNRAIADYLRSNGYEAAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKY | ||||||
Domain | 7-39 | LisH | ||||
Sequence: QRDELNRAIADYLRSNGYEAAYSVFKKEAELDM | ||||||
Coiled coil | 56-82 | |||||
Sequence: TSVIRLQKKVMELESKLNEAKEEFTSG | ||||||
Region | 83-410 | Interaction with dynein and dynactin | ||||
Sequence: GPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVEDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR | ||||||
Repeat | 106-147 | WD 1 | ||||
Sequence: GHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLK | ||||||
Repeat | 148-187 | WD 2 | ||||
Sequence: GHTDSVEDISFDHSGKLLASCSADMTIKLWDFQGFECIRT | ||||||
Repeat | 190-229 | WD 3 | ||||
Sequence: GHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKT | ||||||
Repeat | 232-271 | WD 4 | ||||
Sequence: GHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAE | ||||||
Repeat | 274-333 | WD 5 | ||||
Sequence: EHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMT | ||||||
Repeat | 336-377 | WD 6 | ||||
Sequence: GHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLN | ||||||
Region | 367-409 | Interaction with DCX | ||||
Sequence: YKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWEC | ||||||
Repeat | 378-410 | WD 7 | ||||
Sequence: AHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR | ||||||
Region | 388-410 | Interaction with NDEL1 | ||||
Sequence: FHKTAPYVVTGSVDQTVKVWECR |
Domain
Dimerization mediated by the LisH domain may be required to activate dynein.
Sequence similarities
Belongs to the WD repeat LIS1/nudF family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length410
- Mass (Da)46,613
- Last updated2007-01-23 v2
- ChecksumFE5C2DF0AB98F3B4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D30615 EMBL· GenBank· DDBJ | BAA06305.1 EMBL· GenBank· DDBJ | mRNA |