Overview
| Uniprot ID | H0VRI4 |
|---|
| Protein Name | Platelet-activating factor acetylhydrolase IB subunit alpha |
|---|
| Gene Name | PAFAH1B1 |
|---|
| Organism | Cavia porcellus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 86 |
SGGPLGQKRDPKEWI |
| 90 |
LGQKRDPKEWIPRPP |
Function
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. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position
Protein Sequence
10
SILSEKNERE
20
ASIADYLRSN
30
GYEEAYSVFK
40
KEAELDMNEE
50
LDKKYAGLLE
60
KKWTSVIRLQ
70
KKVMELESKL
80
NEAKEEFTSG
90
GPLGQKRDPK
100
EWIPRPPEKY
110
ALSGHRSPVT
120
RVIFHPVFSV
130
MVSASEDATI
140
KVWDYETGDF
150
ERTLKGHTDS
160
VQDISFDHSG
170
KLLASCSADM
180
TIKLWDFQGF
190
ECIRTMHGHD
200
HNVSSVAIMP
210
NGDHIVSASR
220
DKTIKMWEVQ
230
TGYCVKTFTG
240
HREWVRMVRP
250
NQDGTLIASC
260
SNDQTVRVWV
270
VATKECKAEL
280
REHEHVVECI
290
SWAPESSYSS
300
ISEATGSETK
310
KSGKPGPFLL
320
SGSRDKTIKM
330
WDVSTGMCLM
340
TLVGHDNWVR
350
GVLFHSGGKF
360
ILSCADDKTL
370
RVWDYKNKRC
380
MKTLNAHEHF
390
VTSLDFHKTA
400
PYVVTGSVDQ
TVKVWECR
Gene Ontology
| Classification |
GO ID |
Description |
| Biological Process |
GO:0001764 |
neuron migration |
| Cellular Component |
GO:0005813 |
centrosome |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005874 |
microtubule |
| Cellular Component |
GO:0005875 |
microtubule associated complex |
| Cellular Component |
GO:0031965 |
nuclear membrane |
| Cellular Component |
GO:0005819 |
spindle |
| Molecular Function |
GO:0070840 |
dynein complex binding |
| Biological Process |
GO:0051301 |
cell division |
| Biological Process |
GO:0051642 |
centrosome localization |
| Biological Process |
GO:0000132 |
establishment of mitotic spindle orientation |
| Biological Process |
GO:0030900 |
forebrain development |
| Biological Process |
GO:0016042 |
lipid catabolic process |
| Biological Process |
GO:0051012 |
microtubule sliding |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.