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Protein

Platelet-activating factor acetylhydrolase IB subunit alpha

Gene

Pafah1b1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position (By similarity). 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. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing.By similarity2 Publications

GO - Molecular functioni

  • dynein intermediate chain binding Source: RGD
  • microtubule binding Source: GO_Central
  • platelet-activating factor acetyltransferase activity Source: RGD
  • protein complex binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, Lipid degradation, Lipid metabolism, Mitosis, Neurogenesis, Transport

Enzyme and pathway databases

ReactomeiR-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2500257. Resolution of Sister Chromatid Cohesion.
R-RNO-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.
R-RNO-5663220. RHO GTPases Activate Formins.
R-RNO-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-RNO-68877. Mitotic Prometaphase.
R-RNO-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-activating factor acetylhydrolase IB subunit alphaUniRule annotation
Alternative name(s):
Lissencephaly-1 proteinUniRule annotation
Short name:
LIS-1UniRule annotation
PAF acetylhydrolase 45 kDa subunitUniRule annotation
Short name:
PAF-AH 45 kDa subunitUniRule annotation
PAF-AH alphaUniRule annotation
Short name:
PAFAH alphaUniRule annotation
Gene namesi
Name:Pafah1b1
Synonyms:Lis-1, Lis1, Pafaha
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi620331. Pafah1b1.

Subcellular locationi

GO - Cellular componenti

  • astral microtubule Source: Ensembl
  • axon Source: RGD
  • axon cytoplasm Source: GOC
  • cell cortex Source: GO_Central
  • cell leading edge Source: Ensembl
  • centrosome Source: GO_Central
  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • growth cone Source: RGD
  • kinesin complex Source: RGD
  • kinetochore Source: GO_Central
  • microtubule Source: GO_Central
  • motile primary cilium Source: Ensembl
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • nuclear envelope Source: MGI
  • nuclear membrane Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: Ensembl
  • vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410Platelet-activating factor acetylhydrolase IB subunit alphaPRO_0000051065Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysineBy similarity
Modified residuei109 – 1091PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP63004.
PRIDEiP63004.

2D gel databases

World-2DPAGE0004:P63004.

PTM databases

iPTMnetiP63004.
PhosphoSiteiP63004.
SwissPalmiP63004.

Expressioni

Tissue specificityi

Expressed in most tissues, with highest expression in brain.1 Publication

Gene expression databases

GenevisibleiP63004. RN.

Interactioni

Subunit structurei

Can self-associate. Interacts with DCX, dynactin, IQGAP1, KATNB1, NDE1, 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. Component of cytosolic PAF-AH IB, which is composed of PAFAH1B1 (alpha), PAFAH1B2 (beta) and PAFAH1B3 (gamma) subunits. Trimer formation is not essential for the catalytic activity of the enzyme which is contributed solely by the PAFAH1B2 (beta) and PAFAH1B3 (gamma) subunits (By similarity). Interacts with dynein and NDEL1. Interacts with ASUN (By similarity).By similarity

GO - Molecular functioni

  • dynein intermediate chain binding Source: RGD
  • microtubule binding Source: GO_Central
  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi249758. 1 interaction.
IntActiP63004. 1 interaction.
STRINGi10116.ENSRNOP00000003696.

Structurei

3D structure databases

ProteinModelPortaliP63004.
SMRiP63004. Positions 1-79, 92-408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 3933LisHUniRule annotationAdd
BLAST
Repeati106 – 14742WD 1Add
BLAST
Repeati148 – 18740WD 2Add
BLAST
Repeati190 – 22940WD 3Add
BLAST
Repeati232 – 27140WD 4Add
BLAST
Repeati274 – 33360WD 5Add
BLAST
Repeati336 – 37742WD 6Add
BLAST
Repeati378 – 41033WD 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 102102Interaction with NDEL1UniRule annotationAdd
BLAST
Regioni1 – 6666Interaction with NDE1UniRule annotationAdd
BLAST
Regioni1 – 3838Required for self-association and interaction with PAFAH1B2 and PAFAH1B3UniRule annotationAdd
BLAST
Regioni83 – 410328Interaction with dynein and dynactinUniRule annotationAdd
BLAST
Regioni367 – 40943Interaction with DCXUniRule annotationAdd
BLAST
Regioni388 – 41023Interaction with NDEL1UniRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili56 – 8227UniRule annotationAdd
BLAST

Domaini

Dimerization mediated by the LisH domain may be required to activate dynein.UniRule annotation

Sequence similaritiesi

Belongs to the WD repeat LIS1/nudF family.UniRule annotation
Contains 1 LisH domain.UniRule annotation
Contains 7 WD repeats.UniRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0295. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000184015.
HOVERGENiHBG006271.
InParanoidiP63004.
KOiK16794.
OMAiNWVRALV.
OrthoDBiEOG7QZG9N.
PhylomeDBiP63004.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03141. lis1.
InterProiIPR017252. Dynein_regulator_LIS1.
IPR020472. G-protein_beta_WD-40_rep.
IPR006594. LisH.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08513. LisH. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PIRSFiPIRSF037647. Dynein_regulator_Lis1. 1 hit.
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00667. LisH. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63004-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDMN EELDKKYAGL
60 70 80 90 100
LEKKWTSVIR LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE
110 120 130 140 150
KYALSGHRSP VTRVIFHPVF SVMVSASEDA TIKVWDYETG DFERTLKGHT
160 170 180 190 200
DSVQDISFDH SGKLLASCSA DMTIKLWDFQ GFECIRTMHG HDHNVSSVAI
210 220 230 240 250
MPNGDHIVSA SRDKTIKMWE VQTGYCVKTF TGHREWVRMV RPNQDGTLIA
260 270 280 290 300
SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY SSISEATGSE
310 320 330 340 350
TKKSGKPGPF LLSGSRDKTI KMWDVSTGMC LMTLVGHDNW VRGVLFHSGG
360 370 380 390 400
KFILSCADDK TLRVWDYKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV
410
DQTVKVWECR
Length:410
Mass (Da):46,670
Last modified:January 23, 2007 - v2
Checksum:i4DBF6A24A6B131CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016049 mRNA. Translation: AAC27975.1.
BC072510 mRNA. Translation: AAH72510.1.
RefSeqiNP_113951.1. NM_031763.3.
UniGeneiRn.5827.

Genome annotation databases

EnsembliENSRNOT00000003696; ENSRNOP00000003696; ENSRNOG00000002755.
ENSRNOT00000092712; ENSRNOP00000075779; ENSRNOG00000002755.
GeneIDi83572.
KEGGirno:83572.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF016049 mRNA. Translation: AAC27975.1.
BC072510 mRNA. Translation: AAH72510.1.
RefSeqiNP_113951.1. NM_031763.3.
UniGeneiRn.5827.

3D structure databases

ProteinModelPortaliP63004.
SMRiP63004. Positions 1-79, 92-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249758. 1 interaction.
IntActiP63004. 1 interaction.
STRINGi10116.ENSRNOP00000003696.

PTM databases

iPTMnetiP63004.
PhosphoSiteiP63004.
SwissPalmiP63004.

2D gel databases

World-2DPAGE0004:P63004.

Proteomic databases

PaxDbiP63004.
PRIDEiP63004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000003696; ENSRNOP00000003696; ENSRNOG00000002755.
ENSRNOT00000092712; ENSRNOP00000075779; ENSRNOG00000002755.
GeneIDi83572.
KEGGirno:83572.

Organism-specific databases

CTDi5048.
RGDi620331. Pafah1b1.

Phylogenomic databases

eggNOGiKOG0295. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000184015.
HOVERGENiHBG006271.
InParanoidiP63004.
KOiK16794.
OMAiNWVRALV.
OrthoDBiEOG7QZG9N.
PhylomeDBiP63004.

Enzyme and pathway databases

ReactomeiR-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2500257. Resolution of Sister Chromatid Cohesion.
R-RNO-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-RNO-380259. Loss of Nlp from mitotic centrosomes.
R-RNO-380270. Recruitment of mitotic centrosome proteins and complexes.
R-RNO-5620912. Anchoring of the basal body to the plasma membrane.
R-RNO-5663220. RHO GTPases Activate Formins.
R-RNO-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-RNO-68877. Mitotic Prometaphase.
R-RNO-8854518. AURKA Activation by TPX2.

Miscellaneous databases

PROiP63004.

Gene expression databases

GenevisibleiP63004. RN.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03141. lis1.
InterProiIPR017252. Dynein_regulator_LIS1.
IPR020472. G-protein_beta_WD-40_rep.
IPR006594. LisH.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08513. LisH. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PIRSFiPIRSF037647. Dynein_regulator_Lis1. 1 hit.
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00667. LisH. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of cDNAs encoding alpha1, alpha2, and beta subunits of rat brain platelet-activating factor acetylhydrolase."
    Watanabe M., Aoki J., Manya H., Arai H., Inoue K.
    Biochim. Biophys. Acta 1401:73-79(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Wistar.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  3. "Interaction between LIS1 and doublecortin, two lissencephaly gene products."
    Caspi M., Atlas R., Kantor A., Sapir T., Reiner O.
    Hum. Mol. Genet. 9:2205-2213(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Regulation of cytoplasmic dynein behaviour and microtubule organization by mammalian Lis1."
    Smith D.S., Niethammer M., Ayala R., Zhou Y., Gambello M.J., Wynshaw-Boris A., Tsai L.-H.
    Nat. Cell Biol. 2:767-775(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "A role for the lissencephaly gene LIS1 in mitosis and cytoplasmic dynein function."
    Faulkner N.E., Dujardin D.L., Tai C.-Y., Vaughan K.T., O'Connell C.B., Wang Y.-L., Vallee R.B.
    Nat. Cell Biol. 2:784-791(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "NUDEL is a novel cdk5 substrate that associates with LIS1 and cytoplasmic dynein."
    Niethammer M., Smith D.S., Ayala R., Peng J., Ko J., Lee M.-S., Morabito M., Tsai L.-H.
    Neuron 28:697-711(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NDEL1 AND DYNEIN.
    Tissue: Brain.
  7. "LIS1 RNA interference blocks neural stem cell division, morphogenesis, and motility at multiple stages."
    Tsai J.-W., Chen Y., Kriegstein A.R., Vallee R.B.
    J. Cell Biol. 170:935-945(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: INTERACTION WITH DYNEIN, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiLIS1_RAT
AccessioniPrimary (citable) accession number: P63004
Secondary accession number(s): O35592
, P43035, P81692, Q9R2A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.