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Q5SW18 (Q5SW18_MOUSE) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Platelet-activating factor acetylhydrolase IB subunit alpha HAMAP-Rule MF_03141
Alternative name(s):
Lissencephaly-1 protein HAMAP-Rule MF_03141
PAF acetylhydrolase 45 kDa subunit HAMAP-Rule MF_03141
PAF-AH alpha HAMAP-Rule MF_03141
Gene names
Name:Pafah1b1 HAMAP-Rule MF_03141 MGI 109520
Synonyms:Lis1 HAMAP-Rule MF_03141
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_03141

Subunit structure

Can self-associate. Interacts with DCX, dynein, dynactin, IQGAP1, KATNB1, NDE1, 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. 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. HAMAP-Rule MF_03141

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Nucleus membrane. Note: Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. 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. HAMAP-Rule MF_03141

Domain

Dimerization mediated by the LisH domain may be required to activate dynein By similarity. HAMAP-Rule MF_03141

Sequence similarities

Belongs to the WD repeat LIS1/nudF family. HAMAP-Rule MF_03141

Contains 1 LisH domain. HAMAP-Rule MF_03141

Contains 7 WD repeats. HAMAP-Rule MF_03141

Contains LisH domain. SAAS SAAS006594

Ontologies

Keywords
   Biological processCell cycle
Cell division
Differentiation HAMAP-Rule MF_03141
Lipid degradation HAMAP-Rule MF_03141
Lipid metabolism
Mitosis SAAS SAAS006594 HAMAP-Rule MF_03141
Neurogenesis HAMAP-Rule MF_03141
Transport SAAS SAAS006594 HAMAP-Rule MF_03141
   Cellular componentCytoplasm
Cytoskeleton SAAS SAAS006594 HAMAP-Rule MF_03141
Membrane HAMAP-Rule MF_03141
Microtubule SAAS SAAS006594 HAMAP-Rule MF_03141
Nucleus HAMAP-Rule MF_03141
   DomainCoiled coil SAAS SAAS006594 HAMAP-Rule MF_03141
Repeat SAAS SAAS006594 RuleBase RU003532 HAMAP-Rule MF_03141
WD repeat SAAS SAAS006594 RuleBase RU000362 HAMAP-Rule MF_03141
   Molecular functionDevelopmental protein HAMAP-Rule MF_03141
Gene Ontology (GO)
   Biological_processacrosome assembly

Inferred from mutant phenotype PubMed 13129914. Source: MGI

actin cytoskeleton organization

Inferred from mutant phenotype PubMed 14507966. Source: MGI

adult locomotory behavior

Inferred from mutant phenotype PubMed 10541472. Source: MGI

ameboidal cell migration

Inferred from mutant phenotype PubMed 22073305. Source: MGI

brain morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell migration

Inferred from mutant phenotype PubMed 12629176. Source: MGI

cerebral cortex development

Inferred from mutant phenotype PubMed 11344260. Source: MGI

cerebral cortex neuron differentiation

Inferred from electronic annotation. Source: Ensembl

corpus callosum morphogenesis

Inferred from electronic annotation. Source: Ensembl

establishment of centrosome localization

Inferred from electronic annotation. Source: Ensembl

establishment of mitotic spindle orientation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

hippocampus development

Inferred from mutant phenotype PubMed 10729324. Source: MGI

layer formation in cerebral cortex

Inferred from genetic interaction PubMed 17330141. Source: MGI

learning or memory

Inferred from mutant phenotype PubMed 10541472. Source: MGI

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule cytoskeleton organization

Inferred from mutant phenotype PubMed 22073305. Source: MGI

microtubule organizing center organization

Inferred from electronic annotation. Source: Ensembl

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of JNK cascade

Inferred from genetic interaction PubMed 22073305. Source: MGI

negative regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

neuroblast proliferation

Inferred from mutant phenotype PubMed 12629176. Source: MGI

neuromuscular process controlling balance

Inferred from mutant phenotype PubMed 10541472. Source: MGI

neuron migration

Inferred from mutant phenotype PubMed 14507966PubMed 15331402PubMed 9697693. Source: MGI

nuclear envelope disassembly

Inferred from mutant phenotype PubMed 18809722. Source: MGI

nuclear migration

Inferred from electronic annotation. Source: Ensembl

osteoclast development

Inferred from mutant phenotype PubMed 22073305. Source: MGI

positive regulation of axon extension

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokine-mediated signaling pathway

Inferred from mutant phenotype PubMed 22073305. Source: MGI

positive regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

protein secretion

Inferred from mutant phenotype PubMed 22073305. Source: MGI

regulation of Rho GTPase activity

Inferred from mutant phenotype PubMed 14507966. Source: MGI

retrograde axon cargo transport

Inferred from direct assay PubMed 11163259. Source: MGI

stem cell division

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Inferred from mutant phenotype PubMed 10729324. Source: MGI

transmission of nerve impulse

Inferred from mutant phenotype PubMed 17433713. Source: MGI

vesicle transport along microtubule

Inferred from genetic interaction PubMed 16107726. Source: MGI

   Cellular_componentastral microtubule

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from direct assay PubMed 11163259PubMed 11163260. Source: MGI

cytoplasm

Inferred from direct assay PubMed 12551946PubMed 12950100. Source: MGI

cytosol

Inferred from electronic annotation. Source: Ensembl

growth cone

Inferred from electronic annotation. Source: Ensembl

kinesin complex

Inferred from electronic annotation. Source: Ensembl

kinetochore

Inferred from electronic annotation. Source: Ensembl

microtubule associated complex

Inferred from direct assay PubMed 11163259. Source: MGI

microtubule cytoskeleton

Inferred from direct assay PubMed 13129914. Source: MGI

motile primary cilium

Inferred from direct assay PubMed 17314247. Source: MGI

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nuclear envelope

Inferred from sequence or structural similarity PubMed 18809722. Source: MGI

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay PubMed 14578885. Source: MGI

vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmicrotubule binding

Inferred from direct assay PubMed 11163259. Source: MGI

phosphoprotein binding

Inferred from physical interaction PubMed 14578885. Source: MGI

protein homodimerization activity

Inferred from physical interaction PubMed 11344260. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity HAMAP-Rule MF_03141

Regions

Domain7 – 3933LisH By similarity HAMAP-Rule MF_03141
Repeat106 – 14742WD 1 By similarity HAMAP-Rule MF_03141
Repeat148 – 18740WD 2 By similarity HAMAP-Rule MF_03141
Repeat190 – 22940WD 3 By similarity HAMAP-Rule MF_03141
Repeat232 – 27140WD 4 By similarity HAMAP-Rule MF_03141
Repeat274 – 33360WD 5 By similarity HAMAP-Rule MF_03141
Repeat336 – 37742WD 6 By similarity HAMAP-Rule MF_03141
Repeat378 – 41033WD 7 By similarity HAMAP-Rule MF_03141
Region1 – 102102Interaction with NDEL1 By similarity HAMAP-Rule MF_03141
Region1 – 6666Interaction with NDE1 By similarity HAMAP-Rule MF_03141
Region1 – 3838Required for self-association and interaction with PAFAH1B2 and PAFAH1B3 By similarity HAMAP-Rule MF_03141
Region83 – 410328Interaction with dynein and dynactin By similarity HAMAP-Rule MF_03141
Region367 – 40943Interaction with DCX By similarity HAMAP-Rule MF_03141
Region388 – 41023Interaction with NDEL1 By similarity HAMAP-Rule MF_03141
Coiled coil56 – 8227 By similarity HAMAP-Rule MF_03141

Sequences

Sequence LengthMass (Da)Tools
Q5SW18 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 4DBF6A24A6B131CD

FASTA41046,670
        10         20         30         40         50         60 
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDMN EELDKKYAGL LEKKWTSVIR 

        70         80         90        100        110        120 
LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE KYALSGHRSP VTRVIFHPVF 

       130        140        150        160        170        180 
SVMVSASEDA TIKVWDYETG DFERTLKGHT DSVQDISFDH SGKLLASCSA DMTIKLWDFQ 

       190        200        210        220        230        240 
GFECIRTMHG HDHNVSSVAI MPNGDHIVSA SRDKTIKMWE VQTGYCVKTF TGHREWVRMV 

       250        260        270        280        290        300 
RPNQDGTLIA SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY SSISEATGSE 

       310        320        330        340        350        360 
TKKSGKPGPF LLSGSRDKTI KMWDVSTGMC LMTLVGHDNW VRGVLFHSGG KFILSCADDK 

       370        380        390        400        410 
TLRVWDYKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV DQTVKVWECR 

« Hide

References

[1]"High-efficiency full-length cDNA cloning."
Carninci P., Hayashizaki Y.
Methods Enzymol. 303:19-44(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6 EMBL BAE27977.1 and C57BL/6J EMBL BAE27764.1.
Tissue: Amnion EMBL BAE40742.1, Brain EMBL BAE27977.1, Mammary gland EMBL BAE26129.1, Stomach EMBL BAE40766.1 and Whole body EMBL BAE27764.1.
[2]"Normalization and subtraction of cap-trapper-selected cDNAs to prepare full-length cDNA libraries for rapid discovery of new genes."
Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.
Genome Res. 10:1617-1630(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6 EMBL BAE27977.1 and C57BL/6J EMBL BAE27764.1.
Tissue: Amnion EMBL BAE40742.1, Brain EMBL BAE27977.1, Mammary gland EMBL BAE26129.1, Stomach EMBL BAE40766.1 and Whole body EMBL BAE27764.1.
[3]"RIKEN integrated sequence analysis (RISA) system--384-format sequencing pipeline with 384 multicapillary sequencer."
Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A. expand/collapse author list , Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.
Genome Res. 10:1757-1771(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6 EMBL BAE27977.1 and C57BL/6J EMBL BAE27764.1.
Tissue: Amnion EMBL BAE40742.1, Brain EMBL BAE27977.1, Mammary gland EMBL BAE26129.1, Stomach EMBL BAE40766.1 and Whole body EMBL BAE27764.1.
[4]"Functional annotation of a full-length mouse cDNA collection."
The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium
Nature 409:685-690(2001)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6 EMBL BAE27977.1 and C57BL/6J EMBL BAE27764.1.
Tissue: Amnion EMBL BAE40742.1, Brain EMBL BAE27977.1, Mammary gland EMBL BAE26129.1, Stomach EMBL BAE40766.1 and Whole body EMBL BAE27764.1.
[5]"Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs."
The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team
Nature 420:563-573(2002)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6 EMBL BAE27977.1 and C57BL/6J EMBL BAE27764.1.
Tissue: Amnion EMBL BAE40742.1, Brain EMBL BAE27977.1, Mammary gland EMBL BAE26129.1, Stomach EMBL BAE40766.1 and Whole body EMBL BAE27764.1.
[6]Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H. expand/collapse author list , Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6 EMBL BAE27977.1 and C57BL/6J EMBL BAE27764.1.
Tissue: Brain EMBL BAE27977.1, Mammary gland EMBL BAE26129.1 and Whole body EMBL BAE27764.1.
[7]Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H. expand/collapse author list , Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6J EMBL BAE37586.1.
Tissue: Amnion EMBL BAE40742.1, Stomach EMBL BAE40766.1 and Whole body EMBL BAE37586.1.
[8]"The Transcriptional Landscape of the Mammalian Genome."
The FANTOM Consortium, Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group)
Science 309:1559-1563(2005)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6 EMBL BAE27977.1 and C57BL/6J EMBL BAE27764.1.
Tissue: Amnion EMBL BAE40742.1, Brain EMBL BAE27977.1, Mammary gland EMBL BAE26129.1, Stomach EMBL BAE40766.1 and Whole body EMBL BAE27764.1.
[9]"Antisense Transcription in the Mammalian Transcriptome."
RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium
Science 309:1564-1566(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6 EMBL BAE27977.1 and C57BL/6J EMBL BAE27764.1.
Tissue: Amnion EMBL BAE40742.1, Brain EMBL BAE27977.1, Mammary gland EMBL BAE26129.1, Stomach EMBL BAE40766.1 and Whole body EMBL BAE27764.1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK144908 mRNA. Translation: BAE26129.1.
AK147207 mRNA. Translation: BAE27764.1.
AK147237 mRNA. Translation: BAE27787.1.
AK147507 mRNA. Translation: BAE27961.1.
AK147533 mRNA. Translation: BAE27977.1.
AK164008 mRNA. Translation: BAE37586.1.
AK168929 mRNA. Translation: BAE40742.1.
AK168960 mRNA. Translation: BAE40766.1.
RefSeqNP_038653.1. NM_013625.4.
UniGeneMm.397111.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID18472.
KEGGmmu:18472.

Organism-specific databases

CTD5048.
MGIMGI:109520. Pafah1b1.

Phylogenomic databases

GeneTreeENSGT00750000117266.
HOVERGENHBG006271.
InParanoidQ5SW18.
KOK16794.
OMAWVRGLAF.

Gene expression databases

GenevestigatorQ5SW18.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
HAMAPMF_03141. lis1.
InterProIPR017252. Dynein_regulator_LIS1.
IPR020472. G-protein_beta_WD-40_rep.
IPR006594. LisH_dimerisation.
IPR013720. LisH_dimerisation_subgr.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF08513. LisH. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PIRSFPIRSF037647. Dynein_regulator_Lis1. 1 hit.
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00667. LisH. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAFAH1B1. mouse.
NextBio294162.
SOURCESearch...

Entry information

Entry nameQ5SW18_MOUSE
AccessionPrimary (citable) accession number: Q5SW18
Entry history
Integrated into UniProtKB/TrEMBL: May 10, 2005
Last sequence update: May 10, 2005
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)