ID LIS1_PIG Reviewed; 410 AA.
AC Q9GL51;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 01-MAY-2013, entry version 86.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha;
DE AltName: Full=Lissencephaly-1 protein;
DE Short=LIS-1;
DE AltName: Full=PAF acetylhydrolase 45 kDa subunit;
DE Short=PAF-AH 45 kDa subunit;
DE AltName: Full=PAF-AH alpha;
DE Short=PAFAH alpha;
GN Name=PAFAH1B1; Synonyms=LIS1, PAFAHA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nagasaka T., Boulday G., Coupel S., Coulon F., Tesson L.,
RA Heslan J.-M., Soulillou J.-P., Charreau B.;
RT "Cloning of porcine PAF-AH Ib-alpha cDNA and expression in endothelial
RT cells.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Positively regulates the activity of the minus-end
CC directed microtubule motor protein dynein. May enhance dynein-
CC mediated microtubule sliding by targeting dynein to the
CC microtubule plus end. Required for several dynein- and
CC microtubule-dependent processes such as the maintenance of Golgi
CC integrity, the peripheral transport of microtubule fragments and
CC the coupling of the nucleus and centrosome. Required during brain
CC development for the proliferation of neuronal precursors and the
CC migration of newly formed neurons from the
CC ventricular/subventricular zone toward the cortical plate.
CC Neuronal migration involves a process called nucleokinesis,
CC whereby migrating cells extend an anterior process into which the
CC nucleus subsequently translocates. During nucleokinesis dynein at
CC the nuclear surface may translocate the nucleus towards the
CC centrosome by exerting force on centrosomal microtubules. Also
CC required for proper activation of Rho GTPases and actin
CC polymerization at the leading edge of locomoting cerebellar
CC neurons and postmigratory hippocampal neurons in response to
CC calcium influx triggered via NMDA receptors. May also play a role
CC in other forms of cell locomotion including the migration of
CC fibroblasts during wound healing. Non-catalytic subunit of an
CC acetylhydrolase complex which inactivates platelet-activating
CC factor (PAF) by removing the acetyl group at the SN-2 position (By
CC similarity).
CC -!- SUBUNIT: Can self-associate. Interacts with DCX, dynein, dynactin,
CC IQGAP1, KATNB1, NDE1, NDEL1, NUDC and RSN. Interacts with DISC1,
CC and this interaction is enhanced by NDEL1. Interacts with DAB1
CC when DAB1 is phosphorylated in response to RELN/reelin signaling.
CC Component of cytosolic PAF-AH IB, which is composed of PAFAH1B1
CC (alpha), PAFAH1B2 (beta) and PAFAH1B3 (gamma) subunits. Trimer
CC formation is not essential for the catalytic activity of the
CC enzyme which is contributed solely by the PAFAH1B2 (beta) and
CC PAFAH1B3 (gamma) subunits (By similarity). Interacts with ASUN (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Cytoplasm, cytoskeleton, centrosome (By similarity). Cytoplasm,
CC cytoskeleton, spindle (By similarity). Nucleus membrane (By
CC similarity). Note=Localizes to the plus end of microtubules and to
CC the centrosome. May localize to the nuclear membrane.
CC Redistributes to axons during neuronal development. Also localizes
CC to the microtubules of the manchette in elongating spermatids and
CC to the meiotic spindle in spermatocytes (By similarity).
CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required
CC to activate dynein (By similarity).
CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC -!- SIMILARITY: Contains 1 LisH domain.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF319658; AAG33867.1; -; mRNA.
DR RefSeq; NP_999415.1; NM_214250.1.
DR UniGene; Ssc.802; -.
DR ProteinModelPortal; Q9GL51; -.
DR SMR; Q9GL51; 1-79, 92-408.
DR PaxDb; Q9GL51; -.
DR PRIDE; Q9GL51; -.
DR GeneID; 397482; -.
DR KEGG; ssc:397482; -.
DR CTD; 5048; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000184015; -.
DR HOVERGEN; HBG006271; -.
DR KO; K16794; -.
DR OrthoDB; EOG4P5K93; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03141; lis1; 1; -.
DR InterPro; IPR017252; Dynein_regulator.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006594; LisH_dimerisation.
DR InterPro; IPR013720; LisH_dimerisation_subgr.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR PANTHER; PTHR22847:SF51; PTHR22847:SF51; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 7.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40_like; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Coiled coil;
KW Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Lipid degradation; Lipid metabolism; Membrane;
KW Microtubule; Mitosis; Neurogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1 410 Platelet-activating factor
FT acetylhydrolase IB subunit alpha.
FT /FTId=PRO_0000240413.
FT DOMAIN 7 39 LisH.
FT REPEAT 106 147 WD 1.
FT REPEAT 148 187 WD 2.
FT REPEAT 190 229 WD 3.
FT REPEAT 232 271 WD 4.
FT REPEAT 274 333 WD 5.
FT REPEAT 336 377 WD 6.
FT REPEAT 378 410 WD 7.
FT REGION 1 102 Interaction with NDEL1 (By similarity).
FT REGION 1 66 Interaction with NDE1 (By similarity).
FT REGION 1 38 Required for self-association and
FT interaction with PAFAH1B2 and PAFAH1B3
FT (By similarity).
FT REGION 83 410 Interaction with dynein and dynactin (By
FT similarity).
FT REGION 367 409 Interaction with DCX (By similarity).
FT REGION 388 410 Interaction with NDEL1 (By similarity).
FT COILED 56 82 Potential.
FT MOD_RES 28 28 Phosphotyrosine (By similarity).
FT MOD_RES 53 53 N6-acetyllysine (By similarity).
SQ SEQUENCE 410 AA; 46654 MW; A08DAFCD8B8B2719 CRC64;
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDMN EELDKKYAGL LEKKWTSVIR
LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE KYALSGHRSP VTRVIFHPVF
SVMVSASEDA TIKVWDYETG DFERTLKGHT DSVQDISFDH SGKLLASCSA DMTIKLWDFQ
GFECIRTMHG HDHNVSSVAI MPNGDHIVSA ARDKTIKMWE VQTGYCVKTF TGHREWVRMV
RPNQDGTLIA SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY SSISEATGSE
TKKSGKPGPF LLSGSRDKTI KMWDVSTGMC LMTLVGHDNW VRGVLFHSGG KFILSCADDK
TLRVWDYKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV DQTVKVWECR
//
