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Database: UniProt
Entry: Q9GL51
LinkDB: Q9GL51
Original site: Q9GL51 
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   19-FEB-2014, entry version 92.
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, microtubule organizing center, centrosome
CC       (By similarity). Cytoplasm, cytoskeleton, spindle (By similarity).
CC       Nucleus membrane (By similarity). Note=Localizes to the plus end
CC       of microtubules and to the centrosome. May localize to the nuclear
CC       membrane. Redistributes to axons during neuronal development. Also
CC       localizes to the microtubules of the manchette in elongating
CC       spermatids and to the meiotic spindle in spermatocytes (By
CC       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.
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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   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; IEA:UniProtKB-HAMAP.
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:0006928; P:cellular component movement; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:UniProtKB-HAMAP.
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-HAMAP.
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_LIS1.
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   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; SSF50978; 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; Reference proteome;
KW   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      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
//
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