ID A0A3P9QFG1_POERE Unreviewed; 418 AA.
AC A0A3P9QFG1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Lissencephaly-1 homolog {ECO:0000256|HAMAP-Rule:MF_03141};
GN Name=PAFAH1B1 {ECO:0000256|HAMAP-Rule:MF_03141};
GN Synonyms=LIS1 {ECO:0000256|HAMAP-Rule:MF_03141};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000032488.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000032488.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000032488.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Positively regulates the activity of the minus-end directed
CC microtubule motor protein dynein. May enhance dynein-mediated
CC microtubule sliding by targeting dynein to the microtubule plus end.
CC Required for several dynein- and microtubule-dependent processes such
CC as the maintenance of Golgi integrity, the peripheral transport of
CC microtubule fragments and the coupling of the nucleus and centrosome.
CC May be required for proliferation of neuronal precursors and neuronal
CC migration. {ECO:0000256|HAMAP-Rule:MF_03141}.
CC -!- SUBUNIT: Can self-associate. Component of the cytosolic PAF-AH (I)
CC heterotetrameric enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2
CC (alpha2) and PAFAH1B3 (alpha1) subunits. The catalytic activity of the
CC enzyme resides in the alpha1 (PAFAH1B3) and alpha2 (PAFAH1B2) subunits,
CC whereas the beta subunit (PAFAH1B1) has regulatory activity. Trimer
CC formation is not essential for the catalytic activity (By similarity).
CC Interacts with dynein, dynactin, nde1 and ndel1.
CC {ECO:0000256|ARBA:ARBA00023793}.
CC -!- SUBUNIT: Can self-associate. Interacts with dynein, dynactin, NDE1 and
CC NDEL1. {ECO:0000256|HAMAP-Rule:MF_03141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-
CC Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000256|HAMAP-Rule:MF_03141}. Note=Localizes to the
CC plus end of microtubules and to the centrosome. {ECO:0000256|HAMAP-
CC Rule:MF_03141}.
CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to
CC activate dynein. {ECO:0000256|HAMAP-Rule:MF_03141}.
CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC {ECO:0000256|HAMAP-Rule:MF_03141}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03141}.
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DR AlphaFoldDB; A0A3P9QFG1; -.
DR STRING; 8081.ENSPREP00000032488; -.
DR Ensembl; ENSPRET00000032857.1; ENSPREP00000032488.1; ENSPREG00000022018.1.
DR GeneTree; ENSGT00940000155039; -.
DR OMA; GAHEGPF; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000022018; Expressed in head and 1 other cell type or tissue.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IEA:UniProtKB-UniRule.
DR GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:UniProtKB-UniRule.
DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.960.30; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_03141; lis1; 1.
DR InterPro; IPR017252; Dynein_regulator_LIS1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037190; LIS1_N.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR44129:SF20; LISSENCEPHALY-1 HOMOLOG B; 1.
DR PANTHER; PTHR44129; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 6.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF109925; Lissencephaly-1 protein (Lis-1, PAF-AH alpha) N-terminal domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03141};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|HAMAP-Rule:MF_03141};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902, ECO:0000256|HAMAP-
KW Rule:MF_03141}; Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_03141};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 98..139
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 140..181
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 182..223
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 224..265
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 302..327
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 328..369
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT COILED 27..72
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03141"
SQ SEQUENCE 418 AA; 47326 MW; D24AF4465DAD72D9 CRC64;
FILAQNRAIA DYLRSNGYEE AYSTFKKEAE LDNNEELDKK YAGLLEKKWT SVIRLQKKVM
ELESKLNEAK EEITLGGPVS QKRDPKEWIP RPPERYALSG HRNPVTRVIF HPVFSVMVSA
SEDATIKVWD YETGDFERTL KGHTDSVQDI SFDQTGKLLA SCSADMTIKL WDFQGFECIR
TMHGHDHNVS SVAIMPNGDH IVSASRDKTI KMWEVATGYC VKTFTGHREW VRMVRPNQDG
TLIASCSNDQ TVRVWVVATK ECKAELREHE HVVECISWAP ESAHPTILDA TGSETKKSGK
PGPFLLSGSR DKTIKMWDVS TGMCLMTLVG HDNWVRGILF HPGGKFIVSC ADDKTLRIWD
YKNKRCMKTL SAHEHFVTSL GKLHFDLLKT WPLMCHLCAV VPVSLIASFP LPYPPNLS
//
