ID A0A3L8RWY1_CHLGU Unreviewed; 406 AA.
AC A0A3L8RWY1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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};
GN ORFNames=DV515_00014898 {ECO:0000313|EMBL:RLV89380.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV89380.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV89380.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV89380.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV89380.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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. 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV89380.1}.
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DR EMBL; QUSF01000148; RLV89380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8RWY1; -.
DR STRING; 44316.ENSEGOP00005017079; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
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: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 GO; GO:0007399; P:nervous system development; 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:SF1; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT BETA; 1.
DR PANTHER; PTHR44129; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 7.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
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; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 6.
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}; Developmental protein {ECO:0000256|HAMAP-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:UP000276834};
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 100..141
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 142..183
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 184..225
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 226..267
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 304..329
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 330..371
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 372..406
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 406 AA; 46077 MW; 959B90041A6E7E7F CRC64;
MVVVLARNRA IADYLRSNGY EEAYSVFKKE AELDVNEELD KKYAGLLEKK WTSVIRLQKK
VMELESKLNE AKEEFTSGGP LGQKRDPKEW IPRPPEKYAL SGHRSPVTRV IFHPVFSVMV
SASEDATIKV WDYETGDFER TLKGHTDSVQ DISFDHTGKL LASCSADMTI KLWDFQGFEC
IRTMHGHDHN VSSVAIMPNG DHIVSASRDK TIKMWEVQTG YCVKTFTGHR EWVRMVRPNQ
DGTLIASCSN DQTVRVWVVA TKECKAELRE HEHVVECISW APESSYSTIS EATGSETKKS
GKPGPFLLSG SRDKTIKMWD ISTGMCLMTL VGHDNWVRGV LFHSGGKFIL SCADDKTLRV
WDFKNKRCMK TLNAHEHFVT SLDFHKTAPY VVTGSVDQTV KVWECR
//
