LIS1_CAEEL
ID LIS1_CAEEL Reviewed; 404 AA.
AC Q9NDC9; O45742;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=Pronuclear migration abnormal protein 1;
GN Name=lis-1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=pnm-1 {ECO:0000312|WormBase:T03F6.5};
GN ORFNames=T03F6.5 {ECO:0000312|WormBase:T03F6.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=11685578; DOI=10.1007/s004270100176;
RA Dawe A.L., Caldwell K.A., Harris P.M., Morris N.R., Caldwell G.A.;
RT "Evolutionarily conserved nuclear migration genes required for early
RT embryonic development in Caenorhabditis elegans.";
RL Dev. Genes Evol. 211:434-441(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15254012; DOI=10.1093/hmg/ddh209;
RA Williams S.N., Locke C.J., Braden A.L., Caldwell K.A., Caldwell G.A.;
RT "Epileptic-like convulsions associated with LIS-1 in the cytoskeletal
RT control of neurotransmitter signaling in Caenorhabditis elegans.";
RL Hum. Mol. Genet. 13:2043-2059(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15331665; DOI=10.1242/jcs.01344;
RA Cockell M.M., Baumer K., Goenczy P.;
RT "lis-1 is required for dynein-dependent cell division processes in C.
RT elegans embryos.";
RL J. Cell Sci. 117:4571-4582(2004).
RN [5]
RP FUNCTION, INTERACTION WITH NUD-2, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16996038; DOI=10.1016/j.brainres.2006.08.067;
RA Locke C.J., Williams S.N., Schwarz E.M., Caldwell G.A., Caldwell K.A.;
RT "Genetic interactions among cortical malformation genes that influence
RT susceptibility to convulsions in C. elegans.";
RL Brain Res. 1120:23-34(2006).
RN [6]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH NUD-2, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20005871; DOI=10.1016/j.ydbio.2009.12.004;
RA Fridolfsson H.N., Ly N., Meyerzon M., Starr D.A.;
RT "UNC-83 coordinates kinesin-1 and dynein activities at the nuclear envelope
RT during nuclear migration.";
RL Dev. Biol. 338:237-250(2010).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=20599902; DOI=10.1016/j.ydbio.2010.06.016;
RA Fortin S.M., Marshall S.L., Jaeger E.C., Greene P.E., Brady L.K.,
RA Isaac R.E., Schrandt J.C., Brooks D.R., Lyczak R.;
RT "The PAM-1 aminopeptidase regulates centrosome positioning to ensure
RT anterior-posterior axis specification in one-cell C. elegans embryos.";
RL Dev. Biol. 344:992-1000(2010).
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 nuclear migration during cell division (PubMed:11685578,
CC PubMed:15331665). Part of a complex with nud-2, which is recruited to
CC the nuclear envelope by unc-83, where, in turn, it recruits dynein to
CC the nuclear surface and regulates nuclear migration in hypodermal
CC precursor cells (PubMed:20005871). Plays a role in GABAergic synaptic
CC vesicle localization in the ventral nerve cord (PubMed:16996038).
CC Required for neuronal cell differentiation (PubMed:15254012).
CC {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:11685578,
CC ECO:0000269|PubMed:15254012, ECO:0000269|PubMed:15331665,
CC ECO:0000269|PubMed:16996038, ECO:0000269|PubMed:20005871}.
CC -!- SUBUNIT: Component of a dynein-regulating complex composed of at least
CC lis-1 and nud-2 (PubMed:20005871). Interacts with nud-2; the
CC interaction is direct (PubMed:16996038). {ECO:0000269|PubMed:16996038,
CC ECO:0000305|PubMed:20005871}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Chromosome, centromere,
CC kinetochore {ECO:0000305}. Nucleus envelope
CC {ECO:0000305|PubMed:20005871}. Note=Localizes to the plus end of
CC microtubules (By similarity). Concentrates in the vicinity of
CC microtubule asters, kinetochores, the cell cortex and the perinuclear
CC region (PubMed:15331665). Probably recruited to the nuclear envelope by
CC unc-83 (PubMed:20005871). {ECO:0000250|UniProtKB:P63004,
CC ECO:0000269|PubMed:15331665, ECO:0000305|PubMed:20005871}.
CC -!- TISSUE SPECIFICITY: Expressed in all classes of neurons in the ventral
CC cord (PubMed:11685578, PubMed:16996038). Expressed in the multinucleate
CC spermathecal valves and adult seam cells (PubMed:11685578).
CC {ECO:0000269|PubMed:11685578, ECO:0000269|PubMed:16996038}.
CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to
CC activate dynein. {ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- DISRUPTION PHENOTYPE: Defects lead to convulsions mimicking epilepsy,
CC possibly due to altered neurotransmitter function (PubMed:15254012).
CC RNAi-mediated knockdown results in arrest at the 50-100 cell stage,
CC whereby egg and sperm pronuclei fails to migrate (PubMed:11685578).
CC RNAi-mediated knockdown prevents the sperm-donated centrosome from
CC leaving the posterior cortex in 1-cell embryos (PubMed:20599902). RNAi-
CC mediated knockdown results in an abnormal distribution of GABAergic
CC synaptic vesicles at synaptic termini of the ventral nerve cord
CC (PubMed:16996038). RNAi-mediated knockdown results in nuclear migration
CC defects in hyp7 hypodermal precursor cells, but only in a small number
CC of animals (PubMed:20005871). RNAi-mediated knockdown in a pam-1 mutant
CC background restores anterior-posterior polarity (PubMed:20599902).
CC {ECO:0000269|PubMed:11685578, ECO:0000269|PubMed:15254012,
CC ECO:0000269|PubMed:16996038, ECO:0000269|PubMed:20005871,
CC ECO:0000269|PubMed:20599902}.
CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC {ECO:0000255|HAMAP-Rule:MF_03141}.
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DR EMBL; AF164430; AAF82632.1; -; mRNA.
DR EMBL; Z81113; CAB03282.3; -; Genomic_DNA.
DR PIR; T24399; T24399.
DR RefSeq; NP_499755.1; NM_067354.5.
DR AlphaFoldDB; Q9NDC9; -.
DR SMR; Q9NDC9; -.
DR BioGRID; 41927; 39.
DR ComplexPortal; CPX-1389; lis-1-nud-2 microtubule-associated dynein motor complex.
DR IntAct; Q9NDC9; 2.
DR STRING; 6239.T03F6.5; -.
DR EPD; Q9NDC9; -.
DR PaxDb; Q9NDC9; -.
DR PeptideAtlas; Q9NDC9; -.
DR EnsemblMetazoa; T03F6.5.1; T03F6.5.1; WBGene00003047.
DR GeneID; 176758; -.
DR KEGG; cel:CELE_T03F6.5; -.
DR UCSC; T03F6.5; c. elegans.
DR CTD; 36791; -.
DR WormBase; T03F6.5; CE29339; WBGene00003047; lis-1.
DR eggNOG; KOG0295; Eukaryota.
DR GeneTree; ENSGT00940000155039; -.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q9NDC9; -.
DR OMA; TQECKCV; -.
DR OrthoDB; 995692at2759; -.
DR PhylomeDB; Q9NDC9; -.
DR Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR SignaLink; Q9NDC9; -.
DR PRO; PR:Q9NDC9; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003047; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005818; C:aster; IDA:WormBase.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:WormBase.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:WormBase.
DR GO; GO:0005874; C:microtubule; IDA:WormBase.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0048854; P:brain morphogenesis; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051026; P:chiasma assembly; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IMP:WormBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:WormBase.
DR GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0051661; P:maintenance of centrosome location; IMP:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; IBA:GO_Central.
DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR GO; GO:0007018; P:microtubule-based movement; IMP:WormBase.
DR GO; GO:0007100; P:mitotic centrosome separation; IMP:WormBase.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0031022; P:nuclear migration along microfilament; IMP:ComplexPortal.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0035046; P:pronuclear migration; IMP:WormBase.
DR GO; GO:0008090; P:retrograde axonal transport; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IMP:WormBase.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IMP:WormBase.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:WormBase.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
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; IPR037190; LIS1_N.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
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; SSF109925; SSF109925; 1.
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 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Kinetochore;
KW Microtubule; Mitosis; Neurogenesis; Nucleus; Oogenesis; Reference proteome;
KW Repeat; Transport; WD repeat.
FT CHAIN 1..404
FT /note="Lissencephaly-1 homolog"
FT /id="PRO_0000051066"
FT DOMAIN 7..39
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 104..145
FT /note="WD 1"
FT REPEAT 146..185
FT /note="WD 2"
FT REPEAT 189..228
FT /note="WD 3"
FT REPEAT 231..270
FT /note="WD 4"
FT REPEAT 273..327
FT /note="WD 5"
FT REPEAT 330..369
FT /note="WD 6"
FT REPEAT 372..404
FT /note="WD 7"
FT REGION 69..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..81
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 404 AA; 45777 MW; 7F8E5543D7BA9C65 CRC64;
MSLSERQKEE INRAIAEYMQ NNGYSESFSV FLKESSLSEN DIKPLGGILE KKWTTVLRLQ
RKVNDLESKL QESQREINHG APTRDKRQAA DWIPRPPETQ KLTGHRLPIT RVIFHPLWTI
MASCSEDATI KVWDYETGQL ERTLKGHTDA VNDIAIDAAG KQLVSCSSDL SIKLWDFGQT
YDCLKSLKGH EHTVSSVTFL PTGDFVLSAS RDHTIKQWDI STGYCVYTFR GHNDWVRMIR
ISNDGTLFAS ASLDQTVTVW SFATKSAKLV LRDHEHAVEC VEWAPDTAYT NVTGQQPEGN
STHILFSGSR DRSIKAWNIN TGDVLFTLLA HENWVRGLAF HPKGKYLISV ADDKTLRVWE
LSAQRCMKAI EAHEHFVSTV AFHQTSPFVI TGSVDMSCKV WECR
