LARK_DROME
ID LARK_DROME Reviewed; 352 AA.
AC Q94901; A4V1L0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=RNA-binding protein lark;
GN Name=lark; ORFNames=CG8597;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9120432;
RX DOI=10.1002/(sici)1097-4695(199609)31:1<117::aid-neu10>3.0.co;2-i;
RA Newby L.M., Jackson F.R.;
RT "Regulation of a specific circadian clock output pathway by lark, a
RT putative RNA-binding protein with repressor activity.";
RL J. Neurobiol. 31:117-128(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8307324; DOI=10.1093/genetics/135.4.1077;
RA Newby L.M., Jackson F.R.;
RT "A new biological rhythm mutant of Drosophila melanogaster that identifies
RT a gene with an essential embryonic function.";
RL Genetics 135:1077-1090(1993).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9491990; DOI=10.1016/s0896-6273(00)80457-2;
RA McNeil G.P., Zhang X., Genova G., Jackson F.R.;
RT "A molecular rhythm mediating circadian clock output in Drosophila.";
RL Neuron 20:297-303(1998).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF PHE-10; PHE-89; CYS-170 AND CYS-173.
RX PubMed=11560900; DOI=10.1093/genetics/159.1.229;
RA McNeil G.P., Schroeder A.J., Roberts M.A., Jackson F.R.;
RT "Genetic analysis of functional domains within the Drosophila LARK RNA-
RT binding protein.";
RL Genetics 159:229-240(2001).
RN [8]
RP FUNCTION.
RX PubMed=15452872; DOI=10.1002/gene.20069;
RA McNeil G.P., Smith F., Galioto R.;
RT "The Drosophila RNA-binding protein Lark is required for the organization
RT of the actin cytoskeleton and Hu-li tai shao localization during
RT oogenesis.";
RL Genesis 40:90-100(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-201; SER-315 AND
RP SER-325, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Essential RNA-binding protein. May be required for circadian
CC repression of eclosion. Also essential for nurse cell dumping during
CC oogenesis, the process whereby the cytoplasmic contents of nurse cells
CC are transferred to the oocyte late in it's development.
CC {ECO:0000269|PubMed:11560900, ECO:0000269|PubMed:15452872,
CC ECO:0000269|PubMed:8307324, ECO:0000269|PubMed:9120432,
CC ECO:0000269|PubMed:9491990}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9491990}. Nucleus
CC {ECO:0000269|PubMed:9491990}. Note=The precise location within neurons
CC varies according to the type of neuron, being cytoplasmic in CCAP
CC neurons and nuclear in the CNS.
CC -!- TISSUE SPECIFICITY: Expressed in the CNS and in CCAP neurons of the
CC ventral nervous system (VNS), which control insect ecdysis.
CC {ECO:0000269|PubMed:8307324, ECO:0000269|PubMed:9491990}.
CC -!- INDUCTION: Oscillates in abundance during the circadian cycle at the
CC protein level; peaks during the subjective day.
CC {ECO:0000269|PubMed:9491990}.
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DR EMBL; U59476; AAB07067.1; -; mRNA.
DR EMBL; AE014296; AAF50578.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12053.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12054.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12055.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12056.1; -; Genomic_DNA.
DR EMBL; AY061458; AAL29006.1; -; mRNA.
DR RefSeq; NP_523957.1; NM_079233.6.
DR RefSeq; NP_729237.1; NM_168202.3.
DR RefSeq; NP_729238.1; NM_168203.4.
DR RefSeq; NP_729239.1; NM_168204.3.
DR RefSeq; NP_729240.1; NM_168205.4.
DR AlphaFoldDB; Q94901; -.
DR SMR; Q94901; -.
DR BioGRID; 64251; 37.
DR IntAct; Q94901; 2.
DR STRING; 7227.FBpp0076555; -.
DR iPTMnet; Q94901; -.
DR PaxDb; Q94901; -.
DR PRIDE; Q94901; -.
DR DNASU; 38811; -.
DR EnsemblMetazoa; FBtr0076841; FBpp0076552; FBgn0011640.
DR EnsemblMetazoa; FBtr0076842; FBpp0076553; FBgn0011640.
DR EnsemblMetazoa; FBtr0076843; FBpp0076554; FBgn0011640.
DR EnsemblMetazoa; FBtr0076844; FBpp0076555; FBgn0011640.
DR EnsemblMetazoa; FBtr0076845; FBpp0076556; FBgn0011640.
DR GeneID; 38811; -.
DR KEGG; dme:Dmel_CG8597; -.
DR UCSC; CG8597-RA; d. melanogaster.
DR CTD; 38811; -.
DR FlyBase; FBgn0011640; lark.
DR VEuPathDB; VectorBase:FBgn0011640; -.
DR eggNOG; KOG0109; Eukaryota.
DR GeneTree; ENSGT00940000175488; -.
DR HOGENOM; CLU_045263_1_0_1; -.
DR InParanoid; Q94901; -.
DR OMA; ELNGMMV; -.
DR OrthoDB; 1563362at2759; -.
DR PhylomeDB; Q94901; -.
DR Reactome; R-DME-8941326; RUNX2 regulates bone development.
DR SignaLink; Q94901; -.
DR BioGRID-ORCS; 38811; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 38811; -.
DR PRO; PR:Q94901; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0011640; Expressed in wing disc and 27 other tissues.
DR Genevisible; Q94901; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
DR GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; IMP:UniProtKB.
DR GO; GO:0007562; P:eclosion; TAS:FlyBase.
DR GO; GO:0008062; P:eclosion rhythm; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045804; P:negative regulation of eclosion; IMP:UniProtKB.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:FlyBase.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:FlyBase.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Biological rhythms; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..352
FT /note="RNA-binding protein lark"
FT /id="PRO_0000081758"
FT DOMAIN 7..77
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 86..156
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 168..185
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 187..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 10
FT /note="F->A: Non-functional; when associated with A-89."
FT /evidence="ECO:0000269|PubMed:11560900"
FT MUTAGEN 89
FT /note="F->A: Defects in sensory bristle formation and wing
FT shape, and oogenesis. Non-functional; when associated with
FT A-10."
FT /evidence="ECO:0000269|PubMed:11560900"
FT MUTAGEN 170
FT /note="C->Y: Defects in sensory bristle formation and wing
FT shape, and oogenesis; when associated with Y-173."
FT /evidence="ECO:0000269|PubMed:11560900"
FT MUTAGEN 173
FT /note="C->Y: Defects in sensory bristle formation and wing
FT shape, and oogenesis; when associated with Y-170."
FT /evidence="ECO:0000269|PubMed:11560900"
SQ SEQUENCE 352 AA; 39912 MW; C8D698D4DD122FA9 CRC64;
MPGAGTFKLF IGNLDEKTQA TELRALFEKY GTVVECDVVK NYGFVHMETE QQGRDAIQNL
NGYTLNEFAI KVEAAKSRRA PNTPTTKIFV GNLTDKTRAP EVRELFQKYG TVVECDIVRN
YGFVHLDCVG DVQDAIKELN GRVVDGQPLK VQVSTSRVRP KPGMGDPEQC YRCGRSGHWS
KECPRLYGSA GGGREPPSPL SAGGYRDRMY GRDPYPPPPP PPPFLRDRIM DGFRDYDYYD
RRFEDSRDLY ERRYQTSRMR DFPPPPISRR EPMPLPPTLS GSLRSCSVSR GYDTMFSRRS
PPPPRSSNGM SRYGSPTPHG YEDFSRDAFD ERMISSRGMR GPSPPGRRYA PY
