LARP_DROME
ID LARP_DROME Reviewed; 1673 AA.
AC Q9VAW5; A4V3J4; D0IQE9; E1JJ02; Q8IMM4; Q8MSZ4; Q8MYR3; Q9NHN6; Q9VAW4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 5.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=La-related protein 1;
DE AltName: Full=dLarp;
GN Name=larp; ORFNames=CG42551;
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] (ISOFORM C), DEVELOPMENTAL STAGE, SUBCELLULAR
RP LOCATION, AND INITIATION CODON ATA.
RX PubMed=10878606;
RX DOI=10.1002/1097-0177(200007)218:3<401::aid-dvdy1009>3.0.co;2-6;
RA Chauvet S., Maurel-Zaffran C., Miassod R., Jullien N., Pradel J.,
RA Aragnol D.;
RT "dlarp, a new candidate Hox target in Drosophila whose orthologue in mouse
RT is expressed at sites of epithelium/mesenchymal interactions.";
RL Dev. Dyn. 218:401-413(2000).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM C), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 952-1673 (ISOFORMS A/C/D).
RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-356 (ISOFORM D).
RA Carlson J., Booth B., Frise E., Sandler J., Wan K., Yu C., Celniker S.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=14668392; DOI=10.1093/genetics/165.3.1433;
RA Clyne P.J., Brotman J.S., Sweeney S.T., Davis G.;
RT "Green fluorescent protein tagging Drosophila proteins at their native
RT genomic loci with small P elements.";
RL Genetics 165:1433-1441(2003).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=17951964; DOI=10.1247/csf.07027;
RA Ichihara K., Shimizu H., Taguchi O., Yamaguchi M., Inoue Y.H.;
RT "A Drosophila orthologue of larp protein family is required for multiple
RT processes in male meiosis.";
RL Cell Struct. Funct. 32:89-100(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-69; SER-562 AND
RP SER-851, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-102; THR-107;
RP SER-111; SER-112; SER-219; SER-221; SER-223; SER-229; SER-230; SER-236;
RP SER-284; SER-608; SER-1119; SER-1124; SER-1261; TYR-1315; SER-1510;
RP SER-1512; SER-1578; SER-1585 AND SER-1610, AND IDENTIFICATION BY MASS
RP 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).
RN [10]
RP RNA-BINDING, FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH PABP.
RX PubMed=19631203; DOI=10.1016/j.ydbio.2009.07.016;
RA Blagden S.P., Gatt M.K., Archambault V., Lada K., Ichihara K., Lilley K.S.,
RA Inoue Y.H., Glover D.M.;
RT "Drosophila Larp associates with poly(A)-binding protein and is required
RT for male fertility and syncytial embryo development.";
RL Dev. Biol. 334:186-197(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-66; THR-107;
RP SER-182; SER-186; SER-219; SER-221; THR-828; SER-1119; SER-1510 AND
RP SER-1512, AND MUTAGENESIS OF SER-66; THR-107; SER-182; SER-186;
RP 219-SER--SER-221; THR-828; SER-1119 AND 1510-SER--SER-1512.
RX PubMed=30772175; DOI=10.1016/j.molcel.2019.01.013;
RA Zhang Y., Wang Z.H., Liu Y., Chen Y., Sun N., Gucek M., Zhang F., Xu H.;
RT "PINK1 Inhibits Local Protein Synthesis to Limit Transmission of
RT Deleterious Mitochondrial DNA Mutations.";
RL Mol. Cell 73:1127-1137(2019).
CC -!- FUNCTION: RNA-binding protein required during male meiosis and
CC development of the syncytial embryo (PubMed:17951964, PubMed:19631203,
CC PubMed:30772175). Binds poly-(A) tails of mRNAs and regulates their
CC expression by regulating their stability or translation
CC (PubMed:17951964, PubMed:19631203). {ECO:0000269|PubMed:17951964,
CC ECO:0000269|PubMed:19631203, ECO:0000269|PubMed:30772175}.
CC -!- SUBUNIT: Interacts with pAbp. {ECO:0000269|PubMed:19631203}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:30772175}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:10878606,
CC ECO:0000269|PubMed:14668392, ECO:0000269|PubMed:17951964}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=D;
CC IsoId=Q9VAW5-3; Sequence=Displayed;
CC Name=C;
CC IsoId=Q9VAW5-1; Sequence=VSP_041775, VSP_041776;
CC Name=A; Synonyms=B, E;
CC IsoId=Q9VAW5-2; Sequence=VSP_015117;
CC -!- DEVELOPMENTAL STAGE: At the end of embryogenesis, accumulates in the
CC gut and muscles. {ECO:0000269|PubMed:10878606}.
CC -!- PTM: Phosphorylated on threonine and serine residues (PubMed:30772175).
CC During oogenesis, phosphorylation on Ser-1119 by Pink1 at the outer
CC membrane of defective mitochondria, impairs its ability to promote
CC local translation and mtDNA replication thus reducing transmission of
CC deleterious mtDNA mutations to the mature oocyte (PubMed:30772175).
CC {ECO:0000269|PubMed:30772175}.
CC -!- DISRUPTION PHENOTYPE: Mutant males show multiple meiotic phenotypes
CC such as a failure of chromosome segregation, cytokinesis and
CC mitochondrial partition. Defects in spindle pole organization and
CC spindle formation. Mutant-derived syncytial embryos show a range of
CC mitotic phenotypes, including failure of centrosomes to migrate around
CC the nuclear envelope, detachment of centrosomes from spindle poles, the
CC formation of multipolar spindle arrays and cytokinetic defects.
CC {ECO:0000269|PubMed:17951964, ECO:0000269|PubMed:19631203}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF35862.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ATA isoleucine codon.; Evidence={ECO:0000305};
CC Sequence=AAM29658.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM29658.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ATA isoleucine codon.; Evidence={ECO:0000305};
CC Sequence=AAM29658.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAM49837.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF221108; AAF35862.1; ALT_SEQ; mRNA.
DR EMBL; AE014297; AAF56783.3; -; Genomic_DNA.
DR EMBL; AE014297; AAN14138.5; -; Genomic_DNA.
DR EMBL; AE014297; AAN14139.1; -; Genomic_DNA.
DR EMBL; AE014297; ACZ95051.1; -; Genomic_DNA.
DR EMBL; AY113653; AAM29658.1; ALT_SEQ; mRNA.
DR EMBL; AY118468; AAM49837.1; ALT_INIT; mRNA.
DR EMBL; BT100187; ACY39986.1; -; mRNA.
DR RefSeq; NP_001163757.1; NM_001170286.3. [Q9VAW5-2]
DR RefSeq; NP_001247347.1; NM_001260418.2. [Q9VAW5-3]
DR RefSeq; NP_001247348.1; NM_001260419.2. [Q9VAW5-3]
DR RefSeq; NP_524998.1; NM_080259.3. [Q9VAW5-2]
DR RefSeq; NP_733244.5; NM_170365.4. [Q9VAW5-3]
DR RefSeq; NP_733245.1; NM_170366.4. [Q9VAW5-2]
DR AlphaFoldDB; Q9VAW5; -.
DR SMR; Q9VAW5; -.
DR BioGRID; 72798; 22.
DR IntAct; Q9VAW5; 22.
DR MINT; Q9VAW5; -.
DR STRING; 7227.FBpp0290398; -.
DR iPTMnet; Q9VAW5; -.
DR PaxDb; Q9VAW5; -.
DR PRIDE; Q9VAW5; -.
DR DNASU; 53567; -.
DR EnsemblMetazoa; FBtr0089680; FBpp0088622; FBgn0261618. [Q9VAW5-2]
DR EnsemblMetazoa; FBtr0089682; FBpp0088624; FBgn0261618. [Q9VAW5-2]
DR EnsemblMetazoa; FBtr0301180; FBpp0290398; FBgn0261618. [Q9VAW5-3]
DR EnsemblMetazoa; FBtr0301181; FBpp0290399; FBgn0261618. [Q9VAW5-2]
DR EnsemblMetazoa; FBtr0306389; FBpp0297481; FBgn0261618. [Q9VAW5-3]
DR EnsemblMetazoa; FBtr0306390; FBpp0297482; FBgn0261618. [Q9VAW5-3]
DR GeneID; 53567; -.
DR KEGG; dme:Dmel_CG42551; -.
DR UCSC; CG14066-RB; d. melanogaster.
DR CTD; 53567; -.
DR FlyBase; FBgn0261618; larp.
DR VEuPathDB; VectorBase:FBgn0261618; -.
DR eggNOG; KOG2590; Eukaryota.
DR GeneTree; ENSGT00940000169209; -.
DR InParanoid; Q9VAW5; -.
DR OMA; PTVWPIS; -.
DR PhylomeDB; Q9VAW5; -.
DR SignaLink; Q9VAW5; -.
DR BioGRID-ORCS; 53567; 0 hits in 3 CRISPR screens.
DR ChiTaRS; larp; fly.
DR GenomeRNAi; 53567; -.
DR PRO; PR:Q9VAW5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0261618; Expressed in wing disc and 50 other tissues.
DR ExpressionAtlas; Q9VAW5; baseline and differential.
DR Genevisible; Q9VAW5; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; IDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0000001; P:mitochondrion inheritance; IMP:FlyBase.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IMP:FlyBase.
DR GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; IMP:FlyBase.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR GO; GO:0007053; P:spindle assembly involved in male meiosis; IMP:FlyBase.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IMP:FlyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR006607; DM15.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 3.
DR Pfam; PF05383; La; 1.
DR SMART; SM00684; DM15; 3.
DR SMART; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Meiosis; Mitochondrion; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1673
FT /note="La-related protein 1"
FT /id="PRO_0000207613"
FT DOMAIN 723..814
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT REGION 35..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1542..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:30772175"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 107
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:30772175"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30772175"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30772175"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:30772175"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:30772175"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 828
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:30772175"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 1119
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:30772175"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1261
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1315
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1510
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:30772175"
FT MOD_RES 1512
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:30772175"
FT MOD_RES 1578
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1585
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1610
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..708
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_015117"
FT VAR_SEQ 1..270
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10878606,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_041775"
FT VAR_SEQ 271
FT /note="I -> M (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10878606,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_041776"
FT MUTAGEN 66
FT /note="S->A: Partially rescues mtDNA levels and hatching
FT rate in spoon null mutants; when associated with A-107. In
FT larp-10A, loss of phosphorylation by Pink1; when associated
FT with A-107; A-182; A-186; 219-A-A-221; A-828; A-1119 and
FT 1510-A-A-1512."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 66
FT /note="S->D: Phosphomimetic mutant, partially rescues mtDNA
FT levels and hatching rate in spoon null mutants; when
FT associated with D-107."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 107
FT /note="T->A: Partially rescues mtDNA levels and hatching
FT rate in spoon null mutants; when associated with A-66. In
FT larp-10A, loss of phosphorylation by Pink1; when associated
FT with A-66; A-182; A-186; 219-A-A-221; A-828; A-1119 and
FT 1510-A-A-1512."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 107
FT /note="T->D: Phosphomimetic mutant, partially rescues mtDNA
FT levels and hatching rate in spoon null mutants; when
FT associated with D-66."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 182
FT /note="S->A: Partially rescues mtDNA levels and hatching
FT rate in spoon null mutants; when associated with A-186. In
FT larp-10A, loss of phosphorylation by Pink1; when associated
FT with A-66; A-107; A-186; 219-A-A-221; A-828; A-1119 and
FT 1510-A-A-1512."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 182
FT /note="S->D: Phosphomimetic mutant, partially rescues mtDNA
FT levels and hatching rate in spoon null mutants; when
FT associated with D-186."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 186
FT /note="S->A: Partially rescues mtDNA levels and hatching
FT rate in spoon null mutants; when associated with A-182. In
FT larp-10A, loss of phosphorylation by Pink1; when associated
FT with A-66; A-107; A-182; 219-A-A-221; A-828; A-1119 and
FT 1510-A-A-1512."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 186
FT /note="S->D: Phosphomimetic mutant, partially rescues mtDNA
FT levels and hatching rate in spoon null mutants; when
FT associated with D-182."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 219..221
FT /note="SPS->APA: Partially rescues mtDNA levels and
FT hatching rate in spoon null mutants. In larp-10A, loss of
FT phosphorylation by Pink1; when associated with A-66; A-107;
FT A-182; A-186; A-828; A-1119 and 1510-A-A-1512."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 828
FT /note="T->A: Partially rescues mtDNA levels and hatching
FT rate in spoon null mutants. In larp-10A, loss of
FT phosphorylation by Pink1; when associated with A-66; A-107;
FT A-182; A-186; 219-A-A-221; A-1119 and 1510-A-A-1512."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 828
FT /note="T->D: Phosphomimetic mutant, partially rescues mtDNA
FT levels and hatching rate in spoon null mutants."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 1119
FT /note="S->A: Partially rescues nascent protein synthesis
FT and PolG1 expression in mitochondria containing deleterious
FT mutations. Partially rescues mtDNA levels and hatching rate
FT in spoon null mutants. In larp-10A, loss of phosphorylation
FT by Pink1; when associated with A-66; A-107; A-182; A-186;
FT 219-A-A-221; A-828 and 1510-A-A-1512."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 1119
FT /note="S->D: Phosphomimetic mutant, severe reduction in
FT ability to rescue mtDNA levels and hatching rate in spoon
FT null mutants."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 1510..1512
FT /note="SVS->AVA: Partially rescues mtDNA levels and
FT hatching rate in spoon null mutants. In larp-10A, loss of
FT phosphorylation by Pink1; when associated with A-66; A-107;
FT A-182; A-186; 219-A-A-221; A-828 and A-1119."
FT /evidence="ECO:0000269|PubMed:30772175"
FT MUTAGEN 1510..1512
FT /note="SVS->DVD: Phosphomimetic mutant, partially rescues
FT mtDNA levels and hatching rate in spoon null mutants."
FT /evidence="ECO:0000269|PubMed:30772175"
FT CONFLICT 21
FT /note="A -> V (in Ref. 5; ACY39986)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="G -> D (in Ref. 5; ACY39986)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="V -> A (in Ref. 5; ACY39986)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="A -> T (in Ref. 5; ACY39986)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="A -> V (in Ref. 5; ACY39986)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..352
FT /note="AT -> TA (in Ref. 5; ACY39986)"
FT /evidence="ECO:0000305"
FT CONFLICT 355..356
FT /note="TT -> KA (in Ref. 5; ACY39986)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="P -> A (in Ref. 4; AAM29658)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="P -> S (in Ref. 1; AAF35862)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="S -> R (in Ref. 1; AAF35862)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="A -> E (in Ref. 4; AAM29658)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="T -> A (in Ref. 4; AAM29658)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="S -> T (in Ref. 4; AAM29658)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="Y -> H (in Ref. 4; AAM29658)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="N -> T (in Ref. 1; AAF35862 and 4; AAM29658)"
FT /evidence="ECO:0000305"
FT CONFLICT 1100
FT /note="L -> V (in Ref. 1; AAF35862)"
FT /evidence="ECO:0000305"
FT CONFLICT 1648
FT /note="T -> A (in Ref. 1; AAF35862 and 4; AAM49837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1673 AA; 178145 MW; D865CDA3103B1429 CRC64;
MSSKEETPST GGAAPVATVA ASGSATTSYA NVVQNLETKK SGTSNTTTTT ARATVDNKEN
QPNLKSFKSW SEEAAAAEAA GESPIVGSVS LAQTGEKRAA ASGGDNTAEN SSELDDNNDF
VPVLSHHRRD RKKARKEKPR DQQPAGGRGD GQKPQQAGGR RVPGSSDTER KSVRPRAPRG
GSPRKSAAGA AGAAGSNAGA VSSAVPGGPK VHKDRKDTSP SASIEGAGSS GNEAKSADGD
QQAGEKGAAG AAPPPKRFIA APPPKVNAWK ISAKQSGSPK AGTSPLDKRV LQPKAQQQQQ
QTKQTASQNN NAQNTASNKK TQQQQQPQQG ATTTTQTTTA AAAAATAAAA ATAATTSAAA
ATSSAAAVPA ATTETATTTT VDASQADALA KVVVKDKKKV NQKASDFSNV GDWPTLIGGT
SGSGKATSNE PKRNPTKKQQ SAKTAAAVAA SSNTTSSEVA TESNVAGTTS SSNSNPSSST
TTTNTTTNSQ ATTAPVASTS HDAKAQRDAE PAANSAAGTT GTAAGPALTK KIPKHKWRPL
PIDLAKSSRP KPIGGRPNRR FSDDIADQRR PPRVYHDRQP GAGGAGVESR HPHAGRHPYG
SRPATATSER VDSWRSSSST TTAAFDEQRS GAAGGAGAAG TGVGSATRGP RRYRTPYRGG
RQGRGGFSRQ GPGRPTYRIP RHLLASGEYA NYLPADAAGA DSQSSYVLMG THYFGNVPAA
YIELDANSIK EAIKKQVEYY FSVDNLTGDF FLRRKMDPEG YIPVTLIASF HRVLALTTDV
AVIVNAIKES DKLELFEGYK VRTKTTPTTW PITEVPEVNE GEPKAIGTLE QEQLEQNDGQ
EKLEEQTEAD SPPPILTSAM ATKPLNSIPP PPMPRNPQNL VPKMLQDKQQ SRSSTIAALN
SVNAISALTQ QVEGGAAELA GHLSGLAESV KPKSTSTPDK RNAASAGNGA GSAAALVAEP
EGIWKEVKRR SKTNAIKENA TTPPQQQQPP LSQTLNNNND NVKTNNTSSK SKSSSNNAPS
NASSSATVCV TTNNASSATK ATTKTTTTST ATTTTNNNIK SGNAAYSKTH SKSSSKTAAP
PSAQCHAEKE ELDFQFDEEL MDPLPPGTGR INNFTENFSD DDESDYEFAD RDINKLLIVA
QVGRAPKHEG YDRTADFTSR TKITQDLENI INDGLVNYEE DLWTTTNVVA DYKTVNVISQ
ADFEKLAGGR NKSVLPPQVV PPPPPFEEDL DETLVGDTTL NSTLNNTLKS RRARFYAAPN
SHSIDPRTPR KRKLRHTANP PVEAHVGWLL DTVEHRPRTT SMGSSAGTSP TASSYGSFGS
SVPQSLPVFQ HPSHALLKEN NFTQQAYHKY HSRCLKERRR LGYGQSQEMN TLYRFWSFFL
RENFNKSMYN EFRSLALEDA GNGFRYGLEC LFRFFSYGLE KKFRPNIYQD FQDETIADYE
TGQLYGLEKF WAFLKYYKNG EKLEVQPKLA EYLKSFKNIE DFRVVEPEIN EMLQGVGSLN
PGRQLNRHRS VSESDGTAVI AAGGRRLNTT ITNRSDYVGR LLQQQHQQQQ QQQHHQYQQG
YGGYNQQQNR RRTGSFGSTT VRIRSGSLGN KPQVANRNQG SQHELRRGGS NSGLAPHKRQ
QQQKPKPGAG SQTGSTRATT SAAATATTAA SAATSTAATP AVTVSSGSSS SKK
