ARI1_DROME
ID ARI1_DROME Reviewed; 503 AA.
AC Q94981; Q0KHQ9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=E3 ubiquitin-protein ligase ariadne-1 {ECO:0000303|PubMed:29689197};
DE EC=2.3.2.31 {ECO:0000269|PubMed:21900267, ECO:0000269|PubMed:29689197};
DE AltName: Full=Protein ariadne-1 {ECO:0000303|PubMed:10880484};
DE AltName: Full=RING-type E3 ubiquitin transferase ariadne-1 {ECO:0000305};
GN Name=ari-1 {ECO:0000303|PubMed:10880484, ECO:0000312|FlyBase:FBgn0017418};
GN Synonyms=ari, ari-1a {ECO:0000303|PubMed:21900267};
GN ORFNames=CG5659 {ECO:0000312|FlyBase:FBgn0017418};
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 [GENOMIC DNA / MRNA], FUNCTION, SUBUNIT, INTERACTION
RP WITH UBC10, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF CYS-150 AND CYS-309.
RC STRAIN=Oregon-R;
RX PubMed=10880484; DOI=10.1093/genetics/155.3.1231;
RA Aguilera M., Oliveros M., Martinez-Padron M., Barbas J.A., Ferrus A.;
RT "Ariadne-1: a vital Drosophila gene is required in development and defines
RT a new conserved family of ring-finger proteins.";
RL Genetics 155:1231-1244(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.
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 FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ECR (ISOFORM ECR-A), AND
RP SUBCELLULAR LOCATION.
RX PubMed=21900267; DOI=10.1534/genetics.111.132191;
RA Gradilla A.C., Mansilla A., Ferrus A.;
RT "Isoform-specific regulation of a steroid hormone nuclear receptor by an E3
RT ubiquitin ligase in Drosophila melanogaster.";
RL Genetics 189:871-883(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH UBC10; KOI; PARK
RP AND ARI-2, TISSUE SPECIFICITY, DOMAIN, AUTOPHOSPHORYLATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF CYS-136; VAL-187; CYS-223; CYS-304; SER-332;
RP PHE-377; GLU-378 AND GLU-450.
RX PubMed=29689197; DOI=10.1016/j.devcel.2018.03.020;
RG University of Washington Center for Mendelian Genomics;
RA Tan K.L., Haelterman N.A., Kwartler C.S., Regalado E.S., Lee P.T.,
RA Nagarkar-Jaiswal S., Guo D.C., Duraine L., Wangler M.F., Bamshad M.J.,
RA Nickerson D.A., Lin G., Milewicz D.M., Bellen H.J.;
RT "Ari-1 Regulates Myonuclear Organization Together with Parkin and Is
RT Associated with Aortic Aneurysms.";
RL Dev. Cell 45:226-244(2018).
CC -!- FUNCTION: Atypical E3 ubiquitin-protein ligase, which catalyzes
CC ubiquitination of target proteins together with ubiquitin-conjugating
CC enzyme E2 Ubc10 (PubMed:10880484, PubMed:21900267, PubMed:29689197).
CC Controls the subcellular localization and morphology of muscle nuclei
CC (myonuclei) by regulating the protein levels and distribution of the
CC LINC (LInker of Nucleoskeleton and Cytoskeleton) complex
CC (PubMed:29689197). Functions by mediating the monoubiquitination of the
CC LINC complex subunit koi leading to its subsequent proteasomal
CC degradation (PubMed:29689197). Appears to function, at least partially
CC redundantly, with the RBR E3 ligase family member park in nuclear
CC localization and morphology (PubMed:29689197). Likely to function in
CC metamorphosis by regulating the proteins levels of EcR isoform A (ECR-
CC A) and its heterodimeric partner usp, via the ubiquitination and
CC subsequent degradation of ECR-A (PubMed:21900267).
CC {ECO:0000269|PubMed:10880484, ECO:0000269|PubMed:21900267,
CC ECO:0000269|PubMed:29689197}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000269|PubMed:21900267,
CC ECO:0000269|PubMed:29689197};
CC -!- SUBUNIT: Can form homodimers (PubMed:10880484, PubMed:29689197).
CC Interacts (via RING-type 1 zinc finger) with Ubc10 (PubMed:10880484,
CC PubMed:29689197). Interacts with the LINC complex member koi
CC (PubMed:29689197). Interacts with park (PubMed:29689197). Interacts
CC with ari-2 (PubMed:29689197). Specifically interacts with isoform ECR-A
CC of EcR (PubMed:21900267). {ECO:0000269|PubMed:10880484,
CC ECO:0000269|PubMed:21900267, ECO:0000269|PubMed:29689197}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10880484}. Nucleus
CC {ECO:0000269|PubMed:21900267}. Note=Mainly cytoplasmic.
CC {ECO:0000269|PubMed:10880484}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with prominent levels in the
CC nervous system and female gonads. {ECO:0000269|PubMed:10880484,
CC ECO:0000269|PubMed:29689197}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all tissues throughout development,
CC with maximum levels reached during metamorphosis and maintained in the
CC adult. {ECO:0000269|PubMed:10880484}.
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC interact with E2 conjugating enzymes such as Ubc10 and function like
CC HECT-type E3 enzymes: they bind E2s via the first RING-type zinc
CC finger, but require an obligate trans-thiolation step during the
CC ubiquitin transfer, requiring a conserved active site Cys residue in
CC the second RING-type zinc finger. The active site probably forms a
CC thioester intermediate with ubiquitin taken from the active-site
CC cysteine of the E2 before ultimately transferring it to a Lys residue
CC on the substrate. {ECO:0000269|PubMed:29689197}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:29689197}.
CC -!- DISRUPTION PHENOTYPE: Pharate pupae lethal. Larval muscles exhibit an
CC increase in nuclear clustering. {ECO:0000269|PubMed:29689197}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000305}.
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DR EMBL; X98309; CAA66953.1; -; Genomic_DNA.
DR EMBL; X98310; CAA66954.1; -; mRNA.
DR EMBL; AE014298; AAN09462.1; -; Genomic_DNA.
DR RefSeq; NP_001245736.1; NM_001258807.3.
DR RefSeq; NP_001259671.1; NM_001272742.2.
DR RefSeq; NP_001259672.1; NM_001272743.1.
DR RefSeq; NP_523399.1; NM_078675.4.
DR RefSeq; NP_728145.1; NM_167610.4.
DR RefSeq; NP_996500.1; NM_206777.2.
DR AlphaFoldDB; Q94981; -.
DR SMR; Q94981; -.
DR BioGRID; 59116; 13.
DR DIP; DIP-17812N; -.
DR IntAct; Q94981; 1.
DR STRING; 7227.FBpp0297199; -.
DR PaxDb; Q94981; -.
DR PRIDE; Q94981; -.
DR EnsemblMetazoa; FBtr0089506; FBpp0088499; FBgn0017418.
DR EnsemblMetazoa; FBtr0089507; FBpp0088500; FBgn0017418.
DR EnsemblMetazoa; FBtr0089508; FBpp0089023; FBgn0017418.
DR EnsemblMetazoa; FBtr0306057; FBpp0297199; FBgn0017418.
DR EnsemblMetazoa; FBtr0332850; FBpp0305073; FBgn0017418.
DR EnsemblMetazoa; FBtr0332851; FBpp0305074; FBgn0017418.
DR GeneID; 32796; -.
DR KEGG; dme:Dmel_CG5659; -.
DR UCSC; CG5659-RA; d. melanogaster.
DR CTD; 32796; -.
DR FlyBase; FBgn0017418; ari-1.
DR VEuPathDB; VectorBase:FBgn0017418; -.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000155744; -.
DR HOGENOM; CLU_009823_4_2_1; -.
DR InParanoid; Q94981; -.
DR OMA; CAAHACD; -.
DR OrthoDB; 469819at2759; -.
DR PhylomeDB; Q94981; -.
DR Reactome; R-DME-1169408; ISG15 antiviral mechanism.
DR SignaLink; Q94981; -.
DR BioGRID-ORCS; 32796; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 32796; -.
DR PRO; PR:Q94981; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0017418; Expressed in cleaving embryo and 23 other tissues.
DR ExpressionAtlas; Q94981; baseline and differential.
DR Genevisible; Q94981; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:FlyBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IMP:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:FlyBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00647; IBR; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..503
FT /note="E3 ubiquitin-protein ligase ariadne-1"
FT /id="PRO_0000055754"
FT ZN_FING 133..183
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 203..264
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 291..322
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..340
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 133..201
FT /note="Important for interaction with Ubc10"
FT /evidence="ECO:0000269|PubMed:10880484"
FT COILED 341..361
FT /evidence="ECO:0000255"
FT ACT_SITE 304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT MUTAGEN 136
FT /note="C->Y: In ari-1a; Loss of catalytic activity. Late
FT pupal lethal and adult escapers have a reduced lifespan and
FT thinner bristles. Nuclei in larval muscles (myonuclei) are
FT displaced from the cell membrane, exhibit clustering and
FT morphological defects, likely due to the mislocalization of
FT the LINC complex. Reduced degradation of the LINC complex
FT member koi."
FT /evidence="ECO:0000269|PubMed:29689197"
FT MUTAGEN 150
FT /note="C->Y: In ari1-2; lethal phenotype and loss of
FT interaction with Ubc10."
FT /evidence="ECO:0000269|PubMed:10880484"
FT MUTAGEN 187
FT /note="V->E: In ari-1b; Loss of catalytic activity. Late
FT pupal lethal and adult escapers have a reduced lifespan and
FT thinner bristles. Nuclei in larval muscles (myonuclei) are
FT displaced from the cell membrane, exhibit clustering and
FT morphological defects, likely due to the mislocalization of
FT the LINC complex; when associated with P-332."
FT /evidence="ECO:0000269|PubMed:29689197"
FT MUTAGEN 223
FT /note="C->S: In ari-1d; late pupal lethal and adult
FT escapers have a reduced lifespan and thinner bristles.
FT Nuclei in larval muscles (myonuclei) are displaced from the
FT cell membrane, exhibit clustering and morphological
FT defects."
FT /evidence="ECO:0000269|PubMed:29689197"
FT MUTAGEN 304
FT /note="C->S: Loss of catalytic activity and impaired
FT autoinhibition; when associated with A-377; A-378 and A-
FT 450."
FT /evidence="ECO:0000269|PubMed:29689197"
FT MUTAGEN 309
FT /note="C->Y: In ari1-3; lethal phenotype and no loss of
FT interaction with Ubc10."
FT /evidence="ECO:0000269|PubMed:10880484"
FT MUTAGEN 332
FT /note="S->P: In ari-1b; Loss of catalytic activity. Late
FT pupal lethal and adult escapers have a reduced lifespan and
FT thinner bristles. Nuclei in larval muscles (myonuclei) are
FT displaced from the cell membrane, exhibit clustering and
FT morphological defects, likely due to the mislocalization of
FT the LINC complex; when associated with E-187."
FT /evidence="ECO:0000269|PubMed:29689197"
FT MUTAGEN 377
FT /note="F->A: Impairs autoinhibition; when associated with
FT A-378 and A-450. Loss of activity and impaired
FT autoinhibition; when associated with A-378; A-450 and S-
FT 304."
FT /evidence="ECO:0000269|PubMed:29689197"
FT MUTAGEN 378
FT /note="E->A: Impairs autoinhibition; when associated with
FT A-377 and A-450. Loss of activity and impaired
FT autoinhibition; when associated with A-377; A-450 and S-
FT 304."
FT /evidence="ECO:0000269|PubMed:29689197"
FT MUTAGEN 450
FT /note="E->A: Impairs autoinhibition; when associated with
FT A-377 and A-378. Loss of activity and impaired
FT autoinhibition; when associated with A-377; A-378 and S-
FT 304."
FT /evidence="ECO:0000269|PubMed:29689197"
SQ SEQUENCE 503 AA; 58932 MW; 0AECCE256CF5EC00 CRC64;
MDSDNDNDFC DNVDSGNVSS GDDGDDDFGM EVDLPSSADR QMDQDDYQYK VLTTDEIVQH
QREIIDEANL LLKLPTPTTR ILLNHFKWDK EKLLEKYFDD NTDEFFKCAH VINPFNATEA
IKQKTSRSQC EECEICFSQL PPDSMAGLEC GHRFCMPCWH EYLSTKIVAE GLGQTISCAA
HGCDILVDDV TVANLVTDAR VRVKYQQLIT NSFVECNQLL RWCPSVDCTY AVKVPYAEPR
RVHCKCGHVF CFACGENWHD PVKCRWLKKW IKKCDDDSET SNWIAANTKE CPRCSVTIEK
DGGCNHMVCK NQNCKNEFCW VCLGSWEPHG SSWYNCNRYD EDEAKTARDA QEKLRSSLAR
YLHYYNRYMN HMQSMKFENK LYASVKQKME EMQQHNMSWI EVQFLKKAVD ILCQCRQTLM
YTYVFAYYLK KNNQSMIFED NQKDLESATE MLSEYLERDI TSENLADIKQ KVQDKYRYCE
KRCSVLLKHV HEGYDKEWWE YTE
