ABCE1_DROME
ID ABCE1_DROME Reviewed; 611 AA.
AC Q9VSS1;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Protein Pixie {ECO:0000312|FlyBase:FBgn0086706};
DE AltName: Full=ATP-binding cassette sub-family E member 1 {ECO:0000303|PubMed:25128630};
GN Name=pix {ECO:0000312|FlyBase:FBgn0086706};
GN Synonyms=ABCE1 {ECO:0000312|FlyBase:FBgn0086706};
GN ORFNames=CG5651 {ECO:0000312|FlyBase:FBgn0086706};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
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 [2] {ECO:0000312|Proteomes:UP000000803}
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 [3] {ECO:0000312|EMBL:AAL90382.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL90382.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL90382.1};
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP PRO-38; ALA-77; PRO-146 AND GLN-231.
RX PubMed=16291791; DOI=10.1242/dev.02148;
RA Coelho C.M., Kolevski B., Bunn C., Walker C., Dahanukar A., Leevers S.J.;
RT "Growth and cell survival are unevenly impaired in pixie mutant wing
RT discs.";
RL Development 132:5411-5424(2005).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH EIF3A; EIF3J; EIF3B; EIF3C AND EIF3I,
RP ASSOCIATION WITH THE 40S RIBOSOME, DOMAIN, AND MUTAGENESIS OF GLU-503.
RX PubMed=17392269; DOI=10.1074/jbc.m701361200;
RA Andersen D.S., Leevers S.J.;
RT "The essential Drosophila ATP-binding cassette domain protein, pixie, binds
RT the 40 S ribosome in an ATP-dependent manner and is required for
RT translation initiation.";
RL J. Biol. Chem. 282:14752-14760(2007).
RN [6]
RP FUNCTION, AND INTERACTION WITH GIT AND PAK.
RX PubMed=18996366; DOI=10.1016/j.ydbio.2008.09.001;
RA Bahri S.M., Choy J.M., Manser E., Lim L., Yang X.;
RT "The Drosophila homologue of Arf-GAP GIT1, dGIT, is required for proper
RT muscle morphogenesis and guidance during embryogenesis.";
RL Dev. Biol. 325:15-23(2009).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=25128630; DOI=10.1016/j.biochi.2014.08.001;
RA Kashima I., Takahashi M., Hashimoto Y., Sakota E., Nakamura Y., Inada T.;
RT "A functional involvement of ABCE1, eukaryotic ribosome recycling factor,
RT in nonstop mRNA decay in Drosophila melanogaster cells.";
RL Biochimie 106:10-16(2014).
RN [8] {ECO:0000305}
RP FUNCTION, AND UBIQUITINATION.
RX PubMed=29861391; DOI=10.1016/j.cmet.2018.05.007;
RA Wu Z., Wang Y., Lim J., Liu B., Li Y., Vartak R., Stankiewicz T.,
RA Montgomery S., Lu B.;
RT "Ubiquitination of ABCE1 by NOT4 in Response to Mitochondrial Damage Links
RT Co-translational Quality Control to PINK1-Directed Mitophagy.";
RL Cell Metab. 28:130-144.e7(2018).
CC -!- FUNCTION: Plays a role in translation initiation and quality control of
CC translation (PubMed:16291791, PubMed:17392269, PubMed:29861391).
CC Together with pelo and HBS1, is required for 48S complex formation from
CC 80S ribosomes and dissociation of vacant 80S ribosomes
CC (PubMed:17392269). Stabilizes core components of eIF3 complex promoting
CC their assembly into translation initiation-competent complexes
CC (PubMed:17392269). Together with pelo and HBS1, recognizes stalled
CC ribosomes and promotes dissociation of elongation complexes assembled
CC on non-stop mRNAs; this triggers endonucleolytic cleavage of the mRNA,
CC a mechanism to release non-functional ribosomes and to degrade damaged
CC mRNAs as part of the No-Go Decay (NGD) pathway (PubMed:25128630). Plays
CC a role in the regulation of mRNA turnover (By similarity). Plays a role
CC in quality control of translation of mitochondrial outer membrane-
CC localized mRNA (PubMed:29861391). As part of the Pink1-regulated
CC signaling, ubiquitinated by Cnot4 upon mitochondria damage; this
CC modification generates polyubiquitin signals that recruits autophagy
CC receptors to the mitochondrial outer membrane to initiate mitophagy
CC (PubMed:29861391). Required in the wing disk for cell division and
CC growth as well as cell survival (PubMed:16291791). During muscle
CC embryogenesis, required for the recruitment of Pak to muscle
CC attachments in the embryo, hence may play a role in proper muscle
CC morphogenesis and proper guidance and targeting of subsets of myotubes
CC (PubMed:18996366). {ECO:0000250|UniProtKB:P61221,
CC ECO:0000269|PubMed:16291791, ECO:0000269|PubMed:17392269,
CC ECO:0000269|PubMed:18996366, ECO:0000269|PubMed:25128630,
CC ECO:0000269|PubMed:29861391}.
CC -!- SUBUNIT: Interacts with components of eIF3 complex, namely eIF3a,
CC eIF3j, eIF3b, eIF3c and eIF3i (PubMed:17392269). Associates with the
CC 40S ribosome subunit in an ATP-dependent manner and independently from
CC the presence of the eIF3 complex (PubMed:17392269). Forms a complex
CC with Git and Pak; the interaction with Pak may be mediated by pix/dPIX
CC (PubMed:18996366). {ECO:0000269|PubMed:17392269,
CC ECO:0000269|PubMed:18996366}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16291791}.
CC -!- TISSUE SPECIFICITY: Expressed in early and late larval imaginal disks
CC (at protein level). {ECO:0000269|PubMed:16291791}.
CC -!- DOMAIN: The ABC transporter 2 domain is necessary and sufficient for
CC association to the 40S ribosome subunit. {ECO:0000269|PubMed:17392269}.
CC -!- PTM: Ubiquitinated by Cnot4 (PubMed:29861391). Ubiquitination mediates
CC the recruitment of autophagy receptors to the mitochondrial outer
CC membrane and initiates mitophagy (PubMed:29861391).
CC {ECO:0000269|PubMed:29861391}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCE family.
CC {ECO:0000305}.
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DR EMBL; AE014296; AAF50342.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11979.1; -; Genomic_DNA.
DR EMBL; AY089644; AAL90382.1; -; mRNA.
DR RefSeq; NP_648272.1; NM_140015.3.
DR RefSeq; NP_729435.1; NM_168306.2.
DR AlphaFoldDB; Q9VSS1; -.
DR SMR; Q9VSS1; -.
DR IntAct; Q9VSS1; 9.
DR STRING; 7227.FBpp0076284; -.
DR PaxDb; Q9VSS1; -.
DR PRIDE; Q9VSS1; -.
DR DNASU; 39027; -.
DR EnsemblMetazoa; FBtr0076557; FBpp0076284; FBgn0086706.
DR EnsemblMetazoa; FBtr0076558; FBpp0076285; FBgn0086706.
DR GeneID; 39027; -.
DR KEGG; dme:Dmel_CG5651; -.
DR UCSC; CG5651-RA; d. melanogaster.
DR CTD; 39027; -.
DR FlyBase; FBgn0086706; pix.
DR VEuPathDB; VectorBase:FBgn0086706; -.
DR eggNOG; KOG0063; Eukaryota.
DR GeneTree; ENSGT00390000015089; -.
DR HOGENOM; CLU_017344_4_1_1; -.
DR InParanoid; Q9VSS1; -.
DR OMA; VCVQQAD; -.
DR OrthoDB; 359213at2759; -.
DR PhylomeDB; Q9VSS1; -.
DR BioGRID-ORCS; 39027; 1 hit in 1 CRISPR screen.
DR ChiTaRS; pix; fly.
DR GenomeRNAi; 39027; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0086706; Expressed in eye disc (Drosophila) and 23 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IMP:FlyBase.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:FlyBase.
DR GO; GO:0031369; F:translation initiation factor binding; IPI:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:FlyBase.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IGI:FlyBase.
DR GO; GO:0001558; P:regulation of cell growth; IMP:FlyBase.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0032790; P:ribosome disassembly; ISS:FlyBase.
DR GO; GO:0006412; P:translation; IMP:FlyBase.
DR GO; GO:0006413; P:translational initiation; IMP:FlyBase.
DR GO; GO:0006415; P:translational termination; IBA:GO_Central.
DR CDD; cd03236; ABC_RNaseL_inhibitor_domain1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013283; RLI1.
DR InterPro; IPR034348; RLI_dom_1.
DR InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom.
DR PANTHER; PTHR19248; PTHR19248; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF04068; RLI; 1.
DR PRINTS; PR01868; ABCEFAMILY.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; ATP-binding; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Nucleotide-binding; Reference proteome; Translation regulation;
KW Ubl conjugation.
FT CHAIN 1..611
FT /note="Protein Pixie"
FT /id="PRO_0000451862"
FT DOMAIN 15..45
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 54..83
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 78..323
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 350..570
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 118..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 387..394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 38
FT /note="P->L: Larval lethal. Viable but with reduced body
FT and bristle size; when associated with L-146."
FT /evidence="ECO:0000269|PubMed:16291791"
FT MUTAGEN 77
FT /note="A->T: Embryonic lethal. Viable but with reduced body
FT and bristle size; when associated with L-146."
FT /evidence="ECO:0000269|PubMed:16291791"
FT MUTAGEN 146
FT /note="P->L: Does not affect development. Viable but with
FT reduced body and bristle size; when associated with L-38 or
FT T-77."
FT /evidence="ECO:0000269|PubMed:16291791"
FT MUTAGEN 231
FT /note="Q->L: Embryonic lethal."
FT /evidence="ECO:0000269|PubMed:16291791"
FT MUTAGEN 503
FT /note="E->Q: Constitutively associates with the 40S
FT ribosomal subunit."
FT /evidence="ECO:0000269|PubMed:17392269"
SQ SEQUENCE 611 AA; 69298 MW; F4747F4D69F9E1C2 CRC64;
MSRRKENEEV DKQTRIAIVS DDKCKPKRCR QECKKTCPVV RMGKLCIEVT PTSKIASLSE
ELCIGCGICV KKCPFEAITI INLPSNLEKH TTHRYSKNSF KLHRLPIPRP GEVLGLVGQN
GIGKSTALKI LAGKQKPNLG KYANPPDWTE ILSYFRGSEL QNYFTKILED NLKALVKPQY
VDQIPKAVRG AVGDLLDKKD ERELQTKICE MLDLSHIRDR EIAQLSGGEL QRFAIAMVCI
QNADIFMFDE PSSYLDVKQR LNAALTIRSL LHPTKFIIVV EHDLSVLDYL SDFICCLYGV
PGCYGVVTMP FSVREGINIF LDGFVPTENM RFRTESLTFK VSESATEEEI KRMNHYVYPA
MVKTLGKFEL TVEKGHFSDS EILVLLGENG TGKTTFIRML AGNLQPDGEV ELPMLNISYK
PQKISPKFQN HVRHLLHDKI RDAYVHPQFI ADVMKPMKIE EIMDQEVQNL SGGELQRVAL
VLCLGKPADV YLIDEPSAYL DSEQRLVAAK VIKRYILHAK KTGFVVEHDF IMATYLADRV
IVIEGQPSVK TTAFSPQSLL NGMNRFLELL GITFRRDPNN FRPRINKNNS VKDTEQKRSG
QFFFLEDEAC N
