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CEP89_DROME
ID   CEP89_DROME             Reviewed;         476 AA.
AC   Q7JVA5;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Protein Cep89 homolog;
GN   Name=Cep89; ORFNames=CG8214;
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 [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]
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Larva, and Pupae;
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]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23575228; DOI=10.1093/hmg/ddt170;
RA   van Bon B.W., Oortveld M.A., Nijtmans L.G., Fenckova M., Nijhof B.,
RA   Besseling J., Vos M., Kramer J.M., de Leeuw N., Castells-Nobau A.,
RA   Asztalos L., Viragh E., Ruiter M., Hofmann F., Eshuis L., Collavin L.,
RA   Huynen M.A., Asztalos Z., Verstreken P., Rodenburg R.J., Smeitink J.A.,
RA   de Vries B.B., Schenck A.;
RT   "CEP89 is required for mitochondrial metabolism and neuronal function in
RT   man and fly.";
RL   Hum. Mol. Genet. 22:3138-3151(2013).
CC   -!- FUNCTION: Required for mitochondrial complex IV activity. May be
CC       involved in non-associative learning. {ECO:0000269|PubMed:23575228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Mitochondrion
CC       intermembrane space {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown of the protein causes
CC       complete lethality at a late pupal stage. Muscle-specific knockdown is
CC       lethal under strongly induced conditions, but shows no obvious
CC       alteration in locomotion and behavior under mild induction conditions.
CC       Neuron-specific knockdown flies show striking motor defects. Analysis
CC       of synaptic and subsynaptic organization at larval neuromuscular
CC       junction shows normal overall synapse morphology, but a highly
CC       significant decrease in the amount of active zones, i.e. presynaptic
CC       microdomains of neurotransmitter release. Muscle size is smaller in
CC       knockdown animals compared to wild-type. Neuron-specific knockdown
CC       flies show decreased ability for non-associative learning, tested by
CC       non-associative jump-reflex habituation. Wing-specific knockdown
CC       produces flies with a dramatically reduced wing size. Eye-specific
CC       knockdown disturbs ommatidia and bristle organization and corrupts
CC       integrity of mitochondria. Electroretinograms show a gross defect in
CC       basal neurotransmission. {ECO:0000269|PubMed:23575228}.
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DR   EMBL; AE013599; AAF58113.1; -; Genomic_DNA.
DR   EMBL; AY119085; AAM50945.1; -; mRNA.
DR   RefSeq; NP_611053.1; NM_137209.4.
DR   AlphaFoldDB; Q7JVA5; -.
DR   SMR; Q7JVA5; -.
DR   BioGRID; 62466; 1.
DR   IntAct; Q7JVA5; 3.
DR   STRING; 7227.FBpp0086454; -.
DR   PaxDb; Q7JVA5; -.
DR   DNASU; 36733; -.
DR   EnsemblMetazoa; FBtr0087320; FBpp0086454; FBgn0266708.
DR   GeneID; 36733; -.
DR   KEGG; dme:Dmel_CG8214; -.
DR   UCSC; CG8214-RA; d. melanogaster.
DR   CTD; 84902; -.
DR   FlyBase; FBgn0266708; Cep89.
DR   VEuPathDB; VectorBase:FBgn0266708; -.
DR   eggNOG; ENOG502QWK8; Eukaryota.
DR   HOGENOM; CLU_503635_0_0_1; -.
DR   OMA; QHKESQL; -.
DR   OrthoDB; 476357at2759; -.
DR   PhylomeDB; Q7JVA5; -.
DR   BioGRID-ORCS; 36733; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 36733; -.
DR   PRO; PR:Q7JVA5; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0266708; Expressed in testis and 6 other tissues.
DR   Genevisible; Q7JVA5; DM.
DR   GO; GO:0005814; C:centriole; IBA:GO_Central.
DR   GO; GO:0097539; C:ciliary transition fiber; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR   GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR   GO; GO:0046959; P:habituation; IMP:FlyBase.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:FlyBase.
DR   InterPro; IPR033545; CEP89.
DR   PANTHER; PTHR36170; PTHR36170; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Mitochondrion; Reference proteome.
FT   CHAIN           1..476
FT                   /note="Protein Cep89 homolog"
FT                   /id="PRO_0000423045"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   476 AA;  54448 MW;  BB85196F14A1CCE9 CRC64;
     MSTRNVMITD LDQPDPNQQQ HHQNPKKNRK VLQTLSGNFN RRSRSVEVEV KRQDNLGVVH
     KDRKKDRSFN SLLQAKDQQL EQLVQRLATL HRYNDQFAKE NDQLRKDSGQ LERRLTEAEQ
     QVANCSRCQQ LGQRLDTVLA QNRTLAGDVD MLKTLVFRLN VQIESYQDQR RLGEGAPTCG
     GSTKVSSSSA PYPPLPTHTL GPLLQAYDES LRDKDALLAQ YNTEFEHFTG ELKRALEENT
     KLLQSQEQLR RDLGGWREER VCLQAQLGVC RSKAEAQTRK TDLAKEKLVE VMHCYEQRMQ
     TLILDMDHLQ AAYARTKSEL AALKSASSAA PAAVAPPVPA ESEALHQCKA LLEQLRQEHA
     RERTCLQEQL QATTARAASL VRSTEKAKHS RDRLKARLRM ALQWAQKLEA GQAEVRDTYE
     AVRRLEVLVQ HKESQLRGLH ARNAEEMDKL RHKLQQKEET ICALLRGKME RRPAVD
 
 
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