NDUF6_DROME
ID NDUF6_DROME Reviewed; 334 AA.
AC Q9VYS5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=NADH dehydrogenase (ubiquinone) complex I, assembly factor 6 homolog;
DE Flags: Precursor;
GN Name=sicily; ORFNames=CG15738;
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=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 [4]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH HSP83 AND ND-42, INTERACTION
RP WITH ND-30, TISSUE SPECIFICITY, AND MUTAGENESIS OF 1-MET--ARG-11.
RX PubMed=23509070; DOI=10.1083/jcb.201208033;
RA Zhang K., Li Z., Jaiswal M., Bayat V., Xiong B., Sandoval H., Charng W.L.,
RA David G., Haueter C., Yamamoto S., Graham B.H., Bellen H.J.;
RT "The C8ORF38 homologue Sicily is a cytosolic chaperone for a mitochondrial
RT complex I subunit.";
RL J. Cell Biol. 200:807-820(2013).
CC -!- FUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone
CC oxidoreductase complex (Complex I) at early stages (PubMed:23509070).
CC Interacts with cytosolic Hsp90 to chaperone the Complex I subunit ND-42
CC in the cytoplasm (PubMed:23509070). {ECO:0000269|PubMed:23509070}.
CC -!- SUBUNIT: Forms a complex including sicily, ND-42 and Hsp83; the complex
CC is necessary to chaperone ND-42 in the cytoplasm before mitochondrial
CC import; the interaction between sicily and ND-42 is direct and occurs
CC preferably between the unprocessed forms in the cytoplasm; the
CC interaction with Hsp83 is direct (PubMed:23509070). Interacts with ND-
CC 30; interaction is stronger between the unprocessed forms in the
CC cytoplasm (PubMed:23509070). {ECO:0000269|PubMed:23509070}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:23509070}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:23509070}.
CC -!- TISSUE SPECIFICITY: Expressed in the ventral nerve cord, larval brain,
CC motor neuron axons, imaginal disks, and muscles (at protein level).
CC {ECO:0000269|PubMed:23509070}.
CC -!- SIMILARITY: Belongs to the NDUFAF6 family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48113.1; -; Genomic_DNA.
DR EMBL; AY119646; AAM50300.1; -; mRNA.
DR RefSeq; NP_001285142.1; NM_001298213.1.
DR RefSeq; NP_572765.1; NM_132537.2.
DR AlphaFoldDB; Q9VYS5; -.
DR SMR; Q9VYS5; -.
DR BioGRID; 58556; 9.
DR STRING; 7227.FBpp0073416; -.
DR PaxDb; Q9VYS5; -.
DR PRIDE; Q9VYS5; -.
DR DNASU; 32151; -.
DR EnsemblMetazoa; FBtr0073572; FBpp0073416; FBgn0030352.
DR EnsemblMetazoa; FBtr0346165; FBpp0311993; FBgn0030352.
DR GeneID; 32151; -.
DR KEGG; dme:Dmel_CG15738; -.
DR UCSC; CG15738-RA; d. melanogaster.
DR CTD; 32151; -.
DR FlyBase; FBgn0030352; sicily.
DR VEuPathDB; VectorBase:FBgn0030352; -.
DR eggNOG; KOG4411; Eukaryota.
DR HOGENOM; CLU_037269_6_0_1; -.
DR InParanoid; Q9VYS5; -.
DR OMA; RKFWLAW; -.
DR OrthoDB; 616989at2759; -.
DR PhylomeDB; Q9VYS5; -.
DR Reactome; R-DME-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 32151; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32151; -.
DR PRO; PR:Q9VYS5; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030352; Expressed in Malpighian tubule and 11 other tissues.
DR ExpressionAtlas; Q9VYS5; baseline and differential.
DR Genevisible; Q9VYS5; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR002060; Squ/phyt_synthse.
DR Pfam; PF00494; SQS_PSY; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..11
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 12..334
FT /note="NADH dehydrogenase (ubiquinone) complex I, assembly
FT factor 6 homolog"
FT /id="PRO_0000355147"
FT MUTAGEN 1..11
FT /note="Missing: Mostly localized to cytoplasm. Does not
FT affect interaction with and protein level stabilization of
FT ND-42."
FT /evidence="ECO:0000269|PubMed:23509070"
SQ SEQUENCE 334 AA; 38175 MW; 1C45E2A8BC0A15A0 CRC64;
MRRLVRNWNC RLLFNAKSGQ EIVSHAGIHQ EAKTNAIPRE KKVIEADKNG YGAKHCMSLV
EKYDYENYLC TLLLPRELRR AAFALRAFNV EVSRSVSGHQ IEPQIAKMRL KFWHDSIDKC
FEPDSQRSYV EDQPVLRELK HTVGSRKLNK VYLRRLVTAR ERPPTHAFES IRELEEYTEQ
TFSSLLLLLL EVGGVRDLNA DHAASHLGKA QGIATLLRSI PLAGRQQAPC IPLEVLVLHG
VSQERIIRSK SDDKGVEDCI FDVASAANTH LKLARQLHDK VPPQVRKIFL SAVATDAYLE
RLRRANFLLT HKSCVGRDTL LPARLFWKSL LNRF
