ACPM_DROME
ID ACPM_DROME Reviewed; 152 AA.
AC Q94519; Q94520; Q9W0G8; Q9W0G9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Acyl carrier protein, mitochondrial;
DE Short=ACP;
DE AltName: Full=NADH-ubiquinone oxidoreductase 9.6 kDa subunit;
DE AltName: Full=NADH-ubiquinone oxidoreductase acyl-carrier subunit;
DE Flags: Precursor;
GN Name=ND-ACP {ECO:0000312|FlyBase:FBgn0011361};
GN Synonyms=mtACP, mtacp1 {ECO:0000312|FlyBase:FBgn0011361}, ND-AcC;
GN ORFNames=CG9160 {ECO:0000312|FlyBase:FBgn0011361};
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].
RC TISSUE=Ovary;
RX PubMed=10071211; DOI=10.1007/s004380050942;
RA Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R.,
RA Barsanti P.;
RT "Identification of nuclear genes encoding mitochondrial proteins: isolation
RT of a collection of D. melanogaster cDNAs homologous to sequences in the
RT Human Gene Index database.";
RL Mol. Gen. Genet. 261:64-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Ragone G., Caizzi R., Caggese C.;
RT "Two forms of cDNA and the sequence of Drosophila melanogaster gene for
RT acyl-carrier subunit of NADH:ubiquinone oxidoreductase show evidence of
RT alternatively spliced forms.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis. Accessory and non-catalytic subunit of the mitochondrial
CC membrane respiratory chain NADH dehydrogenase (Complex I), which
CC functions in the transfer of electrons from NADH to the respiratory
CC chain (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Complex I is composed of about 45 different subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=A;
CC IsoId=Q94519-1; Sequence=Displayed;
CC Name=1; Synonyms=B;
CC IsoId=Q94519-2; Sequence=VSP_000148;
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000305}.
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DR EMBL; AJ000879; CAA04368.1; -; Genomic_DNA.
DR EMBL; AJ000879; CAA04369.1; -; Genomic_DNA.
DR EMBL; Y09068; CAA70289.1; -; mRNA.
DR EMBL; Y09069; CAA70290.1; -; mRNA.
DR EMBL; AE014296; AAF47479.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47480.1; -; Genomic_DNA.
DR EMBL; AY089404; AAL90142.1; -; mRNA.
DR RefSeq; NP_477002.1; NM_057654.4. [Q94519-2]
DR RefSeq; NP_477003.1; NM_057655.4.
DR AlphaFoldDB; Q94519; -.
DR SMR; Q94519; -.
DR BioGRID; 63697; 16.
DR IntAct; Q94519; 8.
DR SwissPalm; Q94519; -.
DR DNASU; 38154; -.
DR EnsemblMetazoa; FBtr0072677; FBpp0072570; FBgn0011361. [Q94519-2]
DR GeneID; 38154; -.
DR KEGG; dme:Dmel_CG9160; -.
DR CTD; 38154; -.
DR FlyBase; FBgn0011361; ND-ACP.
DR VEuPathDB; VectorBase:FBgn0011361; -.
DR GeneTree; ENSGT00390000002127; -.
DR HOGENOM; CLU_108696_0_1_1; -.
DR InParanoid; Q94519; -.
DR PhylomeDB; Q94519; -.
DR Reactome; R-DME-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-DME-611105; Respiratory electron transport.
DR Reactome; R-DME-6799198; Complex I biogenesis.
DR Reactome; R-DME-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SignaLink; Q94519; -.
DR BioGRID-ORCS; 38154; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 38154; -.
DR PRO; PR:Q94519; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0011361; Expressed in mouthpart and 29 other tissues.
DR ExpressionAtlas; Q94519; baseline and differential.
DR Genevisible; Q94519; DM.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; ISA:FlyBase.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:FlyBase.
DR GO; GO:0009249; P:protein lipoylation; ISS:FlyBase.
DR Gene3D; 1.10.1200.10; -; 1.
DR HAMAP; MF_01217; Acyl_carrier; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR003231; Acyl_carrier.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR20863; PTHR20863; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Electron transport; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Respiratory chain;
KW Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..152
FT /note="Acyl carrier protein, mitochondrial"
FT /id="PRO_0000000563"
FT DOMAIN 73..148
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 108
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT VAR_SEQ 51..92
FT /note="ECRGRWQTQLVRKYSAKPPLSLKLINERVLLVLKLYDKIDPS -> KFGVRS
FT YSAKSTIEDIKFRVLKVVSAYDKVTAE (in isoform 1)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.5"
FT /id="VSP_000148"
FT CONFLICT 63
FT /note="K -> R (in Ref. 3; AAF47480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 17235 MW; 79C79A8BE1512A54 CRC64;
MSFTQIARSC SRLAATLAPR RVASGILIQS QASRMMHRIA VPSMTSQLSQ ECRGRWQTQL
VRKYSAKPPL SLKLINERVL LVLKLYDKID PSKLNVESHF INDLGLDSLD HVEVIMAMED
EFGFEIPDSD AEKLLKPADI IKYVADKEDV YE
