ID   ACPM_HUMAN              Reviewed;         156 AA.
AC   O14561; B2R4M1; Q9UNV1;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 3.
DT   10-FEB-2021, entry version 195.
DE   RecName: Full=Acyl carrier protein, mitochondrial;
DE            Short=ACP;
DE   AltName: Full=CI-SDAP;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 9.6 kDa subunit;
DE   Flags: Precursor;
GN   Name=NDUFAB1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9878551; DOI=10.1006/bbrc.1998.9786;
RA   Loeffen J.L.C.M., Triepels R.H., van den Heuvel L.P., Schuelke M.,
RA   Buskens C.A.F., Smeets R.J.P., Trijbels J.M.F., Smeitink J.A.M.;
RT   "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase:
RT   human complex I cDNA characterization completed.";
RL   Biochem. Biophys. Res. Commun. 253:415-422(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA   Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA   Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA   Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA   Adams M.D.;
RT   "Genome duplications and other features in 12 Mb of DNA sequence from human
RT   chromosome 16p and 16q.";
RL   Genomics 60:295-308(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 69-83.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA   Xu G., Shin S.B., Jaffrey S.R.;
RT   "Global profiling of protease cleavage sites by chemoselective labeling of
RT   protein N-termini.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN   [7]
RP   IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, SUBCELLULAR
RP   LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12611891; DOI=10.1074/jbc.c300064200;
RA   Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F.,
RA   Ghosh S.S., Capaldi R.A.;
RT   "The subunit composition of the human NADH dehydrogenase obtained by rapid
RT   one-step immunopurification.";
RL   J. Biol. Chem. 278:13619-13622(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [10]
RP   CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER TYR-68, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [11]
RP   INTERACTION WITH ETFRF1.
RX   PubMed=27499296; DOI=10.1016/j.molcel.2016.06.033;
RA   Floyd B.J., Wilkerson E.M., Veling M.T., Minogue C.E., Xia C., Beebe E.T.,
RA   Wrobel R.L., Cho H., Kremer L.S., Alston C.L., Gromek K.A., Dolan B.K.,
RA   Ulbrich A., Stefely J.A., Bohl S.L., Werner K.M., Jochem A.,
RA   Westphall M.S., Rensvold J.W., Taylor R.W., Prokisch H., Kim J.J.,
RA   Coon J.J., Pagliarini D.J.;
RT   "Mitochondrial protein interaction mapping identifies regulators of
RT   respiratory chain function.";
RL   Mol. Cell 63:621-632(2016).
RN   [12]
RP   FUNCTION, AND IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
RX   PubMed=27626371; DOI=10.1038/nature19754;
RA   Stroud D.A., Surgenor E.E., Formosa L.E., Reljic B., Frazier A.E.,
RA   Dibley M.G., Osellame L.D., Stait T., Beilharz T.H., Thorburn D.R.,
RA   Salim A., Ryan M.T.;
RT   "Accessory subunits are integral for assembly and function of human
RT   mitochondrial complex I.";
RL   Nature 538:123-126(2016).
RN   [13]
RP   INTERACTION WITH MIEF1 UPSTREAM OPEN READING FRAME PROTEIN.
RX   PubMed=30215512; DOI=10.1021/acs.biochem.8b00726;
RA   Rathore A., Chu Q., Tan D., Martinez T.F., Donaldson C.J., Diedrich J.K.,
RA   Yates J.R. III, Saghatelian A.;
RT   "MIEF1 microprotein regulates mitochondrial translation.";
RL   Biochemistry 57:5564-5575(2018).
RN   [14]
RP   STRUCTURE BY NMR OF 69-156.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RSGI RUH-059, an ACP domain of acyl carrier protein,
RT   mitochondrial from human.";
RL   Submitted (OCT-2006) to the PDB data bank.
RN   [15] {ECO:0000244|PDB:5OOL, ECO:0000244|PDB:5OOM}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), IDENTIFICATION BY MASS
RP   SPECTROMETRY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=28892042; DOI=10.1038/nsmb.3464;
RA   Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J.,
RA   Amunts A., Ramakrishnan V.;
RT   "Structures of the human mitochondrial ribosome in native states of
RT   assembly.";
RL   Nat. Struct. Mol. Biol. 24:866-869(2017).
CC   -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC       biosynthesis (By similarity). Accessory and non-catalytic subunit of
CC       the mitochondrial membrane respiratory chain NADH dehydrogenase
CC       (Complex I), which functions in the transfer of electrons from NADH to
CC       the respiratory chain (PubMed:27626371). {ECO:0000250|UniProtKB:P52505,
CC       ECO:0000269|PubMed:27626371}.
CC   -!- SUBUNIT: Mammalian complex I is composed of 45 different subunits
CC       (PubMed:12611891). Interacts with ETFRF1 (PubMed:27499296). Identified
CC       in a complex composed of MALSU1, MIEF1 upstream open reading frame
CC       protein and NDUFAB1; within the trimeric complex, MIEF1 upstream open
CC       reading frame protein functions as a bridging scaffold that interacts
CC       with MALSU1 on one side, and with NDUFAB1 on the other side. The
CC       complex interacts with the mitochondrial large ribosomal subunit
CC       (PubMed:28892042, PubMed:30215512). {ECO:0000269|PubMed:12611891,
CC       ECO:0000269|PubMed:27499296, ECO:0000269|PubMed:28892042,
CC       ECO:0000269|PubMed:30215512}.
CC   -!- INTERACTION:
CC       O14561; Q08043: ACTN3; NbExp=3; IntAct=EBI-1246261, EBI-2880652;
CC       O14561; Q96PG8: BBC3; NbExp=3; IntAct=EBI-1246261, EBI-17289784;
CC       O14561; Q5H9J7: BEX5; NbExp=3; IntAct=EBI-1246261, EBI-10243741;
CC       O14561; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-1246261, EBI-1104933;
CC       O14561; P26441: CNTF; NbExp=3; IntAct=EBI-1246261, EBI-1050897;
CC       O14561; Q9BSK4: FEM1A; NbExp=3; IntAct=EBI-1246261, EBI-2515349;
CC       O14561; Q13643: FHL3; NbExp=5; IntAct=EBI-1246261, EBI-741101;
CC       O14561; Q53EP0-3: FNDC3B; NbExp=5; IntAct=EBI-1246261, EBI-10242151;
CC       O14561; Q9BQA5: HINFP; NbExp=3; IntAct=EBI-1246261, EBI-749065;
CC       O14561; Q7L273: KCTD9; NbExp=3; IntAct=EBI-1246261, EBI-4397613;
CC       O14561; P25791-3: LMO2; NbExp=3; IntAct=EBI-1246261, EBI-11959475;
CC       O14561; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1246261, EBI-739832;
CC       O14561; Q6PF18: MORN3; NbExp=3; IntAct=EBI-1246261, EBI-9675802;
CC       O14561; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-1246261, EBI-12025760;
CC       O14561; Q16656-4: NRF1; NbExp=3; IntAct=EBI-1246261, EBI-11742836;
CC       O14561; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1246261, EBI-741158;
CC       O14561; O43482: OIP5; NbExp=3; IntAct=EBI-1246261, EBI-536879;
CC       O14561; Q969H6: POP5; NbExp=3; IntAct=EBI-1246261, EBI-366525;
CC       O14561; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-1246261, EBI-710402;
CC       O14561; P17980: PSMC3; NbExp=6; IntAct=EBI-1246261, EBI-359720;
CC       O14561; Q9GZT3: SLIRP; NbExp=3; IntAct=EBI-1246261, EBI-1050793;
CC       O14561; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-1246261, EBI-741515;
CC       O14561; O43711: TLX3; NbExp=5; IntAct=EBI-1246261, EBI-3939165;
CC       O14561; Q96NM4-3: TOX2; NbExp=3; IntAct=EBI-1246261, EBI-12815137;
CC       O14561; Q08AM6: VAC14; NbExp=3; IntAct=EBI-1246261, EBI-2107455;
CC       O14561; P17023: ZNF19; NbExp=3; IntAct=EBI-1246261, EBI-12884200;
CC       O14561; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-1246261, EBI-11741890;
CC       O14561; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-1246261, EBI-18036029;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12611891,
CC       ECO:0000269|PubMed:28892042}.
CC   -!- MISCELLANEOUS: In contrast to other accessory subunits of complex I,
CC       NDUFAB1 is the only subunit that is essential for cell viability in
CC       HEK293T cells. Since knockout cells lack assembled complex I and die in
CC       galactose media, this suggests that the essential role of NDUFAB1 is
CC       independent of complex I. {ECO:0000269|PubMed:27626371}.
CC   -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC05814.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF087660; AAD23566.1; -; mRNA.
DR   EMBL; AK311877; BAG34818.1; -; mRNA.
DR   EMBL; AC002400; AAC05814.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CH471145; EAW55816.1; -; Genomic_DNA.
DR   EMBL; BC058920; AAH58920.1; -; mRNA.
DR   CCDS; CCDS10614.1; -.
DR   PIR; T00741; T00741.
DR   RefSeq; NP_004994.1; NM_005003.2.
DR   PDB; 2DNW; NMR; -; A=71-156.
DR   PDB; 5OOL; EM; 3.06 A; w=1-156.
DR   PDB; 5OOM; EM; 3.03 A; w=1-156.
DR   PDB; 5XTB; EM; 3.40 A; G=72-156.
DR   PDB; 5XTC; EM; 3.70 A; X=72-156.
DR   PDB; 5XTD; EM; 3.70 A; G/X=72-156.
DR   PDB; 5XTH; EM; 3.90 A; G/X=72-156.
DR   PDB; 5XTI; EM; 17.40 A; BG/BX/G/X=72-156.
DR   PDB; 6ODD; X-ray; 2.00 A; A=72-156.
DR   PDBsum; 2DNW; -.
DR   PDBsum; 5OOL; -.
DR   PDBsum; 5OOM; -.
DR   PDBsum; 5XTB; -.
DR   PDBsum; 5XTC; -.
DR   PDBsum; 5XTD; -.
DR   PDBsum; 5XTH; -.
DR   PDBsum; 5XTI; -.
DR   PDBsum; 6ODD; -.
DR   SMR; O14561; -.
DR   BioGRID; 110786; 106.
DR   ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR   CORUM; O14561; -.
DR   IntAct; O14561; 68.
DR   MINT; O14561; -.
DR   STRING; 9606.ENSP00000458770; -.
DR   BindingDB; O14561; -.
DR   ChEMBL; CHEMBL2363065; -.
DR   DrugBank; DB00157; NADH.
DR   DrugCentral; O14561; -.
DR   iPTMnet; O14561; -.
DR   PhosphoSitePlus; O14561; -.
DR   SwissPalm; O14561; -.
DR   BioMuta; NDUFAB1; -.
DR   EPD; O14561; -.
DR   jPOST; O14561; -.
DR   MassIVE; O14561; -.
DR   MaxQB; O14561; -.
DR   PaxDb; O14561; -.
DR   PeptideAtlas; O14561; -.
DR   PRIDE; O14561; -.
DR   ProteomicsDB; 48088; -.
DR   TopDownProteomics; O14561; -.
DR   Antibodypedia; 25997; 103 antibodies.
DR   Ensembl; ENST00000007516; ENSP00000007516; ENSG00000004779.
DR   Ensembl; ENST00000570319; ENSP00000458770; ENSG00000004779.
DR   GeneID; 4706; -.
DR   KEGG; hsa:4706; -.
DR   UCSC; uc002dlw.4; human.
DR   CTD; 4706; -.
DR   DisGeNET; 4706; -.
DR   GeneCards; NDUFAB1; -.
DR   HGNC; HGNC:7694; NDUFAB1.
DR   HPA; ENSG00000004779; Tissue enhanced (heart muscle, skeletal muscle).
DR   MIM; 603836; gene.
DR   neXtProt; NX_O14561; -.
DR   OpenTargets; ENSG00000004779; -.
DR   PharmGKB; PA31500; -.
DR   VEuPathDB; HostDB:ENSG00000004779.9; -.
DR   eggNOG; KOG1748; Eukaryota.
DR   GeneTree; ENSGT00390000002127; -.
DR   HOGENOM; CLU_108696_0_1_1; -.
DR   InParanoid; O14561; -.
DR   OMA; QYCEAPP; -.
DR   OrthoDB; 1473625at2759; -.
DR   PhylomeDB; O14561; -.
DR   TreeFam; TF314361; -.
DR   BioCyc; MetaCyc:ENSG00000004779-MONOMER; -.
DR   PathwayCommons; O14561; -.
DR   Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   Reactome; R-HSA-6799198; Complex I biogenesis.
DR   Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   BioGRID-ORCS; 4706; 558 hits in 894 CRISPR screens.
DR   ChiTaRS; NDUFAB1; human.
DR   EvolutionaryTrace; O14561; -.
DR   GenomeRNAi; 4706; -.
DR   Pharos; O14561; Tclin.
DR   PRO; PR:O14561; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; O14561; protein.
DR   Bgee; ENSG00000004779; Expressed in myocardium and 250 other tissues.
DR   ExpressionAtlas; O14561; baseline and differential.
DR   Genevisible; O14561; HS.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR   GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR   GO; GO:0005504; F:fatty acid binding; ISS:UniProtKB.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; NAS:UniProtKB.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; TAS:Reactome.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR   GO; GO:0009249; P:protein lipoylation; IMP:UniProtKB.
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   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   TIGRFAMs; TIGR00517; acyl_carrier; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Mitochondrion; Phosphopantetheine; Phosphoprotein;
KW   Reference proteome; Respiratory chain; Transit peptide; Transport.
FT   TRANSIT         1..68
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000244|PubMed:25944712,
FT                   ECO:0000269|PubMed:19892738"
FT   CHAIN           69..156
FT                   /note="Acyl carrier protein, mitochondrial"
FT                   /id="PRO_0000000561"
FT   DOMAIN          77..152
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         88
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CR21"
FT   MOD_RES         112
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   CONFLICT        132
FT                   /note="D -> Y (in Ref. 5; AAH58920)"
FT                   /evidence="ECO:0000305"
FT   HELIX           76..88
FT                   /evidence="ECO:0000244|PDB:6ODD"
FT   STRAND          91..93
FT                   /evidence="ECO:0000244|PDB:5OOM"
FT   HELIX           95..97
FT                   /evidence="ECO:0000244|PDB:6ODD"
FT   STRAND          99..101
FT                   /evidence="ECO:0000244|PDB:5OOM"
FT   TURN            104..108
FT                   /evidence="ECO:0000244|PDB:6ODD"
FT   HELIX           112..126
FT                   /evidence="ECO:0000244|PDB:6ODD"
FT   HELIX           132..135
FT                   /evidence="ECO:0000244|PDB:6ODD"
FT   HELIX           141..151
FT                   /evidence="ECO:0000244|PDB:6ODD"
SQ   SEQUENCE   156 AA;  17417 MW;  0FCE3C3EC6D97AE2 CRC64;
     MASRVLSAYV SRLPAAFAPL PRVRMLAVAR PLSTALCSAG TQTRLGTLQP ALVLAQVPGR
     VTQLCRQYSD MPPLTLEGIQ DRVLYVLKLY DKIDPEKLSV NSHFMKDLGL DSLDQVEIIM
     AMEDEFGFEI PDIDAEKLMC PQEIVDYIAD KKDVYE
//