ACPM_HUMAN
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 03-AUG-2022, entry version 201.
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 INTERACTION WITH ALPHA-1-MICROGLOBULIN.
RX PubMed=23157686; DOI=10.1089/ars.2012.4658;
RA Olsson M.G., Rosenloef L.W., Kotarsky H., Olofsson T., Leanderson T.,
RA Moergelin M., Fellman V., Aakerstroem B.;
RT "The radical-binding lipocalin A1M binds to a Complex I subunit and
RT protects mitochondrial structure and function.";
RL Antioxid. Redox Signal. 18:2017-2028(2013).
RN [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16] {ECO:0007744|PDB:5OOL, ECO:0007744|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). Interacts with alpha-1-
CC microglobulin chain; this interaction is required for the maintenance
CC of mitochondrial redox homeostasis. {ECO:0000269|PubMed:12611891,
CC ECO:0000269|PubMed:23157686, ECO:0000269|PubMed:27499296,
CC ECO:0000269|PubMed:28892042, 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=4; 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 PDB; 7A5H; EM; 3.30 A; w=1-156.
DR PDB; 7A5J; EM; 3.10 A; w=1-156.
DR PDB; 7O9K; EM; 3.10 A; w=1-156.
DR PDB; 7O9M; EM; 2.50 A; w=1-156.
DR PDB; 7ODR; EM; 2.90 A; w=1-156.
DR PDB; 7ODS; EM; 3.10 A; w=1-156.
DR PDB; 7ODT; EM; 3.10 A; w=1-156.
DR PDB; 7OF0; EM; 2.20 A; w=1-156.
DR PDB; 7OF2; EM; 2.70 A; w=1-156.
DR PDB; 7OF3; EM; 2.70 A; w=1-156.
DR PDB; 7OF5; EM; 2.90 A; w=1-156.
DR PDB; 7OF7; EM; 2.50 A; w=1-156.
DR PDB; 7OI6; EM; 5.70 A; w=1-156.
DR PDB; 7OI7; EM; 3.50 A; w=1-156.
DR PDB; 7OI8; EM; 3.50 A; w=1-156.
DR PDB; 7OI9; EM; 3.30 A; w=1-156.
DR PDB; 7OIC; EM; 3.10 A; w=1-156.
DR PDB; 7OID; EM; 3.70 A; w=1-156.
DR PDB; 7OIE; EM; 3.50 A; w=1-156.
DR PDB; 7PD3; EM; 3.40 A; w=1-156.
DR PDB; 7QH6; EM; 3.08 A; w=1-156.
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 PDBsum; 7A5H; -.
DR PDBsum; 7A5J; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7ODR; -.
DR PDBsum; 7ODS; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF0; -.
DR PDBsum; 7OF2; -.
DR PDBsum; 7OF3; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF7; -.
DR PDBsum; 7OI6; -.
DR PDBsum; 7OI7; -.
DR PDBsum; 7OI8; -.
DR PDBsum; 7OI9; -.
DR PDBsum; 7OIC; -.
DR PDBsum; 7OID; -.
DR PDBsum; 7OIE; -.
DR PDBsum; 7PD3; -.
DR PDBsum; 7QH6; -.
DR AlphaFoldDB; O14561; -.
DR SMR; O14561; -.
DR BioGRID; 110786; 150.
DR ComplexPortal; CPX-5641; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; O14561; -.
DR IntAct; O14561; 149.
DR MINT; O14561; -.
DR STRING; 9606.ENSP00000458770; -.
DR BindingDB; O14561; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; O14561; -.
DR GlyGen; O14561; 1 site, 1 O-linked glycan (1 site).
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; 109 antibodies from 25 providers.
DR DNASU; 4706; -.
DR Ensembl; ENST00000007516.8; ENSP00000007516.2; ENSG00000004779.10.
DR Ensembl; ENST00000570319.5; ENSP00000458770.1; ENSG00000004779.10.
DR GeneID; 4706; -.
DR KEGG; hsa:4706; -.
DR MANE-Select; ENST00000007516.8; ENSP00000007516.2; NM_005003.3; NP_004994.1.
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).
DR MIM; 603836; gene.
DR neXtProt; NX_O14561; -.
DR OpenTargets; ENSG00000004779; -.
DR PharmGKB; PA31500; -.
DR VEuPathDB; HostDB:ENSG00000004779; -.
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-MON; -.
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 SignaLink; O14561; -.
DR SIGNOR; O14561; -.
DR BioGRID-ORCS; 4706; 584 hits in 1100 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 heart right ventricle and 209 other tissues.
DR ExpressionAtlas; O14561; baseline and differential.
DR Genevisible; O14561; HS.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IC:ComplexPortal.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
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:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0006633; P:fatty acid biosynthetic process; NAS:UniProtKB.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0009249; P:protein lipoylation; IMP:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
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 PANTHER; PTHR20863; PTHR20863; 1.
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:0000269|PubMed:19892738,
FT ECO:0007744|PubMed:25944712"
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:0007829|PDB:6ODD"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6ODD"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5OOM"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:6ODD"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:6ODD"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:6ODD"
FT HELIX 141..151
FT /evidence="ECO:0007829|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
