ACPM_MOUSE
ID ACPM_MOUSE Reviewed; 156 AA.
AC Q9CR21; Q9D726; Q9D7V5;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cecum, Embryonic stem cell, Kidney, Stomach, Thymus, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP PROTEIN SEQUENCE OF 89-97 AND 138-151, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-88, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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 (By similarity). {ECO:0000250|UniProtKB:O14561,
CC ECO:0000250|UniProtKB:P52505}.
CC -!- SUBUNIT: Mammalian complex I is composed of 45 different subunits.
CC Interacts with ETFRF1. Identified in a complex composed of MALSU1,
CC MIEF1 upstream open reading frame protein and NDUFAB1; within the
CC trimeric complex MIEF1 upstream open reading frame protein functions as
CC a bridging scaffold that interacts with MALSU1 on one side, and with
CC NDUFAB1 on the other side. The complex interacts with the mitochondrial
CC large ribosomal subunit. Interacts with alpha-1-microglobulin chain;
CC this interaction is required for the maintenance of mitochondrial redox
CC homeostasis. {ECO:0000250|UniProtKB:O14561}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O14561}.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000305}.
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DR EMBL; AK008788; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK009698; BAB26446.1; -; mRNA.
DR EMBL; AK010307; BAB26840.1; -; mRNA.
DR EMBL; AK011302; BAB27528.1; -; mRNA.
DR EMBL; AK018688; BAB31346.1; -; mRNA.
DR EMBL; AK018717; BAB31363.1; -; mRNA.
DR EMBL; AK089103; BAC40751.1; -; mRNA.
DR EMBL; BC060951; AAH60951.1; -; mRNA.
DR CCDS; CCDS21809.1; -.
DR RefSeq; NP_082453.2; NM_028177.3.
DR RefSeq; XP_006508263.1; XM_006508200.3.
DR PDB; 6G2J; EM; 3.30 A; T/U=1-156.
DR PDB; 6G72; EM; 3.90 A; T/U=1-156.
DR PDB; 6ZR2; EM; 3.10 A; T/U=1-156.
DR PDB; 6ZTQ; EM; 3.00 A; T/U=1-156.
DR PDB; 7AK5; EM; 3.17 A; T/U=1-156.
DR PDB; 7AK6; EM; 3.82 A; T/U=1-156.
DR PDB; 7B93; EM; 3.04 A; T/U=1-156.
DR PDB; 7PSA; EM; 3.40 A; T/U=1-156.
DR PDBsum; 6G2J; -.
DR PDBsum; 6G72; -.
DR PDBsum; 6ZR2; -.
DR PDBsum; 6ZTQ; -.
DR PDBsum; 7AK5; -.
DR PDBsum; 7AK6; -.
DR PDBsum; 7B93; -.
DR PDBsum; 7PSA; -.
DR AlphaFoldDB; Q9CR21; -.
DR SMR; Q9CR21; -.
DR BioGRID; 213983; 48.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR ComplexPortal; CPX-5823; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR CORUM; Q9CR21; -.
DR IntAct; Q9CR21; 43.
DR STRING; 10090.ENSMUSP00000033157; -.
DR iPTMnet; Q9CR21; -.
DR PhosphoSitePlus; Q9CR21; -.
DR SwissPalm; Q9CR21; -.
DR EPD; Q9CR21; -.
DR jPOST; Q9CR21; -.
DR MaxQB; Q9CR21; -.
DR PaxDb; Q9CR21; -.
DR PeptideAtlas; Q9CR21; -.
DR PRIDE; Q9CR21; -.
DR ProteomicsDB; 285749; -.
DR TopDownProteomics; Q9CR21; -.
DR Antibodypedia; 25997; 109 antibodies from 25 providers.
DR DNASU; 70316; -.
DR Ensembl; ENSMUST00000033157; ENSMUSP00000033157; ENSMUSG00000030869.
DR Ensembl; ENSMUST00000123296; ENSMUSP00000116177; ENSMUSG00000030869.
DR GeneID; 70316; -.
DR KEGG; mmu:70316; -.
DR UCSC; uc009joh.1; mouse.
DR CTD; 4706; -.
DR MGI; MGI:1917566; Ndufab1.
DR VEuPathDB; HostDB:ENSMUSG00000030869; -.
DR eggNOG; KOG1748; Eukaryota.
DR GeneTree; ENSGT00390000002127; -.
DR InParanoid; Q9CR21; -.
DR OMA; QYCEAPP; -.
DR OrthoDB; 1473625at2759; -.
DR PhylomeDB; Q9CR21; -.
DR TreeFam; TF314361; -.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR BioGRID-ORCS; 70316; 27 hits in 74 CRISPR screens.
DR ChiTaRS; Ndufab1; mouse.
DR PRO; PR:Q9CR21; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CR21; protein.
DR Bgee; ENSMUSG00000030869; Expressed in right kidney and 250 other tissues.
DR ExpressionAtlas; Q9CR21; baseline and differential.
DR Genevisible; Q9CR21; MM.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IC:ComplexPortal.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISO:MGI.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR GO; GO:0009249; P:protein lipoylation; ISO:MGI.
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:0000250"
FT CHAIN 69..156
FT /note="Acyl carrier protein, mitochondrial"
FT /id="PRO_0000000562"
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:0007744|PubMed:23576753"
FT MOD_RES 112
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 138
FT /note="L -> F (in Ref. 1; BAB26446)"
FT /evidence="ECO:0000305"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:7B93"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 156 AA; 17370 MW; 2FC53044FE0902C5 CRC64;
MASRVLCACV RRLPAAFAPL PRLPTLALAR PLSTTLCPEG IRRRPGALQS ALALAQVPGT
VTHLCRQYSD APPLTLDGIK DRVLYVLKLY DKIDPEKLSV NSHFMKDLGL DSLDQVEIIM
AMEDEFGFEI PDIDAEKLMC PQEIVDYIAD KKDVYE
