ID   ACPM_PONPY              Reviewed;         156 AA.
AC   Q0MQC1;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Acyl carrier protein, mitochondrial;
DE            Short=ACP;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 9.6 kDa subunit;
DE   Flags: Precursor;
GN   Name=NDUFAB1;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16828987; DOI=10.1016/j.gene.2006.03.015;
RA   Mishmar D., Ruiz-Pesini E., Mondragon-Palomino M., Procaccio V., Gaut B.,
RA   Wallace D.C.;
RT   "Adaptive selection of mitochondrial complex I subunits during primate
RT   radiation.";
RL   Gene 378:11-18(2006).
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
CC       as 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; DQ885713; ABH12222.1; -; mRNA.
DR   AlphaFoldDB; Q0MQC1; -.
DR   SMR; Q0MQC1; -.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS: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   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   2: Evidence at transcript level;
KW   Acetylation; Electron transport; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW   Phosphopantetheine; Phosphoprotein; Respiratory chain; Transit peptide;
KW   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_0000251163"
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"
SQ   SEQUENCE   156 AA;  17413 MW;  64A38AE2B71C3AB3 CRC64;
     MASRVLSAYV SRLPAAFAPL PRVRMLAVAR PLSTALCSAG TQTRLGPLQP ALVLAQVPGR
     VTQLCRQYSD MPPLTLEGIQ DRVLYVLKLY DKIDPEKLSV NSHFMKDLGL DSLDQVEIIM
     AMEDEFGFEI PDIDAEKLMC PQEIVDYIAD KKDVYE