ACPM_BOVIN
ID ACPM_BOVIN Reviewed; 156 AA.
AC P52505; Q3T150;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-156, PROTEIN SEQUENCE OF 69-90,
RP SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND FUNCTION.
RC TISSUE=Heart;
RX PubMed=1907568; DOI=10.1016/0014-5793(91)80955-3;
RA Runswick M.J., Fearnley I.M., Skehel J.M., Walker J.E.;
RT "Presence of an acyl carrier protein in NADH:ubiquinone oxidoreductase from
RT bovine heart mitochondria.";
RL FEBS Lett. 286:121-124(1991).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, IDENTIFICATION IN COMPLEX I,
RP AND SUBCELLULAR LOCATION.
RX PubMed=10852722; DOI=10.1021/bi000335t;
RA Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E.;
RT "Resolution of the membrane domain of bovine complex I into subcomplexes:
RT implications for the structural organization of the enzyme.";
RL Biochemistry 39:7229-7235(2000).
RN [4]
RP FUNCTION, SUBUNIT, IDENTIFICATION IN COMPLEX I, AND SUBCELLULAR LOCATION.
RX PubMed=18721790; DOI=10.1016/j.ab.2008.07.029;
RA Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A.,
RA Robinson N.C.;
RT "Subunit analysis of bovine heart complex I by reversed-phase high-
RT performance liquid chromatography, electrospray ionization-tandem mass
RT spectrometry, and matrix-assisted laser desorption/ionization-time-of-
RT flight mass spectrometry.";
RL Anal. Biochem. 382:116-121(2008).
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis (PubMed:1907568). 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:1907568, PubMed:10852722,
CC PubMed:18721790). {ECO:0000269|PubMed:10852722,
CC ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:1907568}.
CC -!- SUBUNIT: Mammalian complex I is composed of 45 different subunits
CC (PubMed:10852722, PubMed:18721790). Interacts with ETFRF1. 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 (By
CC similarity). Interacts with alpha-1-microglobulin chain; this
CC interaction is required for the maintenance of mitochondrial redox
CC homeostasis. {ECO:0000250|UniProtKB:O14561,
CC ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:1907568,
CC ECO:0000305|PubMed:18721790}.
CC -!- MASS SPECTROMETRY: Mass=10751.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:1907568};
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000305}.
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DR EMBL; BC102128; AAI02129.1; -; mRNA.
DR EMBL; X61997; CAA43970.1; -; mRNA.
DR PIR; S16967; S16967.
DR RefSeq; NP_001035578.1; NM_001040488.2.
DR PDB; 5LC5; EM; 4.35 A; T=76-150, U=72-156.
DR PDB; 5LDW; EM; 4.27 A; T/U=69-156.
DR PDB; 5LDX; EM; 5.60 A; T/U=69-156.
DR PDB; 5O31; EM; 4.13 A; T/U=69-156.
DR PDB; 7QSD; EM; 3.10 A; T/U=1-156.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P52505; -.
DR SMR; P52505; -.
DR CORUM; P52505; -.
DR DIP; DIP-38826N; -.
DR IntAct; P52505; 42.
DR STRING; 9913.ENSBTAP00000008382; -.
DR BindingDB; P52505; -.
DR ChEMBL; CHEMBL614865; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P52505; -.
DR PeptideAtlas; P52505; -.
DR GeneID; 327702; -.
DR KEGG; bta:327702; -.
DR CTD; 4706; -.
DR eggNOG; KOG1748; Eukaryota.
DR InParanoid; P52505; -.
DR OrthoDB; 1473625at2759; -.
DR PRO; PR:P52505; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:AgBase.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:AgBase.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR GO; GO:0005504; F:fatty acid binding; IDA:AgBase.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; TAS:AgBase.
DR GO; GO:0016491; F:oxidoreductase activity; TAS:AgBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; TAS:AgBase.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; TAS:AgBase.
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 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:1907568"
FT CHAIN 69..156
FT /note="Acyl carrier protein, mitochondrial"
FT /id="PRO_0000180271"
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; 17402 MW; 340A12BFF005463F CRC64;
MAVRVLCACV RRLPTAFAPL PRLPTLAAAR PLSTTLFAAE TRTRPGAPLP ALVLAQVPGR
VTQLCRQYSD APPLTLEGIK DRVLYVLKLY DKIDPEKLSV NSHFMKDLGL DSLDQVEIIM
AMEDEFGFEI PDIDAEKLMC PQEIVDYIAD KKDVYE
