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Acyl carrier protein, mitochondrial (ACP) (CI-SDAP) (NADH-ubiquinone oxidoreductase 9.6 kDa subunit)

 ACPM_BOVIN              Reviewed;         156 AA.
P52505; Q3T150;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 2.
12-SEP-2018, entry version 134.
RecName: Full=Acyl carrier protein, mitochondrial;
Short=ACP;
AltName: Full=CI-SDAP;
AltName: Full=NADH-ubiquinone oxidoreductase 9.6 kDa subunit;
Flags: Precursor;
Name=NDUFAB1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 69-156, PROTEIN SEQUENCE OF 69-90,
SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND FUNCTION.
TISSUE=Heart;
PubMed=1907568; DOI=10.1016/0014-5793(91)80955-3;
Runswick M.J., Fearnley I.M., Skehel J.M., Walker J.E.;
"Presence of an acyl carrier protein in NADH:ubiquinone oxidoreductase
from bovine heart mitochondria.";
FEBS Lett. 286:121-124(1991).
[3]
PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, IDENTIFICATION IN COMPLEX
I, AND SUBCELLULAR LOCATION.
PubMed=10852722; DOI=10.1021/bi000335t;
Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E.;
"Resolution of the membrane domain of bovine complex I into
subcomplexes: implications for the structural organization of the
enzyme.";
Biochemistry 39:7229-7235(2000).
[4]
FUNCTION, SUBUNIT, IDENTIFICATION IN COMPLEX I, AND SUBCELLULAR
LOCATION.
PubMed=18721790; DOI=10.1016/j.ab.2008.07.029;
Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A.,
Robinson N.C.;
"Subunit analysis of bovine heart complex I by reversed-phase high-
performance liquid chromatography, electrospray ionization-tandem mass
spectrometry, and matrix-assisted laser desorption/ionization-time-of-
flight mass spectrometry.";
Anal. Biochem. 382:116-121(2008).
-!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
biosynthesis (PubMed:1907568). Accessory and non-catalytic subunit
of the mitochondrial membrane respiratory chain NADH dehydrogenase
(Complex I), which functions in the transfer of electrons from
NADH to the respiratory chain (PubMed:1907568, PubMed:10852722,
PubMed:18721790). {ECO:0000269|PubMed:10852722,
ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:1907568}.
-!- SUBUNIT: Mammalian complex I is composed of 45 different subunits
(PubMed:10852722, PubMed:18721790). Interacts with ETFRF1.
Intentified in a complex composed of MALSU1, MIEF1 upstream open
reading frame protein and NDUFAB1; within the trimeric complex
MIEF1 upstream open reading frame protein functions as a bridging
scaffold that interacts with MALSU1 on one side, and with NDUFAB1
on the other side. The complex interacts with the mitochondrial
large ribosomal subunit (By similarity).
{ECO:0000250|UniProtKB:O14561, ECO:0000269|PubMed:10852722,
ECO:0000269|PubMed:18721790}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:1907568,
ECO:0000305|PubMed:18721790}.
-!- MASS SPECTROMETRY: Mass=10751.6; Method=Electrospray; Range=69-
156; Evidence={ECO:0000269|PubMed:1907568};
-!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
{ECO:0000305}.
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EMBL; BC102128; AAI02129.1; -; mRNA.
EMBL; X61997; CAA43970.1; -; mRNA.
PIR; S16967; S16967.
RefSeq; NP_001035578.1; NM_001040488.2.
UniGene; Bt.321; -.
PDB; 5LC5; EM; 4.35 A; T=76-150, U=72-156.
PDB; 5LDW; EM; 4.27 A; T/U=69-156.
PDB; 5LDX; EM; 5.60 A; T/U=69-156.
PDB; 5O31; EM; 4.13 A; T/U=69-156.
PDBsum; 5LC5; -.
PDBsum; 5LDW; -.
PDBsum; 5LDX; -.
PDBsum; 5O31; -.
ProteinModelPortal; P52505; -.
SMR; P52505; -.
CORUM; P52505; -.
DIP; DIP-38826N; -.
IntAct; P52505; 42.
STRING; 9913.ENSBTAP00000008382; -.
BindingDB; P52505; -.
ChEMBL; CHEMBL614865; -.
TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
PaxDb; P52505; -.
PeptideAtlas; P52505; -.
PRIDE; P52505; -.
GeneID; 327702; -.
KEGG; bta:327702; -.
CTD; 4706; -.
eggNOG; KOG1748; Eukaryota.
eggNOG; COG0236; LUCA.
HOGENOM; HOG000178184; -.
HOVERGEN; HBG024318; -.
InParanoid; P52505; -.
KO; K03955; -.
PRO; PR:P52505; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005759; C:mitochondrial matrix; IDA:AgBase.
GO; GO:0031966; C:mitochondrial membrane; IDA:AgBase.
GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
GO; GO:0000035; F:acyl binding; IBA:GO_Central.
GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
GO; GO:0005504; F:fatty acid binding; IDA:AgBase.
GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; TAS:AgBase.
GO; GO:0016491; F:oxidoreductase activity; TAS:AgBase.
GO; GO:0031177; F:phosphopantetheine binding; IBA:GO_Central.
GO; GO:0006633; P:fatty acid biosynthetic process; TAS:AgBase.
GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; TAS:AgBase.
GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
Gene3D; 1.10.1200.10; -; 1.
HAMAP; MF_01217; Acyl_carrier; 1.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR003231; Acyl_carrier.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR006162; Ppantetheine_attach_site.
Pfam; PF00550; PP-binding; 1.
ProDom; PD000887; PD000887; 1.
SUPFAM; SSF47336; SSF47336; 1.
TIGRFAMs; TIGR00517; acyl_carrier; 1.
PROSITE; PS50075; CARRIER; 1.
PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Electron transport;
Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
Lipid metabolism; Mitochondrion; Phosphopantetheine; Phosphoprotein;
Reference proteome; Respiratory chain; Transit peptide; Transport.
TRANSIT 1 68 Mitochondrion.
{ECO:0000269|PubMed:1907568}.
CHAIN 69 156 Acyl carrier protein, mitochondrial.
/FTId=PRO_0000180271.
DOMAIN 77 152 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
MOD_RES 88 88 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CR21}.
MOD_RES 112 112 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
SEQUENCE 156 AA; 17402 MW; 340A12BFF005463F CRC64;
MAVRVLCACV RRLPTAFAPL PRLPTLAAAR PLSTTLFAAE TRTRPGAPLP ALVLAQVPGR
VTQLCRQYSD APPLTLEGIK DRVLYVLKLY DKIDPEKLSV NSHFMKDLGL DSLDQVEIIM
AMEDEFGFEI PDIDAEKLMC PQEIVDYIAD KKDVYE


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