ACPM1_ARATH
ID ACPM1_ARATH Reviewed; 122 AA.
AC P53665;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Acyl carrier protein 1, mitochondrial;
DE AltName: Full=MtACP-1;
DE Short=ACP;
DE AltName: Full=NADH-ubiquinone oxidoreductase 9.6 kDa subunit;
DE Flags: Precursor;
GN Name=MTACP1; OrderedLocusNames=At2g44620; ORFNames=F16B22.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8016262; DOI=10.1104/pp.104.4.1221;
RA Shintani D.K., Ohlrogge J.B.;
RT "The characterization of a mitochondrial acyl carrier protein isoform
RT isolated from Arabidopsis thaliana.";
RL Plant Physiol. 104:1221-1229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-34.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis (By similarity). May be involved in the synthesis of short
CC and medium chain fatty acids. 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}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Complex I is composed of at least 49 different subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:25732537}.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of the apo-ACP-like protein. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000305}.
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DR EMBL; L23574; AAB96840.1; -; mRNA.
DR EMBL; AC003672; AAC27464.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10448.1; -; Genomic_DNA.
DR PIR; T01589; T01589.
DR RefSeq; NP_181990.1; NM_130026.4.
DR PDB; 7A23; EM; 3.70 A; k=1-122.
DR PDB; 7A24; EM; 3.80 A; k=1-122.
DR PDB; 7AQW; EM; 3.17 A; T=1-122.
DR PDB; 7AR7; EM; 3.72 A; T=38-121.
DR PDB; 7AR8; EM; 3.53 A; T=1-122.
DR PDB; 7ARB; EM; 3.41 A; T=1-122.
DR PDBsum; 7A23; -.
DR PDBsum; 7A24; -.
DR PDBsum; 7AQW; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; P53665; -.
DR SMR; P53665; -.
DR BioGRID; 4406; 1.
DR STRING; 3702.AT2G44620.1; -.
DR PaxDb; P53665; -.
DR PRIDE; P53665; -.
DR ProteomicsDB; 244740; -.
DR EnsemblPlants; AT2G44620.1; AT2G44620.1; AT2G44620.
DR GeneID; 819070; -.
DR Gramene; AT2G44620.1; AT2G44620.1; AT2G44620.
DR KEGG; ath:AT2G44620; -.
DR Araport; AT2G44620; -.
DR TAIR; locus:2042331; AT2G44620.
DR eggNOG; KOG1748; Eukaryota.
DR HOGENOM; CLU_108696_0_3_1; -.
DR InParanoid; P53665; -.
DR OMA; DKIDSCA; -.
DR OrthoDB; 1473625at2759; -.
DR PhylomeDB; P53665; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:P53665; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P53665; baseline and differential.
DR Genevisible; P53665; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:TAIR.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IMP:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:TAIR.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IDA:TAIR.
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; Electron transport; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Respiratory chain;
KW Transit peptide; Transport.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 35..122
FT /note="Acyl carrier protein 1, mitochondrial"
FT /id="PRO_0000000567"
FT DOMAIN 44..119
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 79
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:7AQW"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7AQW"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:7AQW"
FT HELIX 79..93
FT /evidence="ECO:0007829|PDB:7AQW"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:7AQW"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:7AQW"
SQ SEQUENCE 122 AA; 13718 MW; 589D6573F4FCC5A8 CRC64;
MALRNAILRH LRVPVQTLGL NQSKIGFLGT IRSFSSHDDH LSREAVVDRV LDVVKSFPKV
DPSKVTPEVH FQNDLGLDSL DTVEIVMAIE EEFKLEIPDK EADKIDSCSL AIEYVYNHPM
SS
