ACPM2_ARATH
ID ACPM2_ARATH Reviewed; 126 AA.
AC O80800; Q8LEU1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Acyl carrier protein 2, mitochondrial;
DE AltName: Full=MtACP-2;
DE Short=ACP;
DE AltName: Full=NADH-ubiquinone oxidoreductase 9.6 kDa subunit;
DE Flags: Precursor;
GN Name=MTACP2; OrderedLocusNames=At1g65290; ORFNames=T8F5.6;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-36.
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 -!- INTERACTION:
CC O80800; Q39016: CPK11; NbExp=4; IntAct=EBI-2298689, EBI-979321;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004512; AAC27139.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34354.1; -; Genomic_DNA.
DR EMBL; AY085236; AAM62469.1; -; mRNA.
DR PIR; T02351; T02351.
DR RefSeq; NP_176708.1; NM_105202.5.
DR PDB; 7A23; EM; 3.70 A; e=1-126.
DR PDB; 7AQR; EM; 2.91 A; U=1-126.
DR PDB; 7AR7; EM; 3.72 A; U=44-126.
DR PDB; 7AR8; EM; 3.53 A; U=1-126.
DR PDB; 7ARB; EM; 3.41 A; U=1-126.
DR PDBsum; 7A23; -.
DR PDBsum; 7AQR; -.
DR PDBsum; 7AR7; -.
DR PDBsum; 7AR8; -.
DR PDBsum; 7ARB; -.
DR AlphaFoldDB; O80800; -.
DR SMR; O80800; -.
DR BioGRID; 28057; 1.
DR IntAct; O80800; 1.
DR STRING; 3702.AT1G65290.1; -.
DR TCDB; 3.D.1.6.3; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; O80800; -.
DR PRIDE; O80800; -.
DR ProteomicsDB; 244501; -.
DR EnsemblPlants; AT1G65290.1; AT1G65290.1; AT1G65290.
DR GeneID; 842836; -.
DR Gramene; AT1G65290.1; AT1G65290.1; AT1G65290.
DR KEGG; ath:AT1G65290; -.
DR Araport; AT1G65290; -.
DR TAIR; locus:2206300; AT1G65290.
DR eggNOG; KOG1748; Eukaryota.
DR HOGENOM; CLU_108696_0_3_1; -.
DR OMA; HSIHHRR; -.
DR OrthoDB; 1473625at2759; -.
DR PhylomeDB; O80800; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:O80800; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80800; baseline and differential.
DR Genevisible; O80800; 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:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IMP:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; 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..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 37..126
FT /note="Acyl carrier protein 2, mitochondrial"
FT /id="PRO_0000410992"
FT DOMAIN 48..123
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 83
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 7
FT /note="M -> L (in Ref. 3; AAM62469)"
FT /evidence="ECO:0000305"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7AQR"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:7AQR"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:7AQR"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:7AQR"
SQ SEQUENCE 126 AA; 14167 MW; ADE6ED3C25AEE138 CRC64;
MAARGAMLRY LRVNVNPTIQ NPRECVLPFS ILLRRFSEEV RGSFLDKSEV TDRVLSVVKN
FQKVDPSKVT PKANFQNDLG LDSLDSVEVV MALEEEFGFE IPDNEADKIQ SIDLAVDFIA
SHPQAK
