ACPM3_ARATH
ID ACPM3_ARATH Reviewed; 131 AA.
AC Q9FGJ4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Acyl carrier protein 3, mitochondrial;
DE AltName: Full=MtACP-3;
DE Short=ACP;
DE AltName: Full=NADH-ubiquinone oxidoreductase 9.6 kDa subunit;
DE Flags: Precursor;
GN Name=MTACP2; OrderedLocusNames=At5g47630; ORFNames=MNJ7.22;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP THR-39.
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; AB025628; BAB09089.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95542.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95543.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70148.1; -; Genomic_DNA.
DR EMBL; AY063951; AAL36307.1; -; mRNA.
DR EMBL; AY096717; AAM20351.1; -; mRNA.
DR RefSeq; NP_001078726.1; NM_001085257.1.
DR RefSeq; NP_001331779.1; NM_001344735.1.
DR RefSeq; NP_199574.1; NM_124136.5.
DR AlphaFoldDB; Q9FGJ4; -.
DR SMR; Q9FGJ4; -.
DR STRING; 3702.AT5G47630.2; -.
DR PaxDb; Q9FGJ4; -.
DR PRIDE; Q9FGJ4; -.
DR ProteomicsDB; 244378; -.
DR EnsemblPlants; AT5G47630.1; AT5G47630.1; AT5G47630.
DR EnsemblPlants; AT5G47630.2; AT5G47630.2; AT5G47630.
DR EnsemblPlants; AT5G47630.3; AT5G47630.3; AT5G47630.
DR GeneID; 834813; -.
DR Gramene; AT5G47630.1; AT5G47630.1; AT5G47630.
DR Gramene; AT5G47630.2; AT5G47630.2; AT5G47630.
DR Gramene; AT5G47630.3; AT5G47630.3; AT5G47630.
DR KEGG; ath:AT5G47630; -.
DR Araport; AT5G47630; -.
DR TAIR; locus:2168968; AT5G47630.
DR eggNOG; KOG1748; Eukaryota.
DR HOGENOM; CLU_108696_0_3_1; -.
DR InParanoid; Q9FGJ4; -.
DR OMA; FISKMNF; -.
DR OrthoDB; 1473625at2759; -.
DR PhylomeDB; Q9FGJ4; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9FGJ4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGJ4; baseline and differential.
DR Genevisible; Q9FGJ4; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IMP: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 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.
PE 1: Evidence at protein level;
KW Electron transport; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Respiratory chain; Transit peptide;
KW Transport.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 40..131
FT /note="Acyl carrier protein 3, mitochondrial"
FT /id="PRO_0000410993"
FT DOMAIN 49..124
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 84
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 131 AA; 14615 MW; 1109BED2FA615614 CRC64;
MHCIRSSILQ HLRLRVSVRP TSLLQNENGF KSIGIFNFTS EAAADGGQDQ ILSRVIELVK
KYDKTNTSEV TERADFQKDL SLDSLDKTEL VMAIEEEFSI EIPDEKADKL TCCGDVATYI
LSETPTKASE S
