OP163_ARATH
ID OP163_ARATH Reviewed; 159 AA.
AC O48528; F4IMZ5;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Outer envelope pore protein 16-3, chloroplastic/mitochondrial;
DE AltName: Full=Chloroplastic outer envelope pore protein of 16 kDa 3;
DE Short=AtOEP16-3;
DE Short=OEP16-3;
DE AltName: Full=Mitochondrial complex I subunit B14.7;
GN Name=OEP163; Synonyms=B14.7; OrderedLocusNames=At2g42210;
GN ORFNames=T24P15.12;
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] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX PubMed=17098851; DOI=10.1104/pp.106.090688;
RA Murcha M.W., Elhafez D., Lister R., Tonti-Filippini J., Baumgartner M.,
RA Philippar K., Carrie C., Mokranjac D., Soll J., Whelan J.;
RT "Characterization of the preprotein and amino acid transporter gene family
RT in Arabidopsis.";
RL Plant Physiol. 143:199-212(2007).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND GENE FAMILY.
RX PubMed=17406791; DOI=10.1007/s11103-007-9156-9;
RA Meyer E.H., Heazlewood J.L., Millar A.H.;
RT "Mitochondrial acyl carrier proteins in Arabidopsis thaliana are
RT predominantly soluble matrix proteins and none can be confirmed as subunits
RT of respiratory Complex I.";
RL Plant Mol. Biol. 64:319-327(2007).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17202255; DOI=10.1073/pnas.0610062104;
RA Philippar K., Geis T., Ilkavets I., Oster U., Schwenkert S., Meurer J.,
RA Soll J.;
RT "Chloroplast biogenesis: the use of mutants to study the etioplast-
RT chloroplast transition.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:678-683(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18189341; DOI=10.1021/pr700595p;
RA Meyer E.H., Taylor N.L., Millar A.H.;
RT "Resolving and identifying protein components of plant mitochondrial
RT respiratory complexes using three dimensions of gel electrophoresis.";
RL J. Proteome Res. 7:786-794(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=21841088; DOI=10.1104/pp.111.182352;
RA Klodmann J., Senkler M., Rode C., Braun H.-P.;
RT "Defining the protein complex proteome of plant mitochondria.";
RL Plant Physiol. 157:587-598(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
RP INTERACTION WITH TIM23-2, SUBCELLULAR LOCATION, SUBUNIT, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22730406; DOI=10.1105/tpc.112.098731;
RA Wang Y., Carrie C., Giraud E., Elhafez D., Narsai R., Duncan O., Whelan J.,
RA Murcha M.W.;
RT "Dual location of the mitochondrial preprotein transporters B14.7 and
RT Tim23-2 in complex I and the TIM17:23 complex in Arabidopsis links
RT mitochondrial activity and biogenesis.";
RL Plant Cell 24:2675-2695(2012).
CC -!- FUNCTION: Voltage-dependent high-conductance channel with a slight
CC cation-selectivity; selective for amino acids but excludes
CC triosephosphates or uncharged sugars. Non-essential amino acid-
CC selective channel protein and translocation pore for
CC NADPH:protochlorophyllide oxidoreductase A (PORA) and possibly PORB (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and oligomers in membrane (By similarity). Part of
CC both the NADH-ubiquinone oxidoreductase complex I and of the TIM17:23
CC complex. Interacts with TIM23-2. {ECO:0000250,
CC ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:22730406}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:18431481}; Multi-pass membrane protein.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:21841088}; Multi-pass
CC membrane protein {ECO:0000255}. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:21841088}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O48528-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O48528-2; Sequence=VSP_042321;
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:22730406}.
CC -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. Plastid outer
CC envelope porin OEP16 (TC 1.B.30) subfamily. {ECO:0000305}.
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DR EMBL; DQ386643; ABD48955.1; -; mRNA.
DR EMBL; AC002561; AAB88646.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10086.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10087.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10088.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10089.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62006.1; -; Genomic_DNA.
DR EMBL; AY086879; AAM63925.1; -; mRNA.
DR EMBL; BT025617; ABF59035.1; -; mRNA.
DR PIR; T00930; T00930.
DR RefSeq; NP_001031527.1; NM_001036450.2. [O48528-2]
DR RefSeq; NP_001031528.1; NM_001036451.2. [O48528-1]
DR RefSeq; NP_001031529.1; NM_001036452.1. [O48528-1]
DR RefSeq; NP_001324189.1; NM_001336959.1. [O48528-1]
DR RefSeq; NP_565968.1; NM_129783.4. [O48528-1]
DR AlphaFoldDB; O48528; -.
DR SMR; O48528; -.
DR BioGRID; 4158; 1.
DR IntAct; O48528; 1.
DR STRING; 3702.AT2G42210.2; -.
DR iPTMnet; O48528; -.
DR MetOSite; O48528; -.
DR PaxDb; O48528; -.
DR PRIDE; O48528; -.
DR ProteomicsDB; 248897; -. [O48528-1]
DR DNASU; 818821; -.
DR EnsemblPlants; AT2G42210.1; AT2G42210.1; AT2G42210. [O48528-1]
DR EnsemblPlants; AT2G42210.2; AT2G42210.2; AT2G42210. [O48528-2]
DR EnsemblPlants; AT2G42210.3; AT2G42210.3; AT2G42210. [O48528-1]
DR EnsemblPlants; AT2G42210.4; AT2G42210.4; AT2G42210. [O48528-1]
DR EnsemblPlants; AT2G42210.5; AT2G42210.5; AT2G42210. [O48528-1]
DR GeneID; 818821; -.
DR Gramene; AT2G42210.1; AT2G42210.1; AT2G42210. [O48528-1]
DR Gramene; AT2G42210.2; AT2G42210.2; AT2G42210. [O48528-2]
DR Gramene; AT2G42210.3; AT2G42210.3; AT2G42210. [O48528-1]
DR Gramene; AT2G42210.4; AT2G42210.4; AT2G42210. [O48528-1]
DR Gramene; AT2G42210.5; AT2G42210.5; AT2G42210. [O48528-1]
DR KEGG; ath:AT2G42210; -.
DR Araport; AT2G42210; -.
DR TAIR; locus:2059989; AT2G42210.
DR eggNOG; KOG3225; Eukaryota.
DR HOGENOM; CLU_114728_0_0_1; -.
DR InParanoid; O48528; -.
DR OrthoDB; 1456214at2759; -.
DR PRO; PR:O48528; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48528; baseline and differential.
DR Genevisible; O48528; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009527; C:plastid outer membrane; ISS:TAIR.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IEA:InterPro.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IEA:InterPro.
DR InterPro; IPR039175; TIM22.
DR PANTHER; PTHR14110; PTHR14110; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chloroplast; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Mitochondrion outer membrane;
KW Plastid; Plastid outer membrane; Porin; Reference proteome; Transmembrane;
KW Transmembrane beta strand; Transmembrane helix; Transport.
FT CHAIN 1..159
FT /note="Outer envelope pore protein 16-3,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000415698"
FT TRANSMEM 24..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..65
FT /note="Contains beta strands"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1
FT /note="M -> MFNLCALGRTVEEIM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042321"
SQ SEQUENCE 159 AA; 16999 MW; 3102BC2ACFA389E7 CRC64;
MDPAEMRYLE EEDGPLMKTI KGSITGFGAG TIYGTILATW KDVPRVERNV ALPGLIRTLK
MMGTHGLTFA AIGGVYIGVE QLVQNFRSKR DFYNGAIGGF VAGASVLGYR ARSIPTAIAA
GATLAVTSAL IDSGGQTTRV DNGREYYPYT VEKRAEADS
