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Outer envelope protein 64, mitochondrial (Mitochondrial outer membrane protein 64) (mtOM64) (Translocon at the outer membrane of chloroplasts 64-V) (AtTOC64-V)

 OE64M_ARATH             Reviewed;         603 AA.
F4KCL7; Q9FY73;
16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
22-NOV-2017, entry version 59.
RecName: Full=Outer envelope protein 64, mitochondrial;
AltName: Full=Mitochondrial outer membrane protein 64;
Short=mtOM64;
AltName: Full=Translocon at the outer membrane of chloroplasts 64-V;
Short=AtTOC64-V;
Name=OM64; Synonyms=TOC64-V; OrderedLocusNames=At5g09420;
ORFNames=T5E8.220;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=14741350; DOI=10.1016/S0014-5793(03)01457-1;
Chew O., Lister R., Qbadou S., Heazlewood J.L., Soll J., Schleiff E.,
Millar A.H., Whelan J.;
"A plant outer mitochondrial membrane protein with high amino acid
sequence identity to a chloroplast protein import receptor.";
FEBS Lett. 557:109-114(2004).
[4]
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=17655652; DOI=10.1111/j.1365-313X.2007.03207.x;
Aronsson H., Boij P., Patel R., Wardle A., Toepel M., Jarvis P.;
"Toc64/OEP64 is not essential for the efficient import of proteins
into chloroplasts in Arabidopsis thaliana.";
Plant J. 52:53-68(2007).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[6]
3D-STRUCTURE MODELING.
PubMed=19198901; DOI=10.1007/s00894-008-0449-y;
Mirus O., Bionda T., von Haeseler A., Schleiff E.;
"Evolutionarily evolved discriminators in the 3-TPR domain of the
Toc64 family involved in protein translocation at the outer membrane
of chloroplasts and mitochondria.";
J. Mol. Model. 15:971-982(2009).
-!- FUNCTION: Chaperone receptor mediating Hsp90-dependent protein
targeting to mitochondria. {ECO:0000250}.
-!- INTERACTION:
Q7DM06:- (xeno); NbExp=2; IntAct=EBI-2124066, EBI-2124012;
O80413:541617 (xeno); NbExp=2; IntAct=EBI-2124066, EBI-2362258;
Q07185:AOX1 (xeno); NbExp=2; IntAct=EBI-2124066, EBI-2123914;
Q9LHE5:TOM40-1; NbExp=2; IntAct=EBI-2124066, EBI-2124038;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000305};
Single-pass membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in roots and flower buds. Detected
in leaves. {ECO:0000269|PubMed:14741350,
ECO:0000269|PubMed:17655652}.
-!- DISRUPTION PHENOTYPE: No visible phenotype.
{ECO:0000269|PubMed:17655652}.
-!- SEQUENCE CAUTION:
Sequence=CAC05468.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AL391712; CAC05468.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED91391.1; -; Genomic_DNA.
RefSeq; NP_196504.2; NM_120979.3.
UniGene; At.10055; -.
ProteinModelPortal; F4KCL7; -.
BioGrid; 16079; 9.
IntAct; F4KCL7; 5.
STRING; 3702.AT5G09420.1; -.
iPTMnet; F4KCL7; -.
SwissPalm; F4KCL7; -.
PaxDb; F4KCL7; -.
EnsemblPlants; AT5G09420.1; AT5G09420.1; AT5G09420.
GeneID; 830801; -.
Gramene; AT5G09420.1; AT5G09420.1; AT5G09420.
KEGG; ath:AT5G09420; -.
Araport; AT5G09420; -.
TAIR; locus:2184757; AT5G09420.
eggNOG; KOG1124; Eukaryota.
eggNOG; KOG1211; Eukaryota.
eggNOG; COG0154; LUCA.
eggNOG; COG0457; LUCA.
HOGENOM; HOG000116697; -.
InParanoid; F4KCL7; -.
OMA; NGANATY; -.
OrthoDB; EOG093606IM; -.
PRO; PR:F4KCL7; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; F4KCL7; baseline and differential.
Genevisible; F4KCL7; AT.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0004040; F:amidase activity; IEA:InterPro.
GO; GO:0006626; P:protein targeting to mitochondrion; IMP:TAIR.
Gene3D; 1.25.40.10; -; 1.
Gene3D; 3.90.1300.10; -; 1.
InterPro; IPR000120; Amidase.
InterPro; IPR023631; Amidase_dom.
InterPro; IPR036928; AS_sf.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR11895; PTHR11895; 1.
Pfam; PF01425; Amidase; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
SUPFAM; SSF75304; SSF75304; 1.
PROSITE; PS50005; TPR; 3.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Membrane; Mitochondrion;
Mitochondrion outer membrane; Protein transport; Reference proteome;
Repeat; TPR repeat; Transmembrane; Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 603 Outer envelope protein 64, mitochondrial.
/FTId=PRO_0000414024.
TRANSMEM 16 32 Helical. {ECO:0000255}.
REPEAT 488 521 TPR 1.
REPEAT 523 555 TPR 2.
REPEAT 556 589 TPR 3.
COMPBIAS 58 65 Poly-Pro.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
SEQUENCE 603 AA; 65912 MW; 6D4191B24EB9205F CRC64;
MSNTLSLIQS NASNPKVWVV IGVTVAGIVI LAETRKRRIR ALREEDFGAF LDRFELLPFP
PPPPPAAKQS LSGLTFSISD AFDVKDYITG FGCPQWKKTH EAAEKTAVVV TTLLKNGATC
VGKTIMDELG FGIIGENKHY GTPINPLMPD NVPGGCSSGS AVSVGAELVD FSLGIDTTGG
VRVPAAFCGI LGFRPSQGTV SSVGVLPNSQ SLETVGWFAS DPSVLCQVGH ALLNLSAVTH
RRQRSLIFAD DLFELSDIPK QKSVQVVRKA IENLSGYKTP KHVNVGQYVA SNVPSLAEFC
EQSGKSQNSA STLRALSSVM LAIQRHEFKT NHEEWWQTCK SFLGPRFSND VVTALKSKNE
SIKSLYRVKN EMRATIQSLL KEDGILVIPT VADPPPRLNT KRNKSLNEFL DRTYALSCIA
SMSGCCQVTI PLGEHGDRPI SVSLLTYYGG DKFLLDTTLD VYASLQDQAK LASNLAPVSD
TNGNMEASEV MKEKGNAAYK GKQWNKAVNF YTEAIKLNGA NATYYCNRAA AFLELCCFQQ
AEQDCTKAML IDKKNVKAYL RRGTARESLV RYKEAAADFR HALVLEPQNK TAKVAEKRLR
KHI


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