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OE64M_ARATH
ID   OE64M_ARATH             Reviewed;         603 AA.
AC   F4KCL7; Q9FY73;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Outer envelope protein 64, mitochondrial;
DE   AltName: Full=Mitochondrial outer membrane protein 64;
DE            Short=mtOM64;
DE   AltName: Full=Translocon at the outer membrane of chloroplasts 64-V;
DE            Short=AtTOC64-V;
GN   Name=OM64; Synonyms=TOC64-V; OrderedLocusNames=At5g09420;
GN   ORFNames=T5E8.220;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=14741350; DOI=10.1016/s0014-5793(03)01457-1;
RA   Chew O., Lister R., Qbadou S., Heazlewood J.L., Soll J., Schleiff E.,
RA   Millar A.H., Whelan J.;
RT   "A plant outer mitochondrial membrane protein with high amino acid sequence
RT   identity to a chloroplast protein import receptor.";
RL   FEBS Lett. 557:109-114(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=17655652; DOI=10.1111/j.1365-313x.2007.03207.x;
RA   Aronsson H., Boij P., Patel R., Wardle A., Toepel M., Jarvis P.;
RT   "Toc64/OEP64 is not essential for the efficient import of proteins into
RT   chloroplasts in Arabidopsis thaliana.";
RL   Plant J. 52:53-68(2007).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [6]
RP   3D-STRUCTURE MODELING.
RX   PubMed=19198901; DOI=10.1007/s00894-008-0449-y;
RA   Mirus O., Bionda T., von Haeseler A., Schleiff E.;
RT   "Evolutionarily evolved discriminators in the 3-TPR domain of the Toc64
RT   family involved in protein translocation at the outer membrane of
RT   chloroplasts and mitochondria.";
RL   J. Mol. Model. 15:971-982(2009).
CC   -!- FUNCTION: Chaperone receptor mediating Hsp90-dependent protein
CC       targeting to mitochondria. {ECO:0000250}.
CC   -!- INTERACTION:
CC       F4KCL7; Q9LHE5: TOM40-1; NbExp=2; IntAct=EBI-2124066, EBI-2124038;
CC       F4KCL7; O80413: 103627788; Xeno; NbExp=2; IntAct=EBI-2124066, EBI-2362258;
CC       F4KCL7; Q07185: AOX1; Xeno; NbExp=2; IntAct=EBI-2124066, EBI-2123914;
CC       F4KCL7; Q7DM06; Xeno; NbExp=2; IntAct=EBI-2124066, EBI-2124012;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and flower buds. Detected in
CC       leaves. {ECO:0000269|PubMed:14741350, ECO:0000269|PubMed:17655652}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:17655652}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC05468.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL391712; CAC05468.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED91391.1; -; Genomic_DNA.
DR   RefSeq; NP_196504.2; NM_120979.3.
DR   PDB; 6HPG; X-ray; 2.00 A; A/B/C/D/E/F=483-603.
DR   PDB; 6Q3Q; X-ray; 2.00 A; A/B=483-603.
DR   PDBsum; 6HPG; -.
DR   PDBsum; 6Q3Q; -.
DR   AlphaFoldDB; F4KCL7; -.
DR   SMR; F4KCL7; -.
DR   BioGRID; 16079; 9.
DR   IntAct; F4KCL7; 5.
DR   STRING; 3702.AT5G09420.1; -.
DR   iPTMnet; F4KCL7; -.
DR   SwissPalm; F4KCL7; -.
DR   PaxDb; F4KCL7; -.
DR   PRIDE; F4KCL7; -.
DR   ProteomicsDB; 239016; -.
DR   EnsemblPlants; AT5G09420.1; AT5G09420.1; AT5G09420.
DR   GeneID; 830801; -.
DR   Gramene; AT5G09420.1; AT5G09420.1; AT5G09420.
DR   KEGG; ath:AT5G09420; -.
DR   Araport; AT5G09420; -.
DR   TAIR; locus:2184757; AT5G09420.
DR   eggNOG; KOG1124; Eukaryota.
DR   eggNOG; KOG1211; Eukaryota.
DR   HOGENOM; CLU_009600_17_1_1; -.
DR   InParanoid; F4KCL7; -.
DR   OMA; TGENSHY; -.
DR   OrthoDB; 447457at2759; -.
DR   PRO; PR:F4KCL7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4KCL7; baseline and differential.
DR   Genevisible; F4KCL7; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:CACAO.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; IMP:TAIR.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF01425; Amidase; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Protein transport; Reference proteome;
KW   Repeat; TPR repeat; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..603
FT                   /note="Outer envelope protein 64, mitochondrial"
FT                   /id="PRO_0000414024"
FT   TRANSMEM        16..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          488..521
FT                   /note="TPR 1"
FT   REPEAT          523..555
FT                   /note="TPR 2"
FT   REPEAT          556..589
FT                   /note="TPR 3"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   HELIX           484..500
FT                   /evidence="ECO:0007829|PDB:6HPG"
FT   HELIX           504..517
FT                   /evidence="ECO:0007829|PDB:6HPG"
FT   HELIX           522..534
FT                   /evidence="ECO:0007829|PDB:6HPG"
FT   HELIX           538..551
FT                   /evidence="ECO:0007829|PDB:6HPG"
FT   HELIX           556..568
FT                   /evidence="ECO:0007829|PDB:6HPG"
FT   HELIX           572..585
FT                   /evidence="ECO:0007829|PDB:6HPG"
FT   HELIX           590..600
FT                   /evidence="ECO:0007829|PDB:6HPG"
SQ   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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