MTX_ARATH
ID MTX_ARATH Reviewed; 315 AA.
AC O64471;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Mitochondrial outer membrane import complex protein METAXIN;
GN Name=MTX1; OrderedLocusNames=At2g19080; ORFNames=T20K24.9;
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=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 [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 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 [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14730085; DOI=10.1104/pp.103.033910;
RA Lister R., Chew O., Lee M.N., Heazlewood J.L., Clifton R., Parker K.L.,
RA Millar A.H., Whelan J.;
RT "A transcriptomic and proteomic characterization of the Arabidopsis
RT mitochondrial protein import apparatus and its response to mitochondrial
RT dysfunction.";
RL Plant Physiol. 134:777-789(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, SUBUNIT, AND
RP INTERACTION WITH MITOCHONDRIAL PRECURSOR PROTEINS.
RX PubMed=17981999; DOI=10.1105/tpc.107.050534;
RA Lister R., Carrie C., Duncan O., Ho L.H., Howell K.A., Murcha M.W.,
RA Whelan J.;
RT "Functional definition of outer membrane proteins involved in preprotein
RT import into mitochondria.";
RL Plant Cell 19:3739-3759(2007).
RN [7]
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).
CC -!- FUNCTION: Involved in transport of proteins into the mitochondrion.
CC {ECO:0000269|PubMed:17981999}.
CC -!- SUBUNIT: Part of a high molecular weight complex that is distinct from
CC the TOM complex. Interacts with a variety of mitochondrial precursor
CC proteins. {ECO:0000269|PubMed:17981999}.
CC -!- INTERACTION:
CC O64471; Q5ICL9: NPR4; NbExp=3; IntAct=EBI-2123898, EBI-1392093;
CC O64471; Q9LHE5: TOM40-1; NbExp=2; IntAct=EBI-2123898, EBI-2124038;
CC O64471; O80413: 103627788; Xeno; NbExp=2; IntAct=EBI-2123898, EBI-2362258;
CC O64471; Q07185: AOX1; Xeno; NbExp=3; IntAct=EBI-2123898, EBI-2123914;
CC O64471; Q7DM06; Xeno; NbExp=2; IntAct=EBI-2123898, EBI-2124012;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}. Mitochondrion outer membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The
CC inner membrane localization is based on mass spectrometry
CC identification and may be the result of sample contamination.
CC {ECO:0000269|PubMed:14730085, ECO:0000269|PubMed:17981999}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, young cotyledons, flowers and
CC leaves. {ECO:0000269|PubMed:14730085}.
CC -!- DISRUPTION PHENOTYPE: Decreased growth, abnormal leaf morphology and
CC ectopic floral development and sterility. Higher starch accumulation in
CC chloroplasts and reduced rates of mitochondrial protein import.
CC {ECO:0000269|PubMed:17981999}.
CC -!- SIMILARITY: Belongs to the metaxin family. {ECO:0000305}.
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DR EMBL; AC002392; AAD12026.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06846.1; -; Genomic_DNA.
DR EMBL; AY070737; AAL50078.1; -; mRNA.
DR EMBL; AY087648; AAM65186.1; -; mRNA.
DR EMBL; AY142046; AAM98310.1; -; mRNA.
DR PIR; T00528; T00528.
DR RefSeq; NP_565446.1; NM_127465.4.
DR AlphaFoldDB; O64471; -.
DR BioGRID; 1782; 9.
DR IntAct; O64471; 8.
DR STRING; 3702.AT2G19080.1; -.
DR iPTMnet; O64471; -.
DR PaxDb; O64471; -.
DR PRIDE; O64471; -.
DR ProteomicsDB; 238463; -.
DR EnsemblPlants; AT2G19080.1; AT2G19080.1; AT2G19080.
DR GeneID; 816425; -.
DR Gramene; AT2G19080.1; AT2G19080.1; AT2G19080.
DR KEGG; ath:AT2G19080; -.
DR Araport; AT2G19080; -.
DR TAIR; locus:2059024; AT2G19080.
DR eggNOG; KOG3028; Eukaryota.
DR HOGENOM; CLU_071432_0_0_1; -.
DR InParanoid; O64471; -.
DR OMA; PWPENAA; -.
DR OrthoDB; 1219712at2759; -.
DR PhylomeDB; O64471; -.
DR PRO; PR:O64471; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64471; baseline and differential.
DR Genevisible; O64471; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0001401; C:SAM complex; IEA:InterPro.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:TAIR.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR017410; Metaxin1/3.
DR InterPro; IPR033468; Metaxin_GST.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR Pfam; PF17171; GST_C_6; 1.
DR Pfam; PF17172; GST_N_4; 1.
DR PIRSF; PIRSF038150; Metaxin; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion outer membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..315
FT /note="Mitochondrial outer membrane import complex protein
FT METAXIN"
FT /id="PRO_0000420943"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 240..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 157..181
FT /evidence="ECO:0000255"
FT COMPBIAS 240..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 315 AA; 35854 MW; 31933D9255F33B55 CRC64;
MEGDQETNVY TLVARKPSFD LPTACPNCLP AYIYLKLAQL PFELAFNSTF PDSDELPYFE
SDTYVAYNNE DGGVIEKLKK DGIVNLDSQL QSLSDYLSLK ALIVSWLEEA LTYEIWVGTE
GISTSKIYYS DLPWVISKVL FYKQTYLAKN RLGITKENAE QREKQIYKRA SEAYEALSTR
LGEQKFLFED RPSSLDAFLL SHILFIIQAL PVTSVLRCKL LEHSNLVRYA EKLKSEFLEA
SSSSPSPPLH SFPSSFPRKS SKPKSKPKVE KTEEEKKFKK RARFFLAAQF LAVVIYVSVM
GGGSSDELEY EDEDD
