PMD1_ARATH
ID PMD1_ARATH Reviewed; 318 AA.
AC Q9LXR8; Q8L998;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Peroxisomal and mitochondrial division factor 1 {ECO:0000303|PubMed:22147290};
GN Name=PMD1 {ECO:0000303|PubMed:22147290};
GN OrderedLocusNames=At3g58840 {ECO:0000312|Araport:AT3G58840};
GN ORFNames=T20N10.190 {ECO:0000312|EMBL:CAB88301.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, SUBUNIT, INTERACTION WITH PMD2, SUBCELLULAR LOCATION, TOPOLOGY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=22147290; DOI=10.1105/tpc.111.090142;
RA Aung K., Hu J.;
RT "The Arabidopsis tail-anchored protein PEROXISOMAL AND MITOCHONDRIAL
RT DIVISION FACTOR1 is involved in the morphogenesis and proliferation of
RT peroxisomes and mitochondria.";
RL Plant Cell 23:4446-4461(2011).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=21896887; DOI=10.1104/pp.111.183160;
RA Duncan O., Taylor N.L., Carrie C., Eubel H., Kubiszewski-Jakubiak S.,
RA Zhang B., Narsai R., Millar A.H., Whelan J.;
RT "Multiple lines of evidence localize signaling, morphology, and lipid
RT biosynthesis machinery to the mitochondrial outer membrane of
RT Arabidopsis.";
RL Plant Physiol. 157:1093-1113(2011).
CC -!- FUNCTION: Involved in morphogenesis and proliferation of peroxisomes
CC and mitochondria, independently from the previously defined pathway
CC controlled by the FIS1-DRP3 complex. {ECO:0000269|PubMed:22147290}.
CC -!- SUBUNIT: Homodimer. Interacts with PMD2. {ECO:0000269|PubMed:22147290}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:22147290}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:21896887, ECO:0000269|PubMed:22147290}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Enlarged peroxisomes and elongated mitochondria.
CC {ECO:0000269|PubMed:22147290}.
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DR EMBL; AL353032; CAB88301.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79838.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79839.1; -; Genomic_DNA.
DR EMBL; BT024778; ABD59116.1; -; mRNA.
DR EMBL; AY088565; AAM66096.1; -; mRNA.
DR PIR; T49167; T49167.
DR RefSeq; NP_001078312.1; NM_001084843.2.
DR RefSeq; NP_191443.1; NM_115746.1.
DR AlphaFoldDB; Q9LXR8; -.
DR SMR; Q9LXR8; -.
DR STRING; 3702.AT3G58840.1; -.
DR PaxDb; Q9LXR8; -.
DR PRIDE; Q9LXR8; -.
DR ProteomicsDB; 234744; -.
DR EnsemblPlants; AT3G58840.1; AT3G58840.1; AT3G58840.
DR EnsemblPlants; AT3G58840.2; AT3G58840.2; AT3G58840.
DR GeneID; 825053; -.
DR Gramene; AT3G58840.1; AT3G58840.1; AT3G58840.
DR Gramene; AT3G58840.2; AT3G58840.2; AT3G58840.
DR KEGG; ath:AT3G58840; -.
DR Araport; AT3G58840; -.
DR TAIR; locus:2099114; AT3G58840.
DR eggNOG; ENOG502RY0Y; Eukaryota.
DR HOGENOM; CLU_074678_0_0_1; -.
DR InParanoid; Q9LXR8; -.
DR OMA; KRITEMM; -.
DR OrthoDB; 1485208at2759; -.
DR PhylomeDB; Q9LXR8; -.
DR PRO; PR:Q9LXR8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LXR8; baseline and differential.
DR Genevisible; Q9LXR8; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:TAIR.
DR GO; GO:0007031; P:peroxisome organization; IMP:TAIR.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Peroxisome; Peroxisome biogenesis; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..318
FT /note="Peroxisomal and mitochondrial division factor 1"
FT /id="PRO_0000432895"
FT TOPO_DOM 1..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22147290"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..318
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:22147290"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..260
FT /evidence="ECO:0000255"
FT COMPBIAS 20..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 224
FT /note="K -> E (in Ref. 4; AAM66096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 36595 MW; 86036D37B73A00BF CRC64;
MADVEDRAAK GISDYDQGGV KTTELERKIE DMENKNQELT RENRELKERL ERLTGEIEEM
KDVEAEMNQR FGEMEKEIEE YEEEKKALEA ISTRAVELET EVSNLHDDLI TSLNGVDKTA
EEVAELKKAL AEIVEKLEGC EKEAEGLRKD RAEVEKRVRD LERKIGVLEV REMEEKSKKL
RSEEEMREID DEKKREIEEL QKTVIVLNLE LVKNVEELKK WKSKKKLTEE ALSETQKREK
ELELKKDELL KKVEEGNKTV FALNERTMKP SNGVRDTNGG DQKGSLEAEY QWPVVAAGSV
GAAGLVAATF FVCYSKLR
