ELM1_ARATH
ID ELM1_ARATH Reviewed; 427 AA.
AC Q93YN4; Q9FMR7;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Mitochondrial fission protein ELM1;
DE AltName: Full=Protein ELONGATED MITOCHONDRIA 1;
GN Name=ELM1; OrderedLocusNames=At5g22350; ORFNames=MWD9.14;
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], FUNCTION, INTERACTION WITH DRP3A AND DRP3B,
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-241;
RP GLY-333 AND SER-352.
RX PubMed=18559960; DOI=10.1105/tpc.108.058578;
RA Arimura S., Fujimoto M., Doniwa Y., Kadoya N., Nakazono M., Sakamoto W.,
RA Tsutsumi N.;
RT "Arabidopsis ELONGATED MITOCHONDRIA1 is required for localization of
RT DYNAMIN-RELATED PROTEIN3A to mitochondrial fission sites.";
RL Plant Cell 20:1555-1566(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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].
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).
CC -!- FUNCTION: Plant-specific factor involved in mitochondria fission. Is
CC required for the correct localization of DRP3A from the cytosol to
CC mitochondrial fission sites. Does not seem to be required for
CC peroxisomal division. {ECO:0000269|PubMed:18559960}.
CC -!- SUBUNIT: Interacts with DRP3 and DRP3B. {ECO:0000269|PubMed:18559960}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000305|PubMed:18559960}; Peripheral membrane protein
CC {ECO:0000305|PubMed:18559960}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant growth and early bolting. Elongated
CC mitochondria and reduction of the number of mitochondria per cell.
CC {ECO:0000269|PubMed:18559960}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08333.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB379589; BAG66280.1; -; mRNA.
DR EMBL; AB007651; BAB08333.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93015.1; -; Genomic_DNA.
DR EMBL; AY059915; AAL24397.1; -; mRNA.
DR EMBL; AY128808; AAM91208.1; -; mRNA.
DR RefSeq; NP_568417.1; NM_122140.4.
DR AlphaFoldDB; Q93YN4; -.
DR STRING; 3702.AT5G22350.1; -.
DR PaxDb; Q93YN4; -.
DR PRIDE; Q93YN4; -.
DR ProteomicsDB; 222262; -.
DR EnsemblPlants; AT5G22350.1; AT5G22350.1; AT5G22350.
DR GeneID; 832295; -.
DR Gramene; AT5G22350.1; AT5G22350.1; AT5G22350.
DR KEGG; ath:AT5G22350; -.
DR Araport; AT5G22350; -.
DR TAIR; locus:2176332; AT5G22350.
DR eggNOG; ENOG502QSHX; Eukaryota.
DR HOGENOM; CLU_048241_2_0_1; -.
DR InParanoid; Q93YN4; -.
DR OMA; YIWNGQE; -.
DR OrthoDB; 1217183at2759; -.
DR PhylomeDB; Q93YN4; -.
DR PRO; PR:Q93YN4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93YN4; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:TAIR.
DR GO; GO:0000266; P:mitochondrial fission; IMP:TAIR.
DR GO; GO:0033365; P:protein localization to organelle; IMP:TAIR.
DR InterPro; IPR009367; Elm1-like.
DR PANTHER; PTHR33986; PTHR33986; 1.
DR Pfam; PF06258; Mito_fiss_Elm1; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome.
FT CHAIN 1..427
FT /note="Mitochondrial fission protein ELM1"
FT /id="PRO_0000422806"
FT MUTAGEN 241
FT /note="R->C: In elm1-2; intermediate mutant phenotype."
FT /evidence="ECO:0000269|PubMed:18559960"
FT MUTAGEN 333
FT /note="G->N: In elm1-3; intermediate mutant phenotype."
FT /evidence="ECO:0000269|PubMed:18559960"
FT MUTAGEN 352
FT /note="S->N: In elm1-5; weak mutant phenotype."
FT /evidence="ECO:0000269|PubMed:18559960"
SQ SEQUENCE 427 AA; 47605 MW; 3A81A179A1BF21C6 CRC64;
MRPILLPDPP SLSTGVPDIF EQGGSHNVVR RAVVIGNGFP GSENQCIGLV RALGLSDNHL
LYRVTRPKGG LNEWLHWLPV GFHKKLDFIL RHIYLYSRLM LGSKQSKYIS SVPSENGGNV
GLASILEADV KGIVNLARQT YEKDGPLIVI ACGRDTISIA SSIRRLASEN VFVVQIQHPR
SHLNRFDMVI TPRHDYYPLT LEAQEQVPRF MRSWITPREP PQDHVVLTTG ALHQIDYASL
RKAASAWHDE FAALPKPLVV VNIGWPRSNC RYGADLAKQL TDSLLNVLAT CGSVRITLSY
KTPAKVSRVI FKELGDNPKV YIWNGQEPNP YMGHLAWGDA FVVTADSVSL ISEACSTGKP
VYVVGADHCK WKIAEFQKSL RERGVVRSFT GFEDMSESWS YPPLNDTAEA ATRIRRELAA
RGWSLRS