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PMD2_ARATH
ID   PMD2_ARATH              Reviewed;         323 AA.
AC   Q9SHJ6; A6XH03;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Peroxisomal and mitochondrial division factor 2 {ECO:0000303|PubMed:22147290};
DE   AltName: Full=Ubiquitin-interacting factor 7 {ECO:0000303|Ref.3};
GN   Name=PMD2 {ECO:0000303|PubMed:22147290}; Synonyms=UBI7 {ECO:0000303|Ref.3};
GN   OrderedLocusNames=At1g06530 {ECO:0000312|Araport:AT1G06530};
GN   ORFNames=F12K11.14 {ECO:0000312|EMBL:AAF24824.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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 [MRNA] OF 75-200.
RA   Fu H.;
RT   "Functional differentiation of ubiquitin-interacting factors from
RT   Arabidopsis.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [5]
RP   FUNCTION, SUBUNIT, INTERACTION WITH PMD1, AND SUBCELLULAR LOCATION.
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 mitochondria.
CC       Does not act redundantly with PMD1. Is not involved in peroxisomal
CC       proliferation. {ECO:0000269|PubMed:22147290}.
CC   -!- SUBUNIT: Homodimer. Interacts with PMD1. {ECO:0000269|PubMed:22147290}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:21896887, ECO:0000269|PubMed:22147290}; Single-pass
CC       membrane protein {ECO:0000255}.
CC   -!- MISCELLANEOUS: Plant cells silencing PMD2 show enlarged mitochondria.
CC       {ECO:0000269|PubMed:22147290}.
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DR   EMBL; AC007592; AAF24824.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28002.1; -; Genomic_DNA.
DR   EMBL; DQ785480; ABH03547.1; -; mRNA.
DR   RefSeq; NP_172140.1; NM_100532.3.
DR   AlphaFoldDB; Q9SHJ6; -.
DR   SMR; Q9SHJ6; -.
DR   STRING; 3702.AT1G06530.1; -.
DR   iPTMnet; Q9SHJ6; -.
DR   PaxDb; Q9SHJ6; -.
DR   PRIDE; Q9SHJ6; -.
DR   ProteomicsDB; 234688; -.
DR   EnsemblPlants; AT1G06530.1; AT1G06530.1; AT1G06530.
DR   GeneID; 837164; -.
DR   Gramene; AT1G06530.1; AT1G06530.1; AT1G06530.
DR   KEGG; ath:AT1G06530; -.
DR   Araport; AT1G06530; -.
DR   TAIR; locus:2009215; AT1G06530.
DR   eggNOG; ENOG502RY0Y; Eukaryota.
DR   HOGENOM; CLU_074678_0_0_1; -.
DR   InParanoid; Q9SHJ6; -.
DR   OMA; FYDADQT; -.
DR   OrthoDB; 1532887at2759; -.
DR   PhylomeDB; Q9SHJ6; -.
DR   PRO; PR:Q9SHJ6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SHJ6; differential.
DR   Genevisible; Q9SHJ6; AT.
DR   GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:TAIR.
PE   1: Evidence at protein level;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..323
FT                   /note="Peroxisomal and mitochondrial division factor 2"
FT                   /id="PRO_0000432896"
FT   TOPO_DOM        1..297
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LXR8"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..323
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LXR8"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          28..278
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   323 AA;  36119 MW;  8E956C7B9985E077 CRC64;
     MAEERSLNGE ATGQDDESFF DSDQQGDDGK STELNQKIGD LESQNQELAR DNDAINRKIE
     SLTAEIEELR GAESKAKRKM GEMEREIDKS DEERKVLEAI ASRASELETE VARLQHELIT
     ARTEGEEATA EAEKLRSEIS QKGGGIEELE KEVAGLRTVK EENEKRMKEL ESKLGALEVK
     ELDEKNKKFR AEEEMREKID NKEKEVHDLK EKIKSLESDV AKGKTELQKW ITEKMVVEDS
     LKDSEKKVVA LESEIVELQK QLDDAEKMIN GLKNVVEEPL NGIEFKSWSP NVTAVGSGGA
     VAAVAVAVAG AAVVCYIYHS RRV
 
 
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