PDV1_ARATH
ID PDV1_ARATH Reviewed; 272 AA.
AC Q9FK13; Q8LBC3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Plastid division protein PDV1 {ECO:0000303|PubMed:16998069};
DE AltName: Full=Protein PLASTID DIVISION1 {ECO:0000303|PubMed:16998069};
GN Name=PDV1 {ECO:0000303|PubMed:16998069};
GN OrderedLocusNames=At5g53280 {ECO:0000312|Araport:AT5G53280};
GN ORFNames=K19E1.8 {ECO:0000312|EMBL:BAB09790.1};
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 [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP MUTAGENESIS OF GLY-272, TOPOLOGY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16998069; DOI=10.1105/tpc.106.045484;
RA Miyagishima S.-Y., Froehlich J.E., Osteryoung K.W.;
RT "PDV1 and PDV2 mediate recruitment of the dynamin-related protein ARC5 to
RT the plastid division site.";
RL Plant Cell 18:2517-2530(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19453460; DOI=10.1111/j.1365-313x.2009.03905.x;
RA Glynn J.M., Yang Y., Vitha S., Schmitz A.J., Hemmes M., Miyagishima S.-Y.,
RA Osteryoung K.W.;
RT "PARC6, a novel chloroplast division factor, influences FtsZ assembly and
RT is required for recruitment of PDV1 during chloroplast division in
RT Arabidopsis.";
RL Plant J. 59:700-711(2009).
RN [8]
RP INDUCTION BY GIBBERELLIC ACID.
RX PubMed=23020316; DOI=10.1111/j.1365-313x.2012.05118.x;
RA Jiang X., Li H., Wang T., Peng C., Wang H., Wu H., Wang X.;
RT "Gibberellin indirectly promotes chloroplast biogenesis as a means to
RT maintain the chloroplast population of expanded cells.";
RL Plant J. 72:768-780(2012).
RN [9]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=25736058; DOI=10.1105/tpc.115.136234;
RA Okazaki K., Miyagishima S.-Y., Wada H.;
RT "Phosphatidylinositol 4-phosphate negatively regulates chloroplast division
RT in Arabidopsis.";
RL Plant Cell 27:663-674(2015).
RN [10]
RP MUTAGENESIS OF GLY-272, AND INTERACTION WITH CDP1/PARC6.
RC STRAIN=cv. Columbia;
RX PubMed=26527658; DOI=10.1104/pp.15.01460;
RA Zhang M., Chen C., Froehlich J.E., TerBush A.D., Osteryoung K.W.;
RT "Roles of Arabidopsis PARC6 in Coordination of the Chloroplast Division
RT Complex and Negative Regulation of FtsZ Assembly.";
RL Plant Physiol. 170:250-262(2016).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP ARC5/DRP5B.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=32005784; DOI=10.1104/pp.19.01490;
RA Sun B., Zhang Q.-Y., Yuan H., Gao W., Han B., Zhang M.;
RT "PDV1 and PDV2 differentially affect remodeling and assembly of the
RT chloroplast DRP5B ring.";
RL Plant Physiol. 182:1966-1978(2020).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.37 ANGSTROMS) OF 248-272.
RA Delmar J.A., Yu E.W., Osteryoung K.W.;
RT "Cocrystal structure of the intermembrane space region of the plastid
RT division proteins PARC6 and PDV1.";
RL Submitted (DEC-2016) to the PDB data bank.
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 263-272.
RA Feng Y., Liu Z.;
RT "Structure of PARC6 and PDV1 complex from Arabidopsis thaliana.";
RL Submitted (MAY-2019) to the PDB data bank.
CC -!- FUNCTION: Component of the plastid division machinery
CC (PubMed:16998069). Required to mediate the dissociation of ARC5/DRP5B
CC from plastid outer envelope membranes (OEMs) at the midplastid
CC constriction site in the cytoplasm, thus triggering ARC5/DRP5B ring
CC turnover at the chloroplast division site (PubMed:16998069,
CC PubMed:32005784). Binding to phosphatidylinositol 4-phosphate (PI4P)
CC modulates negatively chloroplast division (PubMed:25736058).
CC {ECO:0000269|PubMed:16998069, ECO:0000269|PubMed:25736058,
CC ECO:0000269|PubMed:32005784}.
CC -!- SUBUNIT: Interacts (via C-terminus) with CDP1/PARC6 (via C-terminus)
CC (PubMed:26527658). Interacts with ARC5/DRP5B (PubMed:32005784).
CC {ECO:0000269|PubMed:26527658, ECO:0000269|PubMed:32005784}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:16998069, ECO:0000269|PubMed:19453460,
CC ECO:0000269|PubMed:32005784}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16998069, ECO:0000269|PubMed:19453460}.
CC Note=Plastid equatorial positioning in a discontinuous ring mediated by
CC CDP1 (PubMed:16998069, PubMed:19453460). Colocalizes with ARC5/DRP5B at
CC the chloroplast division site (PubMed:32005784).
CC {ECO:0000269|PubMed:16998069, ECO:0000269|PubMed:19453460,
CC ECO:0000269|PubMed:32005784}.
CC -!- TISSUE SPECIFICITY: Expressed in young developing leaves, root tips,
CC shoot apices, and flower buds (sepals, petals, stamens, and pistils),
CC but not in developed tissues. {ECO:0000269|PubMed:16998069}.
CC -!- INDUCTION: Induced by gibberellic acid (GA).
CC {ECO:0000269|PubMed:23020316}.
CC -!- DISRUPTION PHENOTYPE: Reduced number of constricted and large
CC chloroplasts due to a blocked plastid division (PubMed:16998069,
CC PubMed:32005784). Accumulation of ARC5/DRP5B in the plastid outer
CC envelope membranes (OEMs) at the midplastid constriction site in the
CC cytoplasm (PubMed:32005784). {ECO:0000269|PubMed:16998069,
CC ECO:0000269|PubMed:32005784}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM64850.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB252216; BAF36494.1; -; Genomic_DNA.
DR EMBL; AB252218; BAF36496.1; -; mRNA.
DR EMBL; AB013388; BAB09790.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96332.1; -; Genomic_DNA.
DR EMBL; AY087298; AAM64850.1; ALT_INIT; mRNA.
DR EMBL; AK221634; BAD95268.1; -; mRNA.
DR EMBL; BT024498; ABD19679.1; -; mRNA.
DR RefSeq; NP_200140.1; NM_124707.4.
DR PDB; 5U9O; X-ray; 3.37 A; A/B/C/D/E/F/G/H=248-272.
DR PDB; 6JZN; X-ray; 2.89 A; E/F/G/H=263-272.
DR PDBsum; 5U9O; -.
DR PDBsum; 6JZN; -.
DR AlphaFoldDB; Q9FK13; -.
DR SMR; Q9FK13; -.
DR BioGRID; 20654; 4.
DR IntAct; Q9FK13; 1.
DR STRING; 3702.AT5G53280.1; -.
DR iPTMnet; Q9FK13; -.
DR PaxDb; Q9FK13; -.
DR PRIDE; Q9FK13; -.
DR ProteomicsDB; 251215; -.
DR DNASU; 835409; -.
DR EnsemblPlants; AT5G53280.1; AT5G53280.1; AT5G53280.
DR GeneID; 835409; -.
DR Gramene; AT5G53280.1; AT5G53280.1; AT5G53280.
DR KEGG; ath:AT5G53280; -.
DR Araport; AT5G53280; -.
DR TAIR; locus:2154262; AT5G53280.
DR eggNOG; ENOG502R53V; Eukaryota.
DR HOGENOM; CLU_054471_0_0_1; -.
DR InParanoid; Q9FK13; -.
DR OMA; DHMGGIL; -.
DR OrthoDB; 1358663at2759; -.
DR PhylomeDB; Q9FK13; -.
DR PRO; PR:Q9FK13; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK13; baseline and differential.
DR Genevisible; Q9FK13; AT.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0010020; P:chloroplast fission; IMP:UniProtKB.
DR GO; GO:0009739; P:response to gibberellin; IEP:UniProtKB.
DR InterPro; IPR038939; PDV1/PDV2.
DR PANTHER; PTHR33600; PTHR33600; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Coiled coil; Membrane; Plastid;
KW Plastid outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..272
FT /note="Plastid division protein PDV1"
FT /id="PRO_0000406943"
FT TOPO_DOM 1..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..272
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000255"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 78..102
FT /evidence="ECO:0000255"
FT COMPBIAS 40..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 272
FT /note="G->D: In pdv1-2; reduced number of constricted and
FT large chloroplasts, impaired subchloroplastic localization
FT to the division site in the plastid outermembrane. Impaired
FT interaction with CDP1/PARC6."
FT /evidence="ECO:0000269|PubMed:16998069,
FT ECO:0000269|PubMed:26527658"
FT CONFLICT 154
FT /note="N -> T (in Ref. 4; AAM64850)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..181
FT /note="IPDGIE -> TPYGIK (in Ref. 4; AAM64850)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="A -> S (in Ref. 4; AAM64850)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="A -> T (in Ref. 4; AAM64850)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="A -> G (in Ref. 4; AAM64850)"
FT /evidence="ECO:0000305"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:6JZN"
SQ SEQUENCE 272 AA; 30675 MW; D6EA6676B3DB9CFE CRC64;
MGEMEIEEIE AVLEKIWDLH DKLSDEIHLI SKSHFLKSVK PSNRSEKRKN PHGNSGEDKR
PGYVFIKGFA VDDNDSTIQE AKSLNAIRTA LENLEDQLEF FHTIHTQQRT EKDVAIARLE
QSRILLAMRL AEHHGKNYGV LEEALAFVGS IKSNSHYVSP DHLYDSSRNP DGANSIPDGI
ESNFVINAFA STFGFAKRAL GFNHVKGVLG NAAIFAISVV AMLHLHQVAT SEHHLQKKED
RFYRSQQRKT YGRDKSSADR SLDHLDVMMA RG
