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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
 
 
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