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PDV2_ARATH
ID   PDV2_ARATH              Reviewed;         307 AA.
AC   Q9XII1; Q93ZL0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Plastid division protein PDV2 {ECO:0000303|PubMed:16998069};
DE   AltName: Full=Protein PLASTID DIVISION2 {ECO:0000303|PubMed:16998069};
GN   Name=PDV2 {ECO:0000303|PubMed:16998069};
GN   Synonyms=PD116 {ECO:0000303|PubMed:27988788};
GN   OrderedLocusNames=At2g16070 {ECO:0000312|Araport:AT2G16070};
GN   ORFNames=F7H1.9 {ECO:0000312|EMBL:AAD26950.1};
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] (ISOFORM 1), FUNCTION, AND
RP   DISRUPTION PHENOTYPE.
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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] (ISOFORMS 1 AND 2).
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).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   FUNCTION, INTERACTION WITH ARC6, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF GLY-307.
RC   STRAIN=cv. Columbia;
RX   PubMed=18812496; DOI=10.1105/tpc.108.061440;
RA   Glynn J.M., Froehlich J.E., Osteryoung K.W.;
RT   "Arabidopsis ARC6 coordinates the division machineries of the inner and
RT   outer chloroplast membranes through interaction with PDV2 in the
RT   intermembrane space.";
RL   Plant Cell 20:2460-2470(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [8]
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   [9]
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   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [11]
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   [12]
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   [13]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=27988788; DOI=10.1007/s00299-016-2096-6;
RA   Chang N., Sun Q., Li Y., Mu Y., Hu J., Feng Y., Liu X., Gao H.;
RT   "PDV2 has a dosage effect on chloroplast division in Arabidopsis.";
RL   Plant Cell Rep. 36:471-480(2017).
RN   [14]
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   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 284-307 IN COMPLEX WITH ARC6,
RP   FUNCTION, MUTAGENESIS OF ARG-288, DISRUPTION PHENOTYPE, AND INTERACTION
RP   WITH ARC6.
RX   PubMed=28248291; DOI=10.1038/nplants.2017.11;
RA   Wang W., Li J., Sun Q., Yu X., Zhang W., Jia N., An C., Li Y., Dong Y.,
RA   Han F., Chang N., Liu X., Zhu Z., Yu Y., Fan S., Yang M., Luo S.-Z.,
RA   Gao H., Feng Y.;
RT   "Structural insights into the coordination of plastid division by the ARC6-
RT   PDV2 complex.";
RL   Nat. Plants 3:17011-17011(2017).
CC   -!- FUNCTION: Component of the plastid division machinery consisting in a
CC       binary fission accomplished by the simultaneous constriction of the
CC       FtsZ ring on the stromal side of the inner envelope membrane, and the
CC       ARC5/DRP5B ring on the cytosolic side of the outer envelope membrane
CC       (PubMed:28248291). Positive factor of chloroplast division required,
CC       with a dosage effect, to mediate the recruitment and dimerization of
CC       ARC5/DRP5B at the midplastid constriction site in the cytoplasm at
CC       plastid outer envelope membranes (OEMs) (PubMed:28248291,
CC       PubMed:27988788, PubMed:32005784). Prevents ARC5/DRP5B GTPase acrivity
CC       (PubMed:27988788). Relays plastid division site position between stroma
CC       and outer surface via interactions with the cytoplasmic ARC5/DRP5B and
CC       the inner membrane ARC6 that recruits stromal FtsZ ring
CC       (PubMed:28248291). Binding to phosphatidylinositol 4-phosphate (PI4P)
CC       modulates negatively chloroplast division (PubMed:25736058).
CC       {ECO:0000269|PubMed:16998069, ECO:0000269|PubMed:18812496,
CC       ECO:0000269|PubMed:25736058, ECO:0000269|PubMed:27988788,
CC       ECO:0000269|PubMed:28248291, ECO:0000269|PubMed:32005784}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with ARC6 (via C-terminus) in the
CC       chloroplast intermembrane space; this interaction induces ARC6
CC       homodimerization and leads to the formation of an heterotetramer
CC       containing two ARC6 and two PDV2 subunits (PubMed:18812496,
CC       PubMed:28248291). Interacts with ARC5/DRP5B (PubMed:32005784).
CC       {ECO:0000269|PubMed:18812496, ECO:0000269|PubMed:28248291,
CC       ECO:0000269|PubMed:32005784}.
CC   -!- INTERACTION:
CC       Q9XII1; Q9FIG9: ARC6; NbExp=3; IntAct=EBI-2000823, EBI-2000800;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC       {ECO:0000269|PubMed:18812496, ECO:0000269|PubMed:19453460,
CC       ECO:0000269|PubMed:32005784}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:18812496, ECO:0000269|PubMed:19453460}.
CC       Note=Plastid equatorial positioning in a discontinuous ring mediated by
CC       ARC6 (PubMed:18812496). Colocalizes with ARC5/DRP5B at the chloroplast
CC       division site (PubMed:32005784). {ECO:0000269|PubMed:18812496,
CC       ECO:0000269|PubMed:32005784}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9XII1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9XII1-2; Sequence=VSP_040897;
CC   -!- TISSUE SPECIFICITY: Mostly expressed in young leaves.
CC       {ECO:0000269|PubMed:27988788}.
CC   -!- DEVELOPMENTAL STAGE: Highest levels in young developing leaves with a
CC       sharp expression decrease in fast-growing and mature leaves (at protein
CC       level). {ECO:0000269|PubMed:27988788}.
CC   -!- INDUCTION: Slightly induced by gibberellic acid (GA).
CC       {ECO:0000269|PubMed:23020316}.
CC   -!- DISRUPTION PHENOTYPE: Reduced number of constricted and large
CC       chloroplasts (PubMed:16998069, PubMed:18812496). Attenuated PDV2-
CC       induced ARC6 dimerization in the chloroplast intermembrane space
CC       leading to an abnormal morphology of ARC6 rings thus compromizing
CC       plastidial division (PubMed:28248291). Altered localization of
CC       ARC5/DRP5B in cytosol only rather than at the constriction sites of
CC       enlarged chloroplasts (PubMed:32005784). In pd116, reduced number of
CC       dumbbell-shaped and large chloroplasts in mesophyll cells, with
CC       sometimes unique giant chloroplasts (PubMed:27988788).
CC       {ECO:0000269|PubMed:16998069, ECO:0000269|PubMed:18812496,
CC       ECO:0000269|PubMed:27988788, ECO:0000269|PubMed:28248291,
CC       ECO:0000269|PubMed:32005784}.
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DR   EMBL; AB252217; BAF36495.1; -; Genomic_DNA.
DR   EMBL; AB252219; BAF36497.1; -; mRNA.
DR   EMBL; AC007134; AAD26950.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06464.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06465.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62193.1; -; Genomic_DNA.
DR   EMBL; AY056812; AAL10503.1; -; mRNA.
DR   EMBL; AY080829; AAL87305.1; -; mRNA.
DR   EMBL; AY113976; AAM45024.1; -; mRNA.
DR   EMBL; AY088807; AAM67117.1; -; mRNA.
DR   PIR; D84536; D84536.
DR   RefSeq; NP_001324370.1; NM_001335463.1. [Q9XII1-2]
DR   RefSeq; NP_028242.1; NM_127166.4. [Q9XII1-1]
DR   RefSeq; NP_849959.1; NM_179628.4. [Q9XII1-2]
DR   PDB; 5GTB; X-ray; 2.87 A; B=284-307.
DR   PDBsum; 5GTB; -.
DR   AlphaFoldDB; Q9XII1; -.
DR   SMR; Q9XII1; -.
DR   BioGRID; 1463; 6.
DR   IntAct; Q9XII1; 3.
DR   STRING; 3702.AT2G16070.2; -.
DR   iPTMnet; Q9XII1; -.
DR   PaxDb; Q9XII1; -.
DR   PRIDE; Q9XII1; -.
DR   ProteomicsDB; 251401; -. [Q9XII1-1]
DR   EnsemblPlants; AT2G16070.1; AT2G16070.1; AT2G16070. [Q9XII1-2]
DR   EnsemblPlants; AT2G16070.2; AT2G16070.2; AT2G16070. [Q9XII1-1]
DR   EnsemblPlants; AT2G16070.3; AT2G16070.3; AT2G16070. [Q9XII1-2]
DR   GeneID; 816104; -.
DR   Gramene; AT2G16070.1; AT2G16070.1; AT2G16070. [Q9XII1-2]
DR   Gramene; AT2G16070.2; AT2G16070.2; AT2G16070. [Q9XII1-1]
DR   Gramene; AT2G16070.3; AT2G16070.3; AT2G16070. [Q9XII1-2]
DR   KEGG; ath:AT2G16070; -.
DR   Araport; AT2G16070; -.
DR   TAIR; locus:2052996; AT2G16070.
DR   eggNOG; ENOG502REYJ; Eukaryota.
DR   HOGENOM; CLU_075429_0_0_1; -.
DR   InParanoid; Q9XII1; -.
DR   OMA; ANHERSE; -.
DR   OrthoDB; 1188785at2759; -.
DR   PhylomeDB; Q9XII1; -.
DR   PRO; PR:Q9XII1; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9XII1; baseline and differential.
DR   Genevisible; Q9XII1; AT.
DR   GO; GO:0009707; C:chloroplast outer membrane; IDA:UniProtKB.
DR   GO; GO:0031359; C:integral component of chloroplast outer membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
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; Acetylation; Alternative splicing; Chloroplast; Coiled coil;
KW   Membrane; Phosphoprotein; Plastid; Plastid outer membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..307
FT                   /note="Plastid division protein PDV2"
FT                   /id="PRO_0000406944"
FT   TOPO_DOM        1..213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..307
FT                   /note="Chloroplast intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          28..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..307
FT                   /note="ARC6 binding"
FT                   /evidence="ECO:0000269|PubMed:18812496,
FT                   ECO:0000269|PubMed:28248291, ECO:0007744|PDB:5GTB"
FT   COILED          76..103
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        41..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19245862"
FT   VAR_SEQ         1..93
FT                   /note="MEDEEGIGLILARATELRLKISDCIDNSSTTVSDNGDGNEDLSPGEGRKSEI
FT                   IGNQDKDFDSISSEDVDEAEAERLLRIRDALEALESQLASL -> MWGWFLVCGE (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_040897"
FT   MUTAGEN         288
FT                   /note="R->K: In pdv2-4; impaired interaction with PDV2
FT                   leading to altered chloroplast division and fewer but
FT                   larger chloroplasts."
FT                   /evidence="ECO:0000269|PubMed:28248291"
FT   MUTAGEN         307
FT                   /note="G->D: Impaired ARC6 interaction, and reduced number
FT                   of constricted and large chloroplasts."
FT                   /evidence="ECO:0000269|PubMed:18812496"
FT   STRAND          289..291
FT                   /evidence="ECO:0007829|PDB:5GTB"
SQ   SEQUENCE   307 AA;  33641 MW;  F2EE488B3257303B CRC64;
     MEDEEGIGLI LARATELRLK ISDCIDNSST TVSDNGDGNE DLSPGEGRKS EIIGNQDKDF
     DSISSEDVDE AEAERLLRIR DALEALESQL ASLQNLRQRQ QYEKQLALSE IDYSRKMLLE
     KLKEYKGKDF EVLRETTTFA GERVDYENDL LLPPYPVHPP LSLGLDNNNG YLSHLPSKKK
     SDANGFGSGH VRNEAEAKSP NGGSGGSSHG VIRFLGSVAK IVLPIIGVIS LLSASGYGPE
     MRKRGASLNL FGLLPHRATR GKRTPNQCPP GKVLVIEDGE ARCLVKERVE IPFDSVVAKR
     DVTYGYG
 
 
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