CDP1_ARATH
ID CDP1_ARATH Reviewed; 819 AA.
AC Q8VY16; Q2V3U5; Q9LJL2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Plastid division protein CDP1, chloroplastic {ECO:0000303|PubMed:19564892};
DE AltName: Full=ARC6-homolog protein;
DE AltName: Full=Protein CHLOROPLAST DIVISION SITE POSITIONING 1 {ECO:0000303|PubMed:19564892};
DE Short=AtCDP1 {ECO:0000303|PubMed:19564892};
DE AltName: Full=Protein PARALOG OF ARC6 {ECO:0000303|PubMed:19453460};
DE AltName: Full=Protein STROMULE BIOGENESIS ALTERED 2 {ECO:0000303|PubMed:28984364};
DE Flags: Precursor;
GN Name=CDP1 {ECO:0000303|PubMed:19564892};
GN Synonyms=ARC6H, PARC6 {ECO:0000303|PubMed:19453460},
GN SUBA2 {ECO:0000303|PubMed:28984364};
GN OrderedLocusNames=At3g19180 {ECO:0000312|Araport:AT3G19180};
GN ORFNames=MVI11.9 {ECO:0000312|EMBL:BAB02958.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ARC3, SELF-INTERACTION,
RP AND TISSUE SPECIFICITY.
RX PubMed=19564892; DOI=10.1038/cr.2009.78;
RA Zhang M., Hu Y., Jia J., Li D., Zhang R., Gao H., He Y.;
RT "CDP1, a novel component of chloroplast division site positioning system in
RT Arabidopsis.";
RL Cell Res. 19:877-886(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-112, SUBCELLULAR
RP LOCATION, TOPOLOGY, AND INTERACTION WITH ARC3.
RC STRAIN=cv. Columbia;
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=23936263; DOI=10.1371/journal.pone.0071190;
RA Wang P., Zhang J., Su J., Wang P., Liu J., Liu B., Feng D., Wang J.,
RA Wang H.;
RT "The chloroplast min system functions differentially in two specific
RT nongreen plastids in Arabidopsis thaliana.";
RL PLoS ONE 8:e71190-e71190(2013).
RN [7]
RP FUNCTION, INTERACTION WITH ARC3; PDV1 AND FTSZ2, AND TOPOLOGY.
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, AND INTERACTION WITH MIND1;
RP FTSZ2-1 AND FTSZ2-2.
RC STRAIN=cv. Columbia;
RX PubMed=28984364; DOI=10.1111/ppl.12648;
RA Itoh R.D., Ishikawa H., Nakajima K.P., Moriyama S., Fujiwara M.T.;
RT "Isolation and analysis of a stromule-overproducing Arabidopsis mutant
RT suggest the role of PARC6 in plastid morphology maintenance in the leaf
RT epidermis.";
RL Physiol. Plantarum 162:479-494(2018).
RN [9]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=30824505; DOI=10.1105/tpc.18.00948;
RA Chen C., Cao L., Yang Y., Porter K.J., Osteryoung K.W.;
RT "ARC3 activation by PARC6 promotes FtsZ-ring remodeling at the chloroplast
RT division site.";
RL Plant Cell 31:862-885(2019).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 596-819.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) OF 640-819.
RA Feng Y., Liu Z.;
RT "Structure of PARC6 from Arabidopsis.";
RL Submitted (MAY-2019) to the PDB data bank.
CC -!- FUNCTION: Component of the plastid division machinery required for PDV1
CC localization to constriction sites. Involved in chloroplast division
CC site placement (PubMed:28984364, PubMed:23936263). Required for the
CC proper formation of FtsZ rings at the division site in nongreen
CC plastids (e.g. etioplasts) (PubMed:23936263). Inhibits FtsZ assembly,
CC functioning as an antagonistic regulator of FtsZ dynamics against ARC6,
CC by recruiting ARC3 to the middle of the plastid to facilitates its
CC interaction with FtsZ proteins (PubMed:26527658, PubMed:30824505).
CC Required during stromule biogenesis in the leaf epidermis, especially
CC in non-mesophyll cells plastids (PubMed:28984364).
CC {ECO:0000269|PubMed:19453460, ECO:0000269|PubMed:19564892,
CC ECO:0000269|PubMed:23936263, ECO:0000269|PubMed:26527658,
CC ECO:0000269|PubMed:28984364, ECO:0000269|PubMed:30824505}.
CC -!- SUBUNIT: Self-interacts (PubMed:19564892, PubMed:28984364). Interacts
CC (via N-terminus) with ARC3 (via MORN domains) (PubMed:19453460,
CC PubMed:19564892, PubMed:26527658). Binds (via N-terminus) to FTSZ2
CC proteins, FTSZ2-1 and FTSZ2-2 (PubMed:26527658, PubMed:28984364,
CC PubMed:30824505). Recruited ARC3 to the middle of the plastid where
CC subsequent complex made of CDP1/PARC6, ARC3 and FtsZ proteins can form;
CC this complex enhances the dynamics of Z rings during chloroplast
CC division (PubMed:30824505). Interacts (via C-terminus) with PDV1 (via
CC C-terminus) (PubMed:26527658). Interacts with MIND1 (PubMed:28984364).
CC {ECO:0000269|PubMed:19453460, ECO:0000269|PubMed:19564892,
CC ECO:0000269|PubMed:26527658, ECO:0000269|PubMed:28984364,
CC ECO:0000269|PubMed:30824505}.
CC -!- INTERACTION:
CC Q8VY16; Q6F6B5: ARC3; NbExp=4; IntAct=EBI-2349234, EBI-2367605;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:19453460}; Single-pass membrane protein
CC {ECO:0000269|PubMed:19453460}. Note=Localizes both to the mid-plastid
CC and to a single spot at one pole. {ECO:0000269|PubMed:19453460}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VY16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VY16-2; Sequence=VSP_040894;
CC -!- TISSUE SPECIFICITY: Exclusively expressed in young green tissues such
CC as young cotyledons, shoot apex, emerging leaves and budding
CC inflorescence. {ECO:0000269|PubMed:19564892}.
CC -!- DISRUPTION PHENOTYPE: Defects of chloroplast and FtsZ filament
CC morphology (e.g. long FtsZ filaments formed by multiple rings or
CC spirals); elongated chloroplasts with multiple division sites
CC (PubMed:19453460, PubMed:19564892, PubMed:23936263). Aberrant stromule
CC biogenesis in the leaf epidermis associated with giant and pleomorphic
CC amoeboid chloroplasts, typically having one or more constrictions as
CC well as one or more extremely long stromules (PubMed:28984364). Reduced
CC number of enlarged etioplasts in cotyledons associated with the
CC formation of multiple FtsZ-rings (PubMed:23936263).
CC {ECO:0000269|PubMed:19453460, ECO:0000269|PubMed:19564892,
CC ECO:0000269|PubMed:23936263, ECO:0000269|PubMed:28984364}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02958.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000419; BAB02958.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76203.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76204.1; -; Genomic_DNA.
DR EMBL; AY074283; AAL66980.1; -; mRNA.
DR RefSeq; NP_001030725.1; NM_001035648.1. [Q8VY16-2]
DR RefSeq; NP_188549.2; NM_112805.5. [Q8VY16-1]
DR PDB; 5U9L; X-ray; 2.52 A; A/B=596-819.
DR PDB; 5U9O; X-ray; 3.37 A; A/B/C/D/E/F/G/H=684-819.
DR PDB; 6JZF; X-ray; 2.53 A; A/B=640-819.
DR PDB; 6JZN; X-ray; 2.89 A; A/B/C/D=685-819.
DR PDBsum; 5U9L; -.
DR PDBsum; 5U9O; -.
DR PDBsum; 6JZF; -.
DR PDBsum; 6JZN; -.
DR AlphaFoldDB; Q8VY16; -.
DR SMR; Q8VY16; -.
DR BioGRID; 6785; 4.
DR IntAct; Q8VY16; 1.
DR STRING; 3702.AT3G19180.1; -.
DR iPTMnet; Q8VY16; -.
DR PaxDb; Q8VY16; -.
DR PRIDE; Q8VY16; -.
DR ProteomicsDB; 224471; -. [Q8VY16-1]
DR EnsemblPlants; AT3G19180.1; AT3G19180.1; AT3G19180. [Q8VY16-1]
DR EnsemblPlants; AT3G19180.2; AT3G19180.2; AT3G19180. [Q8VY16-2]
DR GeneID; 821452; -.
DR Gramene; AT3G19180.1; AT3G19180.1; AT3G19180. [Q8VY16-1]
DR Gramene; AT3G19180.2; AT3G19180.2; AT3G19180. [Q8VY16-2]
DR KEGG; ath:AT3G19180; -.
DR Araport; AT3G19180; -.
DR TAIR; locus:2094143; AT3G19180.
DR eggNOG; ENOG502QT67; Eukaryota.
DR HOGENOM; CLU_017942_1_0_1; -.
DR InParanoid; Q8VY16; -.
DR OMA; SWRFCEG; -.
DR PhylomeDB; Q8VY16; -.
DR PRO; PR:Q8VY16; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VY16; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009528; C:plastid inner membrane; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0010020; P:chloroplast fission; IDA:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
DR GO; GO:0043572; P:plastid fission; IMP:TAIR.
DR InterPro; IPR044685; ARC6-like.
DR InterPro; IPR025344; ARC6-like_IMS.
DR PANTHER; PTHR33925; PTHR33925; 1.
DR Pfam; PF13355; ARC6-like_IMS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Coiled coil; Membrane;
KW Plastid; Plastid inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..76
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 77..819
FT /note="Plastid division protein CDP1, chloroplastic"
FT /id="PRO_0000406912"
FT TOPO_DOM 77..572
FT /note="Stromal"
FT /evidence="ECO:0000269|PubMed:26527658"
FT TRANSMEM 573..593
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:26527658"
FT TOPO_DOM 594..819
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000269|PubMed:26527658"
FT COILED 419..439
FT /evidence="ECO:0000255"
FT COILED 762..782
FT /evidence="ECO:0000255"
FT VAR_SEQ 729..819
FT /note="WQTLAQTAEAKSCYWRFVLLHLEVLQAHIFEDGIAGEAAEIEALLEEAAELV
FT DESQPKNAKYYSTYKIRYILKKQEDGLWKFCQSDIQIQK -> VTVSIHLLLFLYLIML
FT VYYS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040894"
FT MUTAGEN 112
FT /note="D->N: In parc6-2; reduced number of heterogeneous
FT chloroplasts."
FT /evidence="ECO:0000269|PubMed:19453460"
FT CONFLICT 268
FT /note="E -> G (in Ref. 3; AAL66980)"
FT /evidence="ECO:0000305"
FT HELIX 646..656
FT /evidence="ECO:0007829|PDB:5U9L"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:5U9L"
FT HELIX 690..707
FT /evidence="ECO:0007829|PDB:5U9L"
FT HELIX 717..720
FT /evidence="ECO:0007829|PDB:5U9L"
FT HELIX 723..738
FT /evidence="ECO:0007829|PDB:5U9L"
FT STRAND 742..759
FT /evidence="ECO:0007829|PDB:5U9L"
FT STRAND 761..763
FT /evidence="ECO:0007829|PDB:5U9L"
FT STRAND 765..780
FT /evidence="ECO:0007829|PDB:5U9L"
FT STRAND 784..786
FT /evidence="ECO:0007829|PDB:6JZF"
FT STRAND 788..802
FT /evidence="ECO:0007829|PDB:5U9L"
FT STRAND 804..817
FT /evidence="ECO:0007829|PDB:5U9L"
SQ SEQUENCE 819 AA; 90823 MW; A3F6FB34A264657E CRC64;
MPVAYTFPVL PSSCLLCGIS NRSTSFVVDR PELQISGLLV VRSESGEFFG SGLSLRRFQR
EGRRRLNAAG GGIHVVDNAP SRTSSLAAST STIELPVTCY QLIGVSEQAE KDEVVKSVIN
LKKTDAEEGY TMEAAAARQD LLMDVRDKLL FESEYAGNLK EKIAPKSPLR IPWAWLPGAL
CLLQEVGQEK LVLDIGRAAL RNLDSKPYIH DIFLSMALAE CAIAKAAFEV NKVSQGFEAL
ARAQSFLKSK VTLGKLALLT QIEESLEELA PPCTLDLLGL PRTPENAERR RGAIAALREL
LRQGLSVEAS CQIQDWPCFL SQAISRLLAT EIVDLLPWDD LAITRKNKKS LESHNQRVVI
DFNCFYMVLL GHIAVGFSGK QNETINKAKT ICECLIASEG VDLKFEEAFC SFLLKQGSEA
EALEKLKQLE SNSDSAVRNS ILGKESRSTS ATPSLEAWLM ESVLANFPDT RGCSPSLANF
FRAEKKYPEN KKMGSPSIMN HKTNQRPLST TQFVNSSQHL YTAVEQLTPT DLQSPVVSAK
NNDETSASMP SVQLKRNLGV HKNKIWDEWL SQSSLIGRVS VVALLGCTVF FSLKLSGIRS
GRLQSMPISV SARPHSESDS FLWKTESGNF RKNLDSVNRN GIVGNIKVLI DMLKMHCGEH
PDALYLKSSG QSATSLSHSA SELHKRPMDT EEAEELVRQW ENVKAEALGP THQVYSLSEV
LDESMLVQWQ TLAQTAEAKS CYWRFVLLHL EVLQAHIFED GIAGEAAEIE ALLEEAAELV
DESQPKNAKY YSTYKIRYIL KKQEDGLWKF CQSDIQIQK
