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Cell division protein FtsZ homolog 1, chloroplastic (AtFtsZ1) (AtFtsZ1-1) (Chloroplast FtsZ) (CpFtsZ) (Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 10) (Protein PLASTID MOVEMENT IMPAIRED4)

 FTSZ1_ARATH             Reviewed;         433 AA.
Q42545; Q9FLN6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
11-JUL-2002, sequence version 2.
25-APR-2018, entry version 139.
RecName: Full=Cell division protein FtsZ homolog 1, chloroplastic;
Short=AtFtsZ1;
Short=AtFtsZ1-1;
Short=Chloroplast FtsZ;
Short=CpFtsZ;
AltName: Full=Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 10;
AltName: Full=Protein PLASTID MOVEMENT IMPAIRED4;
Flags: Precursor;
Name=FTSZ1; Synonyms=ARC10, FTSZ1-1, PMI4;
OrderedLocusNames=At5g55280; ORFNames=MCO15.23;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=7637778; DOI=10.1038/376473b0;
Osteryoung K.W., Vierling E.;
"Conserved cell and organelle division.";
Nature 376:473-474(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV.
Sequence features of the regions of 1,456,315 bp covered by nineteen
physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION.
STRAIN=cv. Columbia;
PubMed=9836740; DOI=10.1105/tpc.10.12.1991;
Osteryoung K.W., Stokes K.D., Rutherford S.M., Percival A.L.,
Lee W.Y.;
"Chloroplast division in higher plants requires members of two
functionally divergent gene families with homology to bacterial
ftsZ.";
Plant Cell 10:1991-2004(1998).
[6]
FUNCTION, AND MUTAGENESIS OF GLY-366.
PubMed=10213777; DOI=10.1105/tpc.11.4.549;
Pyke K.A.;
"Plastid division and development.";
Plant Cell 11:549-556(1999).
[7]
FUNCTION.
PubMed=11115884; DOI=10.1104/pp.124.4.1668;
Stokes K.D., McAndrew R.S., Figueroa R., Vitha S., Osteryoung K.W.;
"Chloroplast division and morphology are differentially affected by
overexpression of FtsZ1 and FtsZ2 genes in Arabidopsis.";
Plant Physiol. 124:1668-1677(2000).
[8]
SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=11285278; DOI=10.1083/jcb.153.1.111;
Vitha S., McAndrew R.S., Osteryoung K.W.;
"FtsZ ring formation at the chloroplast division site in plants.";
J. Cell Biol. 153:111-120(2001).
[9]
SUBCELLULAR LOCATION, AND FUNCTION.
STRAIN=cv. Columbia;
PubMed=11743110; DOI=10.1104/pp.127.4.1656;
McAndrew R.S., Froehlich J.E., Vitha S., Stokes K.D., Osteryoung K.W.;
"Colocalization of plastid division proteins in the chloroplast
stromal compartment establishes a new functional relationship between
FtsZ1 and FtsZ2 in higher plants.";
Plant Physiol. 127:1656-1666(2001).
[10]
INTERACTION WITH FTSZ2-1, AND SELF-INTERACTION.
PubMed=16146521; DOI=10.1111/j.1365-313X.2005.02493.x;
Maple J., Aldridge C., Moeller S.G.;
"Plastid division is mediated by combinatorial assembly of plastid
division proteins.";
Plant J. 43:811-823(2005).
[11]
FUNCTION, AND MUTAGENESIS OF GLY-267.
PubMed=16113226; DOI=10.1104/pp.105.061887;
DeBlasio S.L., Luesse D.L., Hangarter R.P.;
"A plant-specific protein essential for blue-light-induced chloroplast
movements.";
Plant Physiol. 139:101-114(2005).
[12]
INTERACTION WITH ARC3.
PubMed=17304239; DOI=10.1038/sj.embor.7400902;
Maple J., Vojta L., Soll J., Moeller S.G.;
"ARC3 is a stromal Z-ring accessory protein essential for plastid
division.";
EMBO Rep. 8:293-299(2007).
[13]
FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-159; GLY-267;
ARG-298 AND GLY-366, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia, and cv. Wassilewskija-2;
PubMed=17468127; DOI=10.1093/pcp/pcm049;
Yoder D.W., Kadirjan-Kalbach D., Olson B.J.S.C., Miyagishima S.-Y.,
Deblasio S.L., Hangarter R.P., Osteryoung K.W.;
"Effects of mutations in Arabidopsis FtsZ1 on plastid division, FtsZ
ring formation and positioning, and FtsZ filament morphology in
vivo.";
Plant Cell Physiol. 48:775-791(2007).
[14]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
STRAIN=cv. Wassilewskija;
PubMed=17725544; DOI=10.1042/BJ20070543;
El-Kafafi E.-S., Karamoko M., Pignot-Paintrand I., Grunwald D.,
Mandaron P., Lerbs-Mache S., Falconet D.;
"Developmentally regulated association of plastid division protein
FtsZ1 with thylakoid membranes in Arabidopsis thaliana.";
Biochem. J. 409:87-94(2008).
[15]
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=18284374; DOI=10.1042/BJ20071354;
McAndrew R.S., Olson B.J., Kadirjan-Kalbach D.K., Chi-Ham C.L.,
Vitha S., Froehlich J.E., Osteryoung K.W.;
"In vivo quantitative relationship between plastid division proteins
FtsZ1 and FtsZ2 and identification of ARC6 and ARC3 in a native FtsZ
complex.";
Biochem. J. 412:367-378(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=18431481; DOI=10.1371/journal.pone.0001994;
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,
Sun Q., van Wijk K.J.;
"Sorting signals, N-terminal modifications and abundance of the
chloroplast proteome.";
PLoS ONE 3:E1994-E1994(2008).
[17]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=18204083; DOI=10.1093/pcp/pcn012;
Fujiwara M.T., Hashimoto H., Kazama Y., Abe T., Yoshida S., Sato N.,
Itoh R.D.;
"The assembly of the FtsZ ring at the mid-chloroplast division site
depends on a balance between the activities of AtMinE1 and
ARC11/AtMinD1.";
Plant Cell Physiol. 49:345-361(2008).
[18]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=19403522; DOI=10.1093/pcp/pcp063;
Fujiwara M.T., Sekine K., Yamamoto Y.Y., Abe T., Sato N., Itoh R.D.;
"Live imaging of chloroplast FtsZ1 filaments, rings, spirals, and
motile dot structures in the AtMinE1 mutant and overexpressor of
Arabidopsis thaliana.";
Plant Cell Physiol. 50:1116-1126(2009).
[19]
FUNCTION, AND SUBUNIT.
PubMed=19925792; DOI=10.1016/j.febslet.2009.11.044;
Smith A.G., Johnson C.B., Vitha S., Holzenburg A.;
"Plant FtsZ1 and FtsZ2 expressed in a eukaryotic host: GTPase activity
and self-assembly.";
FEBS Lett. 584:166-172(2010).
[20]
FUNCTION AS GTPASE, SUBUNIT, AND MUTAGENESIS OF ASP-275.
PubMed=20421292; DOI=10.1074/jbc.M110.122614;
Olson B.J.S.C., Wang Q., Osteryoung K.W.;
"GTP-dependent heteropolymer formation and bundling of chloroplast
FtsZ1 and FtsZ2.";
J. Biol. Chem. 285:20634-20643(2010).
[21]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND SUBUNIT.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=20195657; DOI=10.1007/s00709-010-0119-7;
Fujiwara M.T., Hashimoto H., Kazama Y., Hirano T., Yoshioka Y.,
Aoki S., Sato N., Itoh R.D., Abe T.;
"Dynamic morphologies of pollen plastids visualised by vegetative-
specific FtsZ1-GFP in Arabidopsis thaliana.";
Protoplasma 242:19-33(2010).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-67, CLEAVAGE OF TRANSIT
PEPTIDE [LARGE SCALE ANALYSIS] AFTER CYS-66, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Exhibits GTPase activity. Component of the plastid
division machinery that forms a contractile ring at the division
site. Required for plastid division in a dose-dependent manner.
Involved in blue light-induced chloroplast movements. May regulate
thylakoid development. {ECO:0000269|PubMed:10213777,
ECO:0000269|PubMed:11115884, ECO:0000269|PubMed:11743110,
ECO:0000269|PubMed:16113226, ECO:0000269|PubMed:17468127,
ECO:0000269|PubMed:17725544, ECO:0000269|PubMed:19925792,
ECO:0000269|PubMed:20421292, ECO:0000269|PubMed:9836740}.
-!- SUBUNIT: Aggregates to form a contractile ring-like structure.
This aggregation is regulated in midchloroplast stroma by MIND1
(repressor) and MINE1 (promoter). Self-interacts and binds to
FTSZ2-1 in heteropolymers to form two morphologically distinct
types of filaments, termed type-I (smooth filaments) and type-II
(rough filaments), in a GTP-dependent manner. Interacts with ARC3.
Part of a complex made of ARC3, ARC6, FTSZ1 and FTSZ2.
{ECO:0000269|PubMed:16146521, ECO:0000269|PubMed:17304239,
ECO:0000269|PubMed:18204083, ECO:0000269|PubMed:18284374,
ECO:0000269|PubMed:19403522, ECO:0000269|PubMed:19925792,
ECO:0000269|PubMed:20195657, ECO:0000269|PubMed:20421292}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-2131124, EBI-2131124;
Q9FIG9:ARC6; NbExp=2; IntAct=EBI-2131124, EBI-2000800;
Q9LXJ0:FTSZ2-2; NbExp=6; IntAct=EBI-2131124, EBI-2430270;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:18431481}. Plastid, chloroplast thylakoid
membrane {ECO:0000269|PubMed:18431481}; Peripheral membrane
protein. Note=Forms a contractile ring at the chloroplast midpoint
that coaligns with FTSZ2-1 rings.
-!- TISSUE SPECIFICITY: In pollen grain, restricted to plastids of
vegetative cells. Also present in pollen tubes plastids.
{ECO:0000269|PubMed:20195657}.
-!- DISRUPTION PHENOTYPE: Highly heterogeneous chloroplast population
with giant chloroplasts and some smaller. Impaired chloroplast
division, some green cells with one single big chloroplast.
Abnormal thylakoids. {ECO:0000269|PubMed:17468127,
ECO:0000269|PubMed:17725544}.
-!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U39877; AAA82068.1; -; mRNA.
EMBL; AB010071; BAB08597.1; -; Genomic_DNA.
EMBL; CP002688; AED96609.1; -; Genomic_DNA.
EMBL; AY034992; AAK59497.1; -; mRNA.
EMBL; AY113896; AAM44944.1; -; mRNA.
RefSeq; NP_200339.1; NM_124910.6.
UniGene; At.1538; -.
ProteinModelPortal; Q42545; -.
SMR; Q42545; -.
BioGrid; 20865; 5.
IntAct; Q42545; 5.
MINT; Q42545; -.
STRING; 3702.AT5G55280.1; -.
iPTMnet; Q42545; -.
PaxDb; Q42545; -.
PRIDE; Q42545; -.
EnsemblPlants; AT5G55280.1; AT5G55280.1; AT5G55280.
GeneID; 835621; -.
Gramene; AT5G55280.1; AT5G55280.1; AT5G55280.
KEGG; ath:AT5G55280; -.
Araport; AT5G55280; -.
TAIR; locus:2161610; AT5G55280.
eggNOG; ENOG410IEJ4; Eukaryota.
eggNOG; COG0206; LUCA.
HOGENOM; HOG000049094; -.
InParanoid; Q42545; -.
KO; K03531; -.
OMA; MRAVKGI; -.
OrthoDB; EOG09360HE6; -.
PhylomeDB; Q42545; -.
PRO; PR:Q42545; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q42545; baseline and differential.
Genevisible; Q42545; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0005874; C:microtubule; IEA:InterPro.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0010020; P:chloroplast fission; IMP:TAIR.
GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
GO; GO:0009902; P:chloroplast relocation; IMP:UniProtKB.
GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
GO; GO:0043572; P:plastid fission; IMP:TAIR.
GO; GO:0009637; P:response to blue light; IMP:UniProtKB.
CDD; cd02201; FtsZ_type1; 1.
Gene3D; 3.40.50.1440; -; 1.
HAMAP; MF_00909; FtsZ; 1.
InterPro; IPR000158; Cell_div_FtsZ.
InterPro; IPR020805; Cell_div_FtsZ_CS.
InterPro; IPR024757; FtsZ_C.
InterPro; IPR008280; Tub_FtsZ_C.
InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
InterPro; IPR017975; Tubulin_CS.
InterPro; IPR003008; Tubulin_FtsZ_GTPase.
Pfam; PF12327; FtsZ_C; 1.
Pfam; PF00091; Tubulin; 1.
PRINTS; PR00423; CELLDVISFTSZ.
SMART; SM00864; Tubulin; 1.
SMART; SM00865; Tubulin_C; 1.
SUPFAM; SSF52490; SSF52490; 1.
SUPFAM; SSF55307; SSF55307; 1.
TIGRFAMs; TIGR00065; ftsZ; 1.
PROSITE; PS01134; FTSZ_1; 1.
PROSITE; PS01135; FTSZ_2; 1.
1: Evidence at protein level;
Acetylation; Cell cycle; Chloroplast; Complete proteome; GTP-binding;
Membrane; Nucleotide-binding; Plastid; Reference proteome; Thylakoid;
Transit peptide.
TRANSIT 1 66 Chloroplast.
{ECO:0000244|PubMed:22223895}.
CHAIN 67 433 Cell division protein FtsZ homolog 1,
chloroplastic.
/FTId=PRO_0000010306.
NP_BIND 83 87 GTP. {ECO:0000250|UniProtKB:P0A029}.
NP_BIND 170 172 GTP. {ECO:0000250|UniProtKB:P0A029}.
BINDING 201 201 GTP. {ECO:0000250|UniProtKB:P0A029}.
BINDING 205 205 GTP. {ECO:0000250|UniProtKB:P0A029}.
BINDING 249 249 GTP. {ECO:0000250|UniProtKB:P0A029}.
MOD_RES 67 67 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
MUTAGEN 159 159 D->N: Forms long filaments with impaired
midplastidial localization, heterogeneous
chloroplast population, one greatly
enlarged with numerous smaller
chloroplasts per cell.
{ECO:0000269|PubMed:17468127}.
MUTAGEN 267 267 G->R: In pmi4; reduced accumulation with
impaired midplastidial localization in
rings and filaments, giant chloroplasts,
and altered chloroplast movements in
response to blue light.
{ECO:0000269|PubMed:16113226,
ECO:0000269|PubMed:17468127}.
MUTAGEN 275 275 D->A: Impaired GTPase activity.
{ECO:0000269|PubMed:20421292}.
MUTAGEN 298 298 R->Q: Reduced accumulation, heterogeneous
chloroplast population.
{ECO:0000269|PubMed:17468127}.
MUTAGEN 366 366 G->A: In arc10; forms long filaments,
heterogeneous chloroplast population, one
greatly enlarged with numerous smaller
chloroplasts per cell.
{ECO:0000269|PubMed:10213777,
ECO:0000269|PubMed:17468127}.
CONFLICT 115 115 S -> F (in Ref. 1; AAA82068).
{ECO:0000305}.
SEQUENCE 433 AA; 45565 MW; 82C942D597171EDB CRC64;
MAIIPLAQLN ELTISSSSSS FLTKSISSHS LHSSCICASS RISQFRGGFS KRRSDSTRSK
SMRLRCSFSP MESARIKVIG VGGGGNNAVN RMISSGLQSV DFYAINTDSQ ALLQSSAENP
LQIGELLTRG LGTGGNPLLG EQAAEESKDA IANALKGSDL VFITAGMGGG TGSGAAPVVA
QISKDAGYLT VGVVTYPFSF EGRKRSLQAL EAIEKLQKNV DTLIVIPNDR LLDIADEQTP
LQDAFLLADD VLRQGVQGIS DIITIPGLVN VDFADVKAVM KDSGTAMLGV GVSSSKNRAE
EAAEQATLAP LIGSSIQSAT GVVYNITGGK DITLQEVNRV SQVVTSLADP SANIIFGAVV
DDRYTGEIHV TIIATGFSQS FQKTLLTDPR AAKLLDKMGS SGQQENKGMS LPHQKQSPST
ISTKSSSPRR LFF


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