MIND1_ARATH
ID MIND1_ARATH Reviewed; 326 AA.
AC Q9MBA2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Septum site-determining protein minD homolog, chloroplastic {ECO:0000303|PubMed:11148270};
DE Short=AtMinD1 {ECO:0000303|PubMed:11148270};
DE AltName: Full=Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 11 {ECO:0000303|PubMed:10417716};
DE AltName: Full=Septum site-determining protein MinD1 {ECO:0000303|PubMed:11148270};
DE Flags: Precursor;
GN Name=MIND1 {ECO:0000303|PubMed:11148270};
GN Synonyms=ARC11 {ECO:0000303|PubMed:10417716};
GN OrderedLocusNames=At5g24020 {ECO:0000312|Araport:AT5G24020};
GN ORFNames=MZF18.10 {ECO:0000312|EMBL:BAB08725.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION
RP BY SEED GERMINATION.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=11148270; DOI=10.1093/pcp/pcd037;
RA Kanamaru K., Fujiwara M., Kim M., Nagashima A., Nakazato E., Tanaka K.,
RA Takahashi H.;
RT "Chloroplast targeting, distribution and transcriptional fluctuation of
RT AtMinD1, a Eubacteria-type factor critical for chloroplast division.";
RL Plant Cell Physiol. 41:1119-1128(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(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].
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 FUNCTION, AND MUTAGENESIS OF ALA-296.
RX PubMed=10417716; DOI=10.1046/j.1365-313x.1999.00500.x;
RA Marrison J.L., Rutherford S.M., Robertson E.J., Lister C., Dean C.,
RA Leech R.M.;
RT "The distinctive roles of five different ARC genes in the chloroplast
RT division process in Arabidopsis.";
RL Plant J. 18:651-662(1999).
RN [6]
RP FUNCTION, MUTAGENESIS OF ALA-296, AND SUBCELLULAR LOCATION.
RX PubMed=10801439; DOI=10.1016/s0960-9822(00)00466-8;
RA Colletti K.S., Tattersall E.A., Pyke K.A., Froelich J.E., Stokes K.D.,
RA Osteryoung K.W.;
RT "A homologue of the bacterial cell division site-determining factor MinD
RT mediates placement of the chloroplast division apparatus.";
RL Curr. Biol. 10:507-516(2000).
RN [7]
RP FUNCTION.
RX PubMed=11800381; DOI=10.1007/s004250100605;
RA Dinkins R., Reddy M.S.S., Leng M., Collins G.B.;
RT "Overexpression of the Arabidopsis thaliana MinD1 gene alters chloroplast
RT size and number in transgenic tobacco plants.";
RL Planta 214:180-188(2001).
RN [8]
RP FUNCTION.
RX PubMed=12897262; DOI=10.1105/tpc.013292;
RA Vitha S., Froehlich J.E., Koksharova O., Pyke K.A., van Erp H.,
RA Osteryoung K.W.;
RT "ARC6 is a J-domain plastid division protein and an evolutionary descendant
RT of the cyanobacterial cell division protein Ftn2.";
RL Plant Cell 15:1918-1933(2003).
RN [9]
RP FUNCTION, MUTAGENESIS OF ALA-296, SUBCELLULAR LOCATION, AND
RP HOMODIMERIZATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=15126639; DOI=10.1242/jcs.01092;
RA Fujiwara M.T., Nakamura A., Itoh R., Shimada Y., Yoshida S., Moeller S.G.;
RT "Chloroplast division site placement requires dimerization of the
RT ARC11/AtMinD1 protein in Arabidopsis.";
RL J. Cell Sci. 117:2399-2410(2004).
RN [10]
RP FUNCTION AS CALCIUM-DEPENDENT ATPASE, MUTAGENESIS OF LYS-72,
RP HOMODIMERIZATION, INTERACTION WITH MINE1, SUBCELLULAR LOCATION, ACTIVITY
RP REGULATION BY MINE1, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16014621; DOI=10.1074/jbc.m505126200;
RA Aldridge C., Moeller S.G.;
RT "The plastid division protein AtMinD1 is a Ca2+-ATPase stimulated by
RT AtMinE1.";
RL J. Biol. Chem. 280:31673-31678(2005).
RN [11]
RP REVIEW.
RX PubMed=15753112; DOI=10.1093/jxb/eri118;
RA Aldridge C., Maple J., Moeller S.G.;
RT "The molecular biology of plastid division in higher plants.";
RL J. Exp. Bot. 56:1061-1077(2005).
RN [12]
RP HOMODIMERIZATION, INTERACTION WITH MINE1, AND SUBCELLULAR LOCATION.
RX PubMed=16146521; DOI=10.1111/j.1365-313x.2005.02493.x;
RA Maple J., Aldridge C., Moeller S.G.;
RT "Plastid division is mediated by combinatorial assembly of plastid division
RT proteins.";
RL Plant J. 43:811-823(2005).
RN [13]
RP INTERACTION WITH ARC3.
RC STRAIN=cv. Columbia;
RX PubMed=17304239; DOI=10.1038/sj.embor.7400902;
RA Maple J., Vojta L., Soll J., Moeller S.G.;
RT "ARC3 is a stromal Z-ring accessory protein essential for plastid
RT division.";
RL EMBO Rep. 8:293-299(2007).
RN [14]
RP INTERACTION WITH MINE1.
RX PubMed=17855384; DOI=10.1242/jcs.010215;
RA Maple J., Moeller S.G.;
RT "Interdependency of formation and localisation of the Min complex controls
RT symmetric plastid division.";
RL J. Cell Sci. 120:3446-3456(2007).
RN [15]
RP REVIEW.
RX PubMed=17451550; DOI=10.1111/j.1600-0854.2007.00545.x;
RA Glynn J.M., Miyagishima S.-Y., Yoder D.W., Osteryoung K.W., Vitha S.;
RT "Chloroplast division.";
RL Traffic 8:451-461(2007).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18204083; DOI=10.1093/pcp/pcn012;
RA Fujiwara M.T., Hashimoto H., Kazama Y., Abe T., Yoshida S., Sato N.,
RA Itoh R.D.;
RT "The assembly of the FtsZ ring at the mid-chloroplast division site depends
RT on a balance between the activities of AtMinE1 and ARC11/AtMinD1.";
RL Plant Cell Physiol. 49:345-361(2008).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ALA-296.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=19584524; DOI=10.1271/bbb.90309;
RA Fujiwara M.T., Li D., Kazama Y., Abe T., Uno T., Yamagata H., Kanamaru K.,
RA Itoh R.D.;
RT "Further evaluation of the localization and functionality of hemagglutinin
RT epitope- and fluorescent protein-tagged AtMinD1 in Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 73:1693-1697(2009).
RN [18]
RP FUNCTION IN E.COLI COMPLEMENTATION.
RX PubMed=19457228; DOI=10.1186/1471-2180-9-101;
RA Zhang M., Hu Y., Jia J., Gao H., He Y.;
RT "A plant MinD homologue rescues Escherichia coli HL1 mutant (DeltaMinDE) in
RT the absence of MinE.";
RL BMC Microbiol. 9:101-101(2009).
RN [19]
RP INTERACTION WITH MCD1.
RX PubMed=19135368; DOI=10.1016/j.cub.2008.12.018;
RA Nakanishi H., Suzuki K., Kabeya Y., Miyagishima S.Y.;
RT "Plant-specific protein MCD1 determines the site of chloroplast division in
RT concert with bacteria-derived MinD.";
RL Curr. Biol. 19:151-156(2009).
RN [20]
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 [21]
RP FUNCTION, MUTAGENESIS OF ALA-296, AND INTERACTION WITH CDP1/PARC6.
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 [22]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=29967285; DOI=10.1105/tpc.18.00189;
RA Chen L., Sun B., Gao W., Zhang Q.Y., Yuan H., Zhang M.;
RT "MCD1 associates with FtsZ filaments via the membrane-tethering protein
RT ARC6 to guide chloroplast division.";
RL Plant Cell 30:1807-1823(2018).
CC -!- FUNCTION: Together with ARC3 and MCD1, regulates FtsZ ring positioning
CC in chloroplasts in an ARC6-dependent manner (PubMed:29967285,
CC PubMed:28984364, PubMed:23936263). Calcium-dependent ATPase required
CC for the correct placement of the plastid division site. Inhibits FtsZ
CC filament and ring formation in the plastid. Mediates inhibition of
CC plastid division (PubMed:28984364). In cooperation with MINE1, prevents
CC FtsZ ring formation anywhere outside of the mid-plastids.
CC {ECO:0000269|PubMed:10417716, ECO:0000269|PubMed:10801439,
CC ECO:0000269|PubMed:11148270, ECO:0000269|PubMed:11800381,
CC ECO:0000269|PubMed:12897262, ECO:0000269|PubMed:15126639,
CC ECO:0000269|PubMed:16014621, ECO:0000269|PubMed:18204083,
CC ECO:0000269|PubMed:19457228, ECO:0000269|PubMed:19584524,
CC ECO:0000269|PubMed:23936263, ECO:0000269|PubMed:28984364,
CC ECO:0000269|PubMed:29967285}.
CC -!- ACTIVITY REGULATION: Stimulated ATPase activity by MINE1.
CC {ECO:0000269|PubMed:16014621}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=500 uM for ATP (at pH 7.4 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:16014621};
CC pH dependence:
CC Optimum pH is 7.5-8. Active from pH 7 to 9.
CC {ECO:0000269|PubMed:16014621};
CC -!- SUBUNIT: Homodimer (Probable). Interacts with MINE1 (PubMed:16014621,
CC PubMed:16146521, PubMed:17855384). Binds to ARC3 (PubMed:17304239).
CC Interacts with MCD1 (PubMed:19135368). Interacts with CDP1/PARC6
CC (PubMed:28984364). {ECO:0000269|PubMed:16014621,
CC ECO:0000269|PubMed:16146521, ECO:0000269|PubMed:17304239,
CC ECO:0000269|PubMed:17855384, ECO:0000269|PubMed:19135368,
CC ECO:0000269|PubMed:28984364, ECO:0000305}.
CC -!- INTERACTION:
CC Q9MBA2; Q9MBA2: MIND1; NbExp=6; IntAct=EBI-2119758, EBI-2119758;
CC Q9MBA2; Q9C4Z7: MINE1; NbExp=6; IntAct=EBI-2119758, EBI-2119860;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:10801439, ECO:0000269|PubMed:11148270,
CC ECO:0000269|PubMed:15126639, ECO:0000269|PubMed:16014621,
CC ECO:0000269|PubMed:16146521, ECO:0000269|PubMed:19584524}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10801439,
CC ECO:0000269|PubMed:11148270, ECO:0000269|PubMed:15126639,
CC ECO:0000269|PubMed:16014621, ECO:0000269|PubMed:16146521,
CC ECO:0000269|PubMed:19584524}. Note=Attached to membranes in punctate
CC structures dispersed on the inner envelope and at the mid-chloroplast
CC division site in an ATPase activity-dependent manner (PubMed:29967285).
CC Also present at the chloroplast to a ring structure at the constriction
CC site (PubMed:29967285). {ECO:0000269|PubMed:29967285}.
CC -!- INDUCTION: Accumulates during seed germination, at the beginning of
CC rapid greening. {ECO:0000269|PubMed:11148270}.
CC -!- DISRUPTION PHENOTYPE: Heterogeneous population of chloroplasts in
CC mesophyll cells and petals, with normal and larger plastids, due to
CC reduced chloroplast divisions and asymmetrically constricted
CC chloroplasts (PubMed:18204083, PubMed:23936263). Contains highly
CC elongated and multiple-arrayed chloroplasts in developing green tissues
CC (PubMed:18204083). Formation of some FtsZ rings that fail to initiate
CC or progress the membrane constriction of developing chloroplasts
CC (PubMed:18204083). Normal shape and number of etioplasts in cotyledons
CC (PubMed:23936263). {ECO:0000269|PubMed:18204083,
CC ECO:0000269|PubMed:23936263}.
CC -!- SIMILARITY: Belongs to the ParA family. MinD subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB030278; BAA90261.1; -; mRNA.
DR EMBL; AB009056; BAB08725.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93246.1; -; Genomic_DNA.
DR EMBL; BT002027; AAN72038.1; -; mRNA.
DR EMBL; BT008819; AAP68258.1; -; mRNA.
DR RefSeq; NP_197790.1; NM_122307.3.
DR AlphaFoldDB; Q9MBA2; -.
DR SMR; Q9MBA2; -.
DR BioGRID; 17742; 3.
DR IntAct; Q9MBA2; 2.
DR MINT; Q9MBA2; -.
DR STRING; 3702.AT5G24020.1; -.
DR MetOSite; Q9MBA2; -.
DR PaxDb; Q9MBA2; -.
DR PRIDE; Q9MBA2; -.
DR ProteomicsDB; 237051; -.
DR EnsemblPlants; AT5G24020.1; AT5G24020.1; AT5G24020.
DR GeneID; 832467; -.
DR Gramene; AT5G24020.1; AT5G24020.1; AT5G24020.
DR KEGG; ath:AT5G24020; -.
DR Araport; AT5G24020; -.
DR TAIR; locus:2178717; AT5G24020.
DR eggNOG; KOG3022; Eukaryota.
DR HOGENOM; CLU_037612_0_1_1; -.
DR InParanoid; Q9MBA2; -.
DR OMA; CESAKAY; -.
DR OrthoDB; 1295474at2759; -.
DR PhylomeDB; Q9MBA2; -.
DR PRO; PR:Q9MBA2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9MBA2; baseline and differential.
DR Genevisible; Q9MBA2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0030899; F:calcium-dependent ATPase activity; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0010020; P:chloroplast fission; IMP:UniProtKB.
DR GO; GO:0051782; P:negative regulation of cell division; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR010223; MinD.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01656; CbiA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01968; minD_bact; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Membrane; Nucleotide-binding; Plastid;
KW Plastid inner membrane; Reference proteome; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 63..326
FT /note="Septum site-determining protein minD homolog,
FT chloroplastic"
FT /id="PRO_0000406150"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q72H90"
FT MUTAGEN 72
FT /note="K->A: Impaired interaction with MINE1 and loss of
FT ATPase activity, but normal homodimerization."
FT /evidence="ECO:0000269|PubMed:16014621"
FT MUTAGEN 296
FT /note="A->G: In arc11; loss of homodimerization, abnormal
FT intraplastidic localization patterns, heterogeneous and
FT reduced population of chloroplasts in mesophyll cells and
FT petals, with normal and larger plastids, due to reduced
FT chloroplast divisions and asymmetrically constricted
FT chloroplasts, and highly elongated and multiple-arrayed
FT chloroplasts in developing green tissues."
FT /evidence="ECO:0000269|PubMed:10417716,
FT ECO:0000269|PubMed:10801439, ECO:0000269|PubMed:15126639,
FT ECO:0000269|PubMed:19584524, ECO:0000269|PubMed:28984364"
SQ SEQUENCE 326 AA; 35690 MW; BE7AEF4307167825 CRC64;
MASLRLFSTN HQSLLLPSSL SQKTLISSPR FVNNPSRRSP IRSVLQFNRK PELAGETPRI
VVITSGKGGV GKTTTTANVG LSLARYGFSV VAIDADLGLR NLDLLLGLEN RVNYTCVEVI
NGDCRLDQAL VRDKRWSNFE LLCISKPRSK LPMGFGGKAL EWLVDALKTR PEGSPDFIII
DCPAGIDAGF ITAITPANEA VLVTTPDITA LRDADRVTGL LECDGIRDIK MIVNRVRTDM
IKGEDMMSVL DVQEMLGLSL LGVIPEDSEV IRSTNRGFPL VLNKPPTLAG LAFEQAAWRL
VEQDSMKAVM VEEEPKKRGF FSFFGG