MINE1_ARATH
ID MINE1_ARATH Reviewed; 229 AA.
AC Q9C4Z7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cell division topological specificity factor homolog, chloroplastic {ECO:0000303|PubMed:11743109};
DE Short=AtMinE1 {ECO:0000303|PubMed:11743109};
DE AltName: Full=Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 12 {ECO:0000303|PubMed:15753112, ECO:0000303|PubMed:29967285};
DE Flags: Precursor;
GN Name=MINE1 {ECO:0000303|PubMed:11743109};
GN Synonyms=ARC12 {ECO:0000303|PubMed:15753112, ECO:0000303|PubMed:29967285};
GN OrderedLocusNames=At1g69390 {ECO:0000312|Araport:AT1G69390};
GN ORFNames=F10D13.22 {ECO:0000312|EMBL:AAG60109.1},
GN F23O10.25 {ECO:0000312|EMBL:AAG52489.1};
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 TISSUE
RP SPECIFICITY.
RX PubMed=11743109; DOI=10.1104/pp.010386;
RA Itoh R., Fujiwara M., Nagata N., Yoshida S.;
RT "A chloroplast protein homologous to the eubacterial topological
RT specificity factor minE plays a role in chloroplast division.";
RL Plant Physiol. 127:1644-1655(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12029464; DOI=10.1007/s00425-001-0728-7;
RA Reddy M.S., Dinkins R., Collins G.B.;
RT "Overexpression of the Arabidopsis thaliana MinE1 bacterial division
RT inhibitor homologue gene alters chloroplast size and morphology in
RT transgenic Arabidopsis and tobacco plants.";
RL Planta 215:167-176(2002).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12164807; DOI=10.1046/j.1365-313x.2002.01358.x;
RA Maple J., Chua N.-H., Moeller S.G.;
RT "The topological specificity factor AtMinE1 is essential for correct
RT plastid division site placement in Arabidopsis.";
RL Plant J. 31:269-277(2002).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=11975738; DOI=10.1034/j.1399-3054.2002.1140417.x;
RA Yamamoto K., Pyke K.A., Kiss J.Z.;
RT "Reduced gravitropism in inflorescence stems and hypocotyls, but not roots,
RT of Arabidopsis mutants with large plastids.";
RL Physiol. Plantarum 114:627-636(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH MIND1.
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 [10]
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 [11]
RP HOMODIMERIZATION, INTERACTION WITH MIND1, 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 [12]
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 [13]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH MIND1, MUTAGENESIS OF ALA-124;
RP ILE-126; ALA-127; LYS-128; GLN-129; ARG-130; LEU-131; LYS-132; ILE-134;
RP LEU-135; ASP-138 AND ARG-139, AND SUBCELLULAR LOCATION.
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 [14]
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 [15]
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 [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19966487; DOI=10.1271/bbb.90473;
RA Kojo K.H., Fujiwara M.T., Itoh R.D.;
RT "Involvement of AtMinE1 in plastid morphogenesis in various tissues of
RT Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 73:2632-2639(2009).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19403522; DOI=10.1093/pcp/pcp063;
RA Fujiwara M.T., Sekine K., Yamamoto Y.Y., Abe T., Sato N., Itoh R.D.;
RT "Live imaging of chloroplast FtsZ1 filaments, rings, spirals, and motile
RT dot structures in the AtMinE1 mutant and overexpressor of Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 50:1116-1126(2009).
RN [18]
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 [19]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=26500667; DOI=10.3389/fpls.2015.00823;
RA Fujiwara M.T., Kojo K.H., Kazama Y., Sasaki S., Abe T., Itoh R.D.;
RT "The Arabidopsis minE mutation causes new plastid and FtsZ1 localization
RT phenotypes in the leaf epidermis.";
RL Front. Plant Sci. 6:823-823(2015).
RN [20]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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: Acts as a topological specificity factor during plastid
CC division and specify plastid constriction sites (such as the Z-ring) in
CC a MCD1-dependent manner (PubMed:29967285, PubMed:23936263). Especially
CC involved in epidermal plastids division in a FTSZ1-dependent manner
CC (PubMed:26500667). Required for the proper formation of FtsZ rings at
CC the division site in nongreen plastids (e.g. etioplasts)
CC (PubMed:23936263). May contribute to gravitropism in stems and
CC hypocotyls. Stimulates MIND1 ATPase activity. In cooperation with
CC MIND1, prevents FtsZ ring formation anywhere outside of the mid-
CC plastids. {ECO:0000269|PubMed:11743109, ECO:0000269|PubMed:11975738,
CC ECO:0000269|PubMed:12029464, ECO:0000269|PubMed:12164807,
CC ECO:0000269|PubMed:16014621, ECO:0000269|PubMed:17855384,
CC ECO:0000269|PubMed:18204083, ECO:0000269|PubMed:19403522,
CC ECO:0000269|PubMed:19966487, ECO:0000269|PubMed:23936263,
CC ECO:0000269|PubMed:26500667, ECO:0000269|PubMed:29967285}.
CC -!- SUBUNIT: Homodimer. Interacts with MIND1. These interactions are
CC required for proper intraplastidic localization. Binds to ARC3.
CC {ECO:0000269|PubMed:16014621, ECO:0000269|PubMed:16146521,
CC ECO:0000269|PubMed:17304239, ECO:0000269|PubMed:17855384}.
CC -!- INTERACTION:
CC Q9C4Z7; Q6F6B5: ARC3; NbExp=3; IntAct=EBI-2119860, EBI-2367605;
CC Q9C4Z7; Q9MBA2: MIND1; NbExp=6; IntAct=EBI-2119860, EBI-2119758;
CC Q9C4Z7; Q9C4Z7: MINE1; NbExp=3; IntAct=EBI-2119860, EBI-2119860;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11743109, ECO:0000269|PubMed:12029464,
CC ECO:0000269|PubMed:12164807, ECO:0000269|PubMed:16146521,
CC ECO:0000269|PubMed:17855384, ECO:0000269|PubMed:26500667}. Note=Dynamic
CC protein that is restricted to a single spot at one end of chloroplasts
CC or as two spots in close proximity normally towards one end of the
CC chloroplast. Seems attached to membranes.
CC -!- TISSUE SPECIFICITY: Expressed in green tissues, especially at the shoot
CC apex. Also present in leaves, stems, buds, and flowers, especially in
CC sepals, siliques (tip and base), and anthers (mostly in pollen grains).
CC {ECO:0000269|PubMed:11743109, ECO:0000269|PubMed:12029464}.
CC -!- DISRUPTION PHENOTYPE: Only one or two large plastids (all type of
CC plastid) in each plastid containing cells (PubMed:23936263). Impaired
CC gravitropism of inflorescence stems and hypocotyls, but not of roots.
CC Wide variation in size and shape of epidermal plastids, occasionally
CC displaying grape-like morphology, associated with a disturbed
CC localization of FTSZ1 ring (PubMed:26500667). Severe inhibition of
CC plastid division, producing motile disorganized dots and short
CC filaments of FtsZ (PubMed:29967285). Reduced number of enlarged
CC etioplasts in cotyledons associated with fragmented FtsZ filaments
CC (PubMed:23936263). Altered localization of MCD1 and MinD1 in puncta on
CC the envelope membranes of giant chloroplasts (PubMed:29967285). The
CC mcd1 arc12 double mutant contains a heterogeneous population of
CC chloroplasts, including some with multiple membrane constrictions
CC associated with an organization of FtsZ1 in multiple rings similar to
CC those observed in mcd1 single mutants (PubMed:29967285).
CC {ECO:0000269|PubMed:11975738, ECO:0000269|PubMed:18204083,
CC ECO:0000269|PubMed:19403522, ECO:0000269|PubMed:19966487,
CC ECO:0000269|PubMed:23936263, ECO:0000269|PubMed:26500667,
CC ECO:0000269|PubMed:29967285}.
CC -!- SIMILARITY: Belongs to the MinE family. {ECO:0000305}.
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DR EMBL; AB046117; BAB79236.1; -; mRNA.
DR EMBL; AC018364; AAG52489.1; -; Genomic_DNA.
DR EMBL; AC073178; AAG60109.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34918.1; -; Genomic_DNA.
DR EMBL; BT002897; AAO22713.1; -; mRNA.
DR EMBL; BT004467; AAO42461.1; -; mRNA.
DR EMBL; AY088828; AAM67135.1; -; mRNA.
DR RefSeq; NP_564964.1; NM_105606.4.
DR AlphaFoldDB; Q9C4Z7; -.
DR BioGRID; 28492; 2.
DR IntAct; Q9C4Z7; 2.
DR MINT; Q9C4Z7; -.
DR STRING; 3702.AT1G69390.1; -.
DR PaxDb; Q9C4Z7; -.
DR PRIDE; Q9C4Z7; -.
DR ProteomicsDB; 250701; -.
DR EnsemblPlants; AT1G69390.1; AT1G69390.1; AT1G69390.
DR GeneID; 843271; -.
DR Gramene; AT1G69390.1; AT1G69390.1; AT1G69390.
DR KEGG; ath:AT1G69390; -.
DR Araport; AT1G69390; -.
DR TAIR; locus:2007171; AT1G69390.
DR eggNOG; ENOG502QVF0; Eukaryota.
DR HOGENOM; CLU_104395_0_0_1; -.
DR InParanoid; Q9C4Z7; -.
DR OMA; ARNTGDY; -.
DR OrthoDB; 1363584at2759; -.
DR PhylomeDB; Q9C4Z7; -.
DR PRO; PR:Q9C4Z7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C4Z7; baseline and differential.
DR Genevisible; Q9C4Z7; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0010020; P:chloroplast fission; IMP:UniProtKB.
DR GO; GO:0032955; P:regulation of division septum assembly; IEA:InterPro.
DR Gene3D; 3.30.1070.10; -; 1.
DR InterPro; IPR005527; MinE.
DR InterPro; IPR036707; MinE_sf.
DR PANTHER; PTHR33404; PTHR33404; 1.
DR Pfam; PF03776; MinE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 31..229
FT /note="Cell division topological specificity factor
FT homolog, chloroplastic"
FT /id="PRO_0000406149"
FT REGION 35..141
FT /note="Interaction with MIND1"
FT REGION 142..169
FT /note="Homodimerization"
FT MUTAGEN 124
FT /note="A->R: Normal interaction with MIND1."
FT /evidence="ECO:0000269|PubMed:17855384"
FT MUTAGEN 126
FT /note="I->R: Normal interaction with MIND1."
FT /evidence="ECO:0000269|PubMed:17855384"
FT MUTAGEN 127
FT /note="A->T: Normal interaction with MIND1."
FT /evidence="ECO:0000269|PubMed:17855384"
FT MUTAGEN 128
FT /note="K->A: Normal interaction with MIND1."
FT /evidence="ECO:0000269|PubMed:17855384"
FT MUTAGEN 129
FT /note="Q->A: Normal interaction with MIND1."
FT /evidence="ECO:0000269|PubMed:17855384"
FT MUTAGEN 130
FT /note="R->A: Normal interaction with MIND1."
FT /evidence="ECO:0000269|PubMed:17855384"
FT MUTAGEN 131
FT /note="L->R: Abolished interaction with MIND1; when
FT associated with R-134."
FT /evidence="ECO:0000269|PubMed:17855384"
FT MUTAGEN 132
FT /note="K->R: Normal interaction with MIND1."
FT /evidence="ECO:0000269|PubMed:17855384"
FT MUTAGEN 134
FT /note="I->R: Abolished interaction with MIND1; when
FT associated with R-131."
FT /evidence="ECO:0000269|PubMed:17855384"
FT MUTAGEN 135
FT /note="L->E: Abolished interaction with MIND1."
FT /evidence="ECO:0000269|PubMed:17855384"
FT MUTAGEN 138
FT /note="D->I: Abolished interaction with MIND1."
FT /evidence="ECO:0000269|PubMed:17855384"
FT MUTAGEN 139
FT /note="R->A,K: Normal interaction with MIND1."
FT /evidence="ECO:0000269|PubMed:17855384"
SQ SEQUENCE 229 AA; 25748 MW; FC307A9E3C4DE123 CRC64;
MAMSSGTLRI SATLVSPYHH HHRNRLSLPS SSSKVDFTGF ISNGVNSLET QKCTPGLAIS
RENTRGQVKV LARNTGDYEL SPSPAEQEIE SFLYNAINMG FFDRLNLAWK IIFPSHASRR
SSNARIAKQR LKMILFSDRC DVSDEAKRKI VNNIIHALSD FVEIESEEKV QLNVSTDGDL
GTIYSVTVPV RRVKPEYQDV DEAGTITNVE YKDTRDGSVD VRFDFYVPE
