MCD1_ARATH
ID MCD1_ARATH Reviewed; 349 AA.
AC Q8GWA7; Q9LM68;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Protein MULTIPLE CHLOROPLAST DIVISION SITE 1 {ECO:0000303|PubMed:19135368};
DE Flags: Precursor;
GN Name=MCD1 {ECO:0000303|PubMed:19135368};
GN OrderedLocusNames=At1g20830 {ECO:0000312|Araport:AT1G20830};
GN ORFNames=F2D10.35 {ECO:0000312|EMBL:AAF80625.1};
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=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 [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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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, INTERACTION WITH MIND1, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP DISRUPTION PHENOTYPE.
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 [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, DISRUPTION PHENOTYPE, TOPOLOGY, INTERACTION WITH ARC6 AND
RP FTSZ2-1, 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: Required for chloroplast division (PubMed:29967285,
CC PubMed:23936263). Together with MIND1 and ARC3, regulates FtsZ ring
CC positioning in chloroplasts in an ARC6-dependent manner
CC (PubMed:29967285). Determines the site of chloroplast division in
CC concert with MIND1 (PubMed:29967285). Not directly involved in ring
CC formation, but required for MIND1 and MINE1 localization to regulate
CC FtsZ ring formation during plastidial constriction (PubMed:29967285).
CC {ECO:0000269|PubMed:23936263, ECO:0000269|PubMed:29967285}.
CC -!- SUBUNIT: Interacts with MIND1 (PubMed:19135368). Interacts with ARC6 in
CC the chloroplast stroma and binds to FtsZ2-1 in an ARC6-dependent manner
CC (PubMed:29967285). {ECO:0000269|PubMed:19135368,
CC ECO:0000269|PubMed:29967285}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:19135368}; Single-pass membrane protein
CC {ECO:0000255}. Note=Localizes at the chloroplast to a ring structure at
CC the constriction site and on the punctate structures of the envelope
CC membrane throughout the chloroplast division.
CC {ECO:0000269|PubMed:19135368, ECO:0000269|PubMed:29967285}.
CC -!- DISRUPTION PHENOTYPE: Heterogeneous population of chloroplasts with
CC variable size and multiple division sites (PubMed:19135368,
CC PubMed:23936263). Abnormal subplastidial localization of the key
CC plastid division proteins FTSZ1 forming multiple rings
CC (PubMed:29967285). Normal shape and number of etioplasts in cotyledons
CC (PubMed:23936263). The double mutant mcd1 arc6 exhibits similar
CC chloroplast defect than the single mutant arc6, including the abnormal
CC localization of FTSZ1 to short filaments and dots within chloroplasts
CC (PubMed:29967285). {ECO:0000269|PubMed:19135368,
CC ECO:0000269|PubMed:23936263, ECO:0000269|PubMed:29967285}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF80625.1; Type=Erroneous gene model prediction; Evidence={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; AC069251; AAF80625.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30029.1; -; Genomic_DNA.
DR EMBL; AK118972; BAC43549.1; -; mRNA.
DR EMBL; BT006034; AAP04021.1; -; mRNA.
DR PIR; G86340; G86340.
DR RefSeq; NP_173507.1; NM_101936.3.
DR AlphaFoldDB; Q8GWA7; -.
DR STRING; 3702.AT1G20830.1; -.
DR PaxDb; Q8GWA7; -.
DR PRIDE; Q8GWA7; -.
DR ProteomicsDB; 238284; -.
DR EnsemblPlants; AT1G20830.1; AT1G20830.1; AT1G20830.
DR GeneID; 838675; -.
DR Gramene; AT1G20830.1; AT1G20830.1; AT1G20830.
DR KEGG; ath:AT1G20830; -.
DR Araport; AT1G20830; -.
DR TAIR; locus:2030512; AT1G20830.
DR eggNOG; ENOG502QVE8; Eukaryota.
DR HOGENOM; CLU_063546_0_0_1; -.
DR InParanoid; Q8GWA7; -.
DR OrthoDB; 1133815at2759; -.
DR PhylomeDB; Q8GWA7; -.
DR PRO; PR:Q8GWA7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GWA7; baseline and differential.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:UniProtKB.
DR GO; GO:0031972; C:chloroplast intermembrane space; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0010020; P:chloroplast fission; IMP:TAIR.
DR InterPro; IPR034572; MCD1.
DR PANTHER; PTHR36317; PTHR36317; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Plastid inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..349
FT /note="Protein MULTIPLE CHLOROPLAST DIVISION SITE 1"
FT /id="PRO_0000435851"
FT TOPO_DOM 53..116
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305|PubMed:19135368,
FT ECO:0000305|PubMed:29967285"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..349
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:19135368,
FT ECO:0000305|PubMed:29967285"
FT REGION 315..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 39416 MW; 72F331FD5E12D974 CRC64;
MASIDSLQFH SLCNLQSSIG RAKLQNPSSL VIFRRRPVNL NWVQFETKGS FVCKAIGDSS
TPDEDIQNTQ SDDNVVVVTA TTQSDIPHDS EYSISRFRSM VTTLPPVVFL MKKCSVNSIW
IGVCITATVL VAAIRAYVVR KSRDNQRAGS VADLVRRGQL RSGDRRGISK SLNYEDPFNN
PFVKLDKGSS TVEMCGKVYR LAPVTLTEKE QTIHQKRRSR AYQWKRPTIF LKEGDSIPPD
VDPDTVRWIP ANHPFATTVS DIDQDLAQNN VYQKQGVPFR IRAEHEAMQK KLEALQNEEK
LNNLSIDSQN ARDFQRPYKF SAKLEGENIQ KNSQENHTGN SSSEETHKS
