PMI1_ARATH
ID PMI1_ARATH Reviewed; 843 AA.
AC Q9C8E6; C0Z238; Q8VY94; Q9C856;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Protein PLASTID MOVEMENT IMPAIRED 1 {ECO:0000303|PubMed:16113226};
GN Name=PMI1 {ECO:0000303|PubMed:16113226};
GN OrderedLocusNames=At1g42550 {ECO:0000312|Araport:AT1G42550};
GN ORFNames=F8D11.1 {ECO:0000312|EMBL:AAG51233.1},
GN T8D8.2 {ECO:0000312|EMBL:AAG51317.1};
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] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-843 (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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16113226; DOI=10.1104/pp.105.061887;
RA DeBlasio S.L., Luesse D.L., Hangarter R.P.;
RT "A plant-specific protein essential for blue-light-induced chloroplast
RT movements.";
RL Plant Physiol. 139:101-114(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-328; THR-404;
RP SER-407 AND THR-410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND REPRESSION BY OSMOTIC STRESS.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=25154696; DOI=10.1016/j.plaphy.2014.07.014;
RA Rojas-Pierce M., Whippo C.W., Davis P.A., Hangarter R.P., Springer P.S.;
RT "PLASTID MOVEMENT IMPAIRED1 mediates ABA sensitivity during germination and
RT implicates ABA in light-mediated Chloroplast movements.";
RL Plant Physiol. Biochem. 83:185-193(2014).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia GL1;
RX PubMed=26324877; DOI=10.1104/pp.15.00214;
RA Suetsugu N., Higa T., Kong S.-G., Wada M.;
RT "PLASTID MOVEMENT IMPAIRED1 and PLASTID MOVEMENT IMPAIRED1-RELATED1 mediate
RT photorelocation movements of both chloroplasts and nuclei.";
RL Plant Physiol. 169:1155-1167(2015).
CC -!- FUNCTION: Necessary for chloroplast and nuclear photorelocation
CC movements via the regulation of chloroplast-actin (cp-actin) filaments
CC in mesophyll cells, and together with PMIR1, in pavement cells
CC (PubMed:26324877). Required component for both the low- and high-light-
CC dependent chloroplast movement responses via an abscisic acid (ABA)
CC pathway (PubMed:16113226, PubMed:25154696). Involved in the ABA
CC response pathway during seed germination. Modulates ABA accumulation
CC during periods of water deficit at the seedling stage
CC (PubMed:25154696). {ECO:0000269|PubMed:16113226,
CC ECO:0000269|PubMed:25154696, ECO:0000269|PubMed:26324877}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26324877}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C8E6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C8E6-2; Sequence=VSP_058206;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, cauline leaves, and
CC flowers but not in roots (PubMed:16113226). Present in leaves in both
CC mesophyll and pavement cells (PubMed:26324877).
CC {ECO:0000269|PubMed:16113226, ECO:0000269|PubMed:26324877}.
CC -!- INDUCTION: Repressed by osmotic stress (300 mM mannitol).
CC {ECO:0000303|PubMed:25154696}.
CC -!- DISRUPTION PHENOTYPE: Severely attenuated chloroplast movements under
CC low- and high-light fluence, leading to evenly distributed chloroplasts
CC in leaf mesophyll in pmi1-1 (PubMed:16113226, PubMed:25154696). Severe
CC defects in both chloroplast and nuclear photorelocation movements
CC resulting from the impaired regulation of chloroplast-actin filaments
CC in pmi1-5 (PubMed:26324877). Reduced response to water-deficit and
CC abscisic acid (ABA) treatments. The mutants pmi1-3 and pmi1-4 are
CC hypersensitive to ABA during seed germination, but not pmi1-1, which is
CC hyposensitive. Chloroplasts of pmi1-3 have altered chloroplast
CC movements in low light (PubMed:25154696). {ECO:0000269|PubMed:16113226,
CC ECO:0000269|PubMed:25154696, ECO:0000269|PubMed:26324877}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL61948.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC025815; AAG51317.1; -; Genomic_DNA.
DR EMBL; AC035249; AAG51233.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31926.1; -; Genomic_DNA.
DR EMBL; AK318652; BAH56767.1; -; mRNA.
DR EMBL; AY072341; AAL61948.1; ALT_INIT; mRNA.
DR EMBL; BT010543; AAQ65166.1; -; mRNA.
DR PIR; D96495; D96495.
DR RefSeq; NP_174979.5; NM_103439.7. [Q9C8E6-1]
DR AlphaFoldDB; Q9C8E6; -.
DR STRING; 3702.AT1G42550.1; -.
DR iPTMnet; Q9C8E6; -.
DR PaxDb; Q9C8E6; -.
DR PRIDE; Q9C8E6; -.
DR ProteomicsDB; 234888; -. [Q9C8E6-1]
DR EnsemblPlants; AT1G42550.1; AT1G42550.1; AT1G42550. [Q9C8E6-1]
DR GeneID; 840860; -.
DR Gramene; AT1G42550.1; AT1G42550.1; AT1G42550. [Q9C8E6-1]
DR KEGG; ath:AT1G42550; -.
DR Araport; AT1G42550; -.
DR TAIR; locus:2036645; AT1G42550.
DR eggNOG; ENOG502QSA1; Eukaryota.
DR HOGENOM; CLU_003931_1_0_1; -.
DR InParanoid; Q9C8E6; -.
DR OMA; SRSEAWT; -.
DR OrthoDB; 182698at2759; -.
DR PhylomeDB; Q9C8E6; -.
DR PRO; PR:Q9C8E6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8E6; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:1902265; P:abscisic acid homeostasis; IMP:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0030048; P:actin filament-based movement; IMP:UniProtKB.
DR GO; GO:0009903; P:chloroplast avoidance movement; IMP:UniProtKB.
DR GO; GO:0009902; P:chloroplast relocation; IMP:UniProtKB.
DR GO; GO:0031022; P:nuclear migration along microfilament; IMP:TAIR.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0010029; P:regulation of seed germination; IMP:UniProtKB.
DR GO; GO:0009637; P:response to blue light; IMP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; TAS:UniProtKB.
DR InterPro; IPR019448; NT-C2.
DR InterPro; IPR033343; PMI1.
DR InterPro; IPR039614; PMI1-like.
DR PANTHER; PTHR33414; PTHR33414; 1.
DR PANTHER; PTHR33414:SF2; PTHR33414:SF2; 1.
DR Pfam; PF10358; NT-C2; 1.
DR PROSITE; PS51840; C2_NT; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Cytoplasm;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..843
FT /note="Protein PLASTID MOVEMENT IMPAIRED 1"
FT /id="PRO_0000435990"
FT DOMAIN 131..284
FT /note="C2 NT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01186"
FT REGION 30..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..398
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 404
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 410
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:19245862"
FT VAR_SEQ 660..780
FT /note="Missing (in isoform 2)"
FT /id="VSP_058206"
SQ SEQUENCE 843 AA; 93875 MW; 9DB3E10DDDF90F59 CRC64;
MAGEYSGSRS SNTQLLAELE ALSENLYQKP QVSVGNRRTN SLALPRSSVP SLVTSADEVS
TARAEDLTVS KPRARRLSLS PWRSRPKLEV EEEENVTQSN RIVKKPEESS SGSGVKEEKK
GIWNWKPIRG LVRIGMQKLS CLLSVEVVAA QNLPASMNGL RLGVCVRKKE TKDGAVQTMP
CRVSQGSADF EETLFIKCHV YYSPANGKGS PAKFEARPFL FYLFAVDAKE LEFGRHVVDL
SELIQESVEK MNYEGARVRQ WDMNWGLSGK AKGGELALKL GFQIMEKDGG AGIYSKQGEF
GMKPSSKPKN FANSFGRKQS KTSFSVPSPK MTSRSEAWTP ASGVESVSDF HGMEHLNLDE
PEEKPEEKPV QKNDKPEQRA EDDQEEPDFE VVDKGVEFDD DLETEKSDGT IGERSVEMKE
QHVNVDDPRH IMRLTELDSI AKQIKALESM MKDESDGGDG ETESQRLDEE EQTVTKEFLQ
LLEDEETEKL KFYQHKMDIS ELRSGESVDD ESENYLSDLG KGIGCVVQTR DGGYLVSMNP
FDTVVMRKDT PKLVMQISKQ IVVLPEAGPA TGFELFHRMA GSGEELESKI SSLMAIDELM
GKTGEQVAFE GIASAIIQGR NKERANTSAA RTVAAVKTMA NAMSSGRRER IMTGIWNVEE
NPLTSAEEVL AVSLQKLEEM VVEGLKIQAD MVDDEAPFEV SAAKGQKNPL ESTIPLEEWQ
KEHRTQQKLT VLATVQLRDP TRRYEAVGGT VVVAVQAEEE EEKGLKVGSL HIGGVKKDAA
EKRRLTAAQW LVEHGMGKKG KKKSNIKKKE KEEEEEEMLW SLSSRVMADM WLKSIRNPDV
KLH
