MSL3_ARATH
ID MSL3_ARATH Reviewed; 678 AA.
AC Q8L7W1; Q9C6R0; Q9C731;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Mechanosensitive ion channel protein 3, chloroplastic;
DE AltName: Full=Mechanosensitive channel of small conductance-like 3;
DE AltName: Full=MscS-Like protein 3;
DE Flags: Precursor;
GN Name=MSL3; OrderedLocusNames=At1g58200; ORFNames=F16M22.2, T18I24.11;
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=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 [4]
RP GENE FAMILY.
RX PubMed=12626684; DOI=10.1128/mmbr.67.1.66-85.2003;
RA Pivetti C.D., Yen M.R., Miller S., Busch W., Tseng Y.H., Booth I.R.,
RA Saier M.H. Jr.;
RT "Two families of mechanosensitive channel proteins.";
RL Microbiol. Mol. Biol. Rev. 67:66-85(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16401419; DOI=10.1016/j.cub.2005.11.044;
RA Haswell E.S., Meyerowitz E.M.;
RT "MscS-like proteins control plastid size and shape in Arabidopsis
RT thaliana.";
RL Curr. Biol. 16:1-11(2006).
RN [6]
RP REVIEW, GENE FAMILY, AND NOMENCLATURE.
RX DOI=10.1016/S1063-5823(06)58013-5;
RA Haswell E.S.;
RT "MscS-like proteins in plants.";
RL (In) Hamill O.P. (eds.);
RL Mechanosensitive Ion Channels, Part A, pp.329-349, Academic Press, San
RL Diego. (2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21810996; DOI=10.1105/tpc.111.088112;
RA Wilson M.E., Jensen G.S., Haswell E.S.;
RT "Two mechanosensitive channel homologs influence division ring placement in
RT Arabidopsis chloroplasts.";
RL Plant Cell 23:2939-2949(2011).
CC -!- FUNCTION: Mechanosensitive channel that opens in response to stretch
CC forces in the membrane lipid bilayer. Controls plastid size, shape, and
CC perhaps division during normal plant development by altering ion flux
CC in response to changes in membrane tension. Acts as a component of the
CC chloroplast division machinery. {ECO:0000269|PubMed:16401419,
CC ECO:0000269|PubMed:21810996}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:16401419}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16401419}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16401419}.
CC -!- DISRUPTION PHENOTYPE: Msl2 and msl3 double mutant shows abnormalities
CC in the size and shape of plastids with enlarged chloroplasts containing
CC multiple FtsZ rings. {ECO:0000269|PubMed:16401419,
CC ECO:0000269|PubMed:21810996}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50758.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50956.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC073943; AAG50956.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC079131; AAG50758.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33512.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33513.1; -; Genomic_DNA.
DR EMBL; AY125504; AAM78096.1; -; mRNA.
DR EMBL; BT002720; AAO11636.1; -; mRNA.
DR PIR; D96615; D96615.
DR RefSeq; NP_176116.2; NM_104601.2.
DR RefSeq; NP_974046.1; NM_202317.3.
DR AlphaFoldDB; Q8L7W1; -.
DR SMR; Q8L7W1; -.
DR BioGRID; 27412; 9.
DR IntAct; Q8L7W1; 9.
DR STRING; 3702.AT1G58200.2; -.
DR iPTMnet; Q8L7W1; -.
DR PaxDb; Q8L7W1; -.
DR PRIDE; Q8L7W1; -.
DR ProteomicsDB; 250959; -.
DR EnsemblPlants; AT1G58200.1; AT1G58200.1; AT1G58200.
DR EnsemblPlants; AT1G58200.2; AT1G58200.2; AT1G58200.
DR GeneID; 842187; -.
DR Gramene; AT1G58200.1; AT1G58200.1; AT1G58200.
DR Gramene; AT1G58200.2; AT1G58200.2; AT1G58200.
DR KEGG; ath:AT1G58200; -.
DR Araport; AT1G58200; -.
DR TAIR; locus:2015297; AT1G58200.
DR eggNOG; ENOG502S0B8; Eukaryota.
DR HOGENOM; CLU_020185_1_0_1; -.
DR InParanoid; Q8L7W1; -.
DR OMA; RQDVWSL; -.
DR OrthoDB; 1186886at2759; -.
DR PhylomeDB; Q8L7W1; -.
DR PRO; PR:Q8L7W1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L7W1; baseline and differential.
DR Genevisible; Q8L7W1; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009526; C:plastid envelope; IDA:TAIR.
DR GO; GO:0010020; P:chloroplast fission; IGI:TAIR.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 2.30.30.60; -; 1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR006685; MscS_channel.
DR InterPro; IPR023408; MscS_dom_sf.
DR InterPro; IPR045042; YnaI-like.
DR PANTHER; PTHR43634; PTHR43634; 1.
DR Pfam; PF00924; MS_channel; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Ion channel; Ion transport; Membrane; Phosphoprotein; Plastid;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..678
FT /note="Mechanosensitive ion channel protein 3,
FT chloroplastic"
FT /id="PRO_0000415326"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 494..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 678 AA; 74189 MW; 549D3B3FFEBE0810 CRC64;
MMMRTVALPL SHDLNVHKIH EASGFHNSAA GKNRVYLTRT GLSSCATRQD VWSLQLLESL
SGSIVPVSSR CNAFVCRSAL SPGNGNEGPI LKSTAVIFTR VYDALGGNPH LVKLIPAVGI
LAFATWGLRP LLRLARTTLF EKGNDANSQK SSTQYIVVSY LQPLLLWSGA ILLCRTLDPI
VLPSSAGQAI KQRLLIFARS ISTVLAFSCC LSSLLQQVQK FFMETNNPAD TRNMGFSFAG
KAVYTAAWVA AASLFMELLG FSTQKWLTAG GLGTVLLTLA GREILTNFLS SIMIHATRPF
VLNEWIQTKI GGYEVSGTVE QVGWWSPTII RGDDREAVHI PNHQFSVNIV RNLTQKTHWR
IKTHLAISHL DVSKINNIVA DMRKVLSKNP QIEQQKIHRR VFLEDIDPEN QALRILISCF
VKTSRFEEYL CVKEAVLLDL LTVIRHHGAR LATPIRTVQR MRNEAEVDTA GFSDIVFNQA
AMNRRYMLIE PSYKINSDDN SKSPSPSPGQ KSPSPGQKSE ERDLQEEPSE TKAETENNGS
VPVSNAKKEN QKAALGSNSN TGTKGSSTST SDQPVAQKSE EKKKESVGDP HKAEKDEVSD
DEATIEQTLK SKAKQGSEKN NGESKARDGG GSGTSSLLEE NLVLGVALDG SKRTLPIDEE
HKASGALMDS EELGIGSE
