MSL9_ARATH
ID MSL9_ARATH Reviewed; 742 AA.
AC Q84M97;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Mechanosensitive ion channel protein 9;
DE AltName: Full=Mechanosensitive channel of small conductance-like 9;
DE AltName: Full=MscS-Like protein 9;
DE Short=AtMSL9;
GN Name=MSL9; OrderedLocusNames=At5g19520; ORFNames=T20D1.40;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [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 FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18485707; DOI=10.1016/j.cub.2008.04.039;
RA Haswell E.S., Peyronnet R., Barbier-Brygoo H., Meyerowitz E.M.,
RA Frachisse J.M.;
RT "Two MscS homologs provide mechanosensitive channel activities in the
RT Arabidopsis root.";
RL Curr. Biol. 18:730-734(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-36, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [9]
RP FUNCTION.
RX PubMed=19704841; DOI=10.4161/psb.3.9.6487;
RA Peyronnet R., Haswell E.S., Barbier-Brygoo H., Frachisse J.M.;
RT "AtMSL9 and AtMSL10: Sensors of plasma membrane tension in Arabidopsis
RT roots.";
RL Plant Signal. Behav. 3:726-729(2008).
CC -!- FUNCTION: Mechanosensitive channel that opens in response to stretch
CC forces in the membrane lipid bilayer. {ECO:0000269|PubMed:18485707,
CC ECO:0000269|PubMed:19704841}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18485707};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18485707}.
CC -!- TISSUE SPECIFICITY: Detected in the epidermis, cortex, and endodermis
CC of the root tip. {ECO:0000269|PubMed:18485707}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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DR EMBL; AF296830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92720.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69951.1; -; Genomic_DNA.
DR EMBL; BT006457; AAP21265.1; -; mRNA.
DR EMBL; AK228195; BAF00149.1; -; mRNA.
DR RefSeq; NP_001331595.1; NM_001343609.1.
DR RefSeq; NP_197453.1; NM_121957.4.
DR AlphaFoldDB; Q84M97; -.
DR SMR; Q84M97; -.
DR BioGRID; 17348; 2.
DR STRING; 3702.AT5G19520.1; -.
DR iPTMnet; Q84M97; -.
DR PaxDb; Q84M97; -.
DR PRIDE; Q84M97; -.
DR ProteomicsDB; 250960; -.
DR EnsemblPlants; AT5G19520.1; AT5G19520.1; AT5G19520.
DR EnsemblPlants; AT5G19520.2; AT5G19520.2; AT5G19520.
DR GeneID; 832072; -.
DR Gramene; AT5G19520.1; AT5G19520.1; AT5G19520.
DR Gramene; AT5G19520.2; AT5G19520.2; AT5G19520.
DR KEGG; ath:AT5G19520; -.
DR Araport; AT5G19520; -.
DR TAIR; locus:2180811; AT5G19520.
DR eggNOG; KOG4629; Eukaryota.
DR HOGENOM; CLU_013552_1_0_1; -.
DR InParanoid; Q84M97; -.
DR OMA; LNHSMHD; -.
DR OrthoDB; 609350at2759; -.
DR PhylomeDB; Q84M97; -.
DR PRO; PR:Q84M97; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84M97; baseline and differential.
DR Genevisible; Q84M97; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IMP:TAIR.
DR GO; GO:0006820; P:anion transport; IBA:GO_Central.
DR GO; GO:0050982; P:detection of mechanical stimulus; IMP:TAIR.
DR Gene3D; 2.30.30.60; -; 1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR016688; MscS-like_plants/fungi.
DR InterPro; IPR006685; MscS_channel.
DR InterPro; IPR023408; MscS_dom_sf.
DR PANTHER; PTHR31618; PTHR31618; 1.
DR Pfam; PF00924; MS_channel; 1.
DR PIRSF; PIRSF017209; Memb_At2g17000_prd; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..742
FT /note="Mechanosensitive ion channel protein 9"
FT /id="PRO_0000415331"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LYG9"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LYG9"
SQ SEQUENCE 742 AA; 84249 MW; 42E588958BAE2F85 CRC64;
MAERRVSNGE EVVINVSDKE DSKDPRASPS FNPLASPDSD AGIEKSKPVP PISIPTPEIY
KFSGSVHKPP KIPSPEGLVR RKSLSRSIYS KPKSRFGEQQ SFRYDSTREE NGGRSLREQF
GAGSFARGSF DRASPNNKSN RSVASAALSK VAEEEPDENE EIYKKVKLHR VKRSGMKPLA
FLELVVFMAI LGALIVSLTI DVVNKHTIWG LEFWKWCVLV MVTLSGMLVT NWFMHFVVFI
IEKNYLLRKK VLYFVHGLKK NVQVFIWFSL VLIAWICLFD GDVKRTRKTK RFLDFITWTI
VSLLVGSILF LVKTFALKVL ASKFNVRNFF ERIQESVFHQ YVLQTLSGPP LIEEAENVGR
VPSTGHLSFT RTKDGKVKDK KVIDMGKVHR MKQEKVSAWT MRVLIEAVGT SGISTISSTL
DEVNNKKERT DKEITNEMEA VAAAYDVFNN VAKPNHNYIE EDDLLRFMIK EEVDLVLPLI
EDADTGKITR KTFTEWVVNV YTSRKTIGHS LNDTKTAVKQ LDKLITGILT VITFIVWMVL
LDIASTKLLL VFSSQFLGLA FMIGSTCKNI FESFMFVFVM HPYDVGDRCV VDGVMLLVEE
IDLLTTVFLK IDNEKVFYPN SVLISKPISN FYRSPDMGDY VDFGIAFSTP AEKIGCLKGK
IGEYLVANSQ HWYPEAQVMV RAIENMNKLV LNILVQHTIN FQVYVEKSLR RTALIIAIKR
ILEDLEIDYT LLPQDVNLTG HK
