MSL1_ARATH
ID MSL1_ARATH Reviewed; 497 AA.
AC Q8VZL4; O23073;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Mechanosensitive ion channel protein 1, mitochondrial;
DE AltName: Full=Mechanosensitive channel of small conductance-like 1;
DE AltName: Full=MscS-Like protein 1;
DE Flags: Precursor;
GN Name=MSL1; OrderedLocusNames=At4g00290; ORFNames=A_IG005I10.9, F5I10.9;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 (SEP-2004) 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).
CC -!- FUNCTION: Mechanosensitive channel that opens in response to stretch
CC forces in the membrane lipid bilayer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB62830.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF02788.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80787.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF013293; AAB62830.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF195115; AAF02788.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161471; CAB80787.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81850.1; -; Genomic_DNA.
DR EMBL; AY064027; AAL36383.1; -; mRNA.
DR EMBL; AY096611; AAM20261.1; -; mRNA.
DR EMBL; AK176463; BAD44226.1; -; mRNA.
DR EMBL; AK176579; BAD44342.1; -; mRNA.
DR PIR; T01542; T01542.
DR RefSeq; NP_567165.2; NM_116250.5.
DR PDB; 6LYP; EM; 3.30 A; A/B/C/D/E/F/G=1-497.
DR PDB; 6VXM; EM; 3.06 A; A/B/C/D/E/F/G=79-497.
DR PDB; 6VXN; EM; 2.96 A; A/B/C/D/E/F/G=79-497.
DR PDB; 6VXP; EM; 3.39 A; A/B/C/D/E/F/G=79-497.
DR PDBsum; 6LYP; -.
DR PDBsum; 6VXM; -.
DR PDBsum; 6VXN; -.
DR PDBsum; 6VXP; -.
DR AlphaFoldDB; Q8VZL4; -.
DR SMR; Q8VZL4; -.
DR STRING; 3702.AT4G00290.1; -.
DR TCDB; 1.A.23.4.11; the small conductance mechanosensitive ion channel (mscs) family.
DR iPTMnet; Q8VZL4; -.
DR PaxDb; Q8VZL4; -.
DR PRIDE; Q8VZL4; -.
DR ProteomicsDB; 250956; -.
DR EnsemblPlants; AT4G00290.1; AT4G00290.1; AT4G00290.
DR GeneID; 828077; -.
DR Gramene; AT4G00290.1; AT4G00290.1; AT4G00290.
DR KEGG; ath:AT4G00290; -.
DR Araport; AT4G00290; -.
DR TAIR; locus:2126061; AT4G00290.
DR eggNOG; ENOG502QRDM; Eukaryota.
DR HOGENOM; CLU_024228_1_0_1; -.
DR InParanoid; Q8VZL4; -.
DR OMA; NIMEICL; -.
DR OrthoDB; 622812at2759; -.
DR PhylomeDB; Q8VZL4; -.
DR PRO; PR:Q8VZL4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VZL4; baseline and differential.
DR Genevisible; Q8VZL4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IDA:TAIR.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:TAIR.
DR Gene3D; 2.30.30.60; -; 1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR006685; MscS_channel.
DR InterPro; IPR011014; MscS_channel_TM-2.
DR InterPro; IPR023408; MscS_dom_sf.
DR Pfam; PF00924; MS_channel; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
DR SUPFAM; SSF82861; SSF82861; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion channel; Ion transport; Membrane; Mitochondrion;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..86
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 87..497
FT /note="Mechanosensitive ion channel protein 1,
FT mitochondrial"
FT /id="PRO_0000415324"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 205..226
FT /evidence="ECO:0007829|PDB:6VXN"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:6LYP"
FT HELIX 239..266
FT /evidence="ECO:0007829|PDB:6VXN"
FT HELIX 278..299
FT /evidence="ECO:0007829|PDB:6VXN"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:6LYP"
FT HELIX 316..340
FT /evidence="ECO:0007829|PDB:6VXN"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:6VXN"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:6VXN"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:6VXN"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:6VXN"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:6VXN"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:6VXN"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:6VXN"
FT STRAND 396..407
FT /evidence="ECO:0007829|PDB:6VXN"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:6VXN"
FT HELIX 414..427
FT /evidence="ECO:0007829|PDB:6VXN"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:6VXN"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:6VXN"
FT STRAND 439..446
FT /evidence="ECO:0007829|PDB:6VXN"
FT STRAND 449..460
FT /evidence="ECO:0007829|PDB:6VXN"
FT HELIX 463..483
FT /evidence="ECO:0007829|PDB:6VXN"
SQ SEQUENCE 497 AA; 53884 MW; 1BB1EBAEFECBCAD6 CRC64;
MAGVRLSLLK SIQRSIKPHA TAKSCSGLLN SHARAFTCGN LLDGPKASPS MISFSSNIRL
HNDAKPFNYL GHSSYARAFS SKSDDFGSIV ASGVTGSGDG NGNGNDWVEK AKDVLQTSVD
AVTETAKKTK DVSDEMIPHV QQFLDSNPYL KDVIVPVSLT MTGTLFAWVV MPRILRRFHT
YAMQSSAKLL PVGFSNEDVP YEKSFWGALE DPARYLVTFI AFAQIAAMVA PTTIAAQYFS
PTVKGAVILS LVWFLYRWKT NVITRMLSAK SFGGLDREKV LTLDKVSSVG LFAIGLMASA
EACGVAVQSI LTVGGVGGVA TAFAARDILG NVLSGLSMQF SRPFSMGDTI KAGSVEGQVI
EMGLTTTSLL NAEKFPVLVP NSLFSSQVIV NKSRAQWRAI ASKIPLQIDD LDMIPQISNE
IKEMLRSNTK VFLGKEAPHC YLSRVEKSFA ELTIGCNLIR MGKEELYNTQ QEVLLEAVKI
IKKHGVSLGT TWDNSTL
