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MSL10_ARATH
ID   MSL10_ARATH             Reviewed;         734 AA.
AC   Q9LYG9; C0Z2U6;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=Mechanosensitive ion channel protein 10;
DE   AltName: Full=Mechanosensitive channel of small conductance-like 10;
DE   AltName: Full=MscS-Like protein 10;
DE            Short=AtMSL10;
GN   Name=MSL10; OrderedLocusNames=At5g12080; ORFNames=F14F18.230, MXC9.3;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
RN   [2]
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   [3]
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   [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128 AND SER-131, AND
RP   IDENTIFICATION BY 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128 AND SER-131, AND
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   [9]
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   [10]
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   [11]
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).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, 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).
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 root tip and throughout the
CC       vasculature of the root and leaf. {ECO:0000269|PubMed:18485707}.
CC   -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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DR   EMBL; AB007727; BAB10026.1; -; Genomic_DNA.
DR   EMBL; AL163812; CAB87679.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91759.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91760.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91761.1; -; Genomic_DNA.
DR   EMBL; AY075640; AAL77649.1; -; mRNA.
DR   EMBL; BT002236; AAN72247.1; -; mRNA.
DR   EMBL; AK318910; BAH57025.1; -; mRNA.
DR   PIR; T48565; T48565.
DR   RefSeq; NP_001119212.1; NM_001125740.2.
DR   RefSeq; NP_196769.1; NM_121246.5.
DR   RefSeq; NP_850810.1; NM_180479.2.
DR   AlphaFoldDB; Q9LYG9; -.
DR   SMR; Q9LYG9; -.
DR   BioGRID; 16359; 1.
DR   IntAct; Q9LYG9; 1.
DR   STRING; 3702.AT5G12080.2; -.
DR   TCDB; 1.A.23.4.14; the small conductance mechanosensitive ion channel (mscs) family.
DR   iPTMnet; Q9LYG9; -.
DR   PaxDb; Q9LYG9; -.
DR   PRIDE; Q9LYG9; -.
DR   ProteomicsDB; 250955; -.
DR   EnsemblPlants; AT5G12080.1; AT5G12080.1; AT5G12080.
DR   EnsemblPlants; AT5G12080.2; AT5G12080.2; AT5G12080.
DR   EnsemblPlants; AT5G12080.3; AT5G12080.3; AT5G12080.
DR   GeneID; 831081; -.
DR   Gramene; AT5G12080.1; AT5G12080.1; AT5G12080.
DR   Gramene; AT5G12080.2; AT5G12080.2; AT5G12080.
DR   Gramene; AT5G12080.3; AT5G12080.3; AT5G12080.
DR   KEGG; ath:AT5G12080; -.
DR   Araport; AT5G12080; -.
DR   TAIR; locus:2143069; AT5G12080.
DR   eggNOG; KOG4629; Eukaryota.
DR   HOGENOM; CLU_013552_1_0_1; -.
DR   InParanoid; Q9LYG9; -.
DR   OMA; WTIIAYA; -.
DR   OrthoDB; 609350at2759; -.
DR   PhylomeDB; Q9LYG9; -.
DR   PRO; PR:Q9LYG9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LYG9; baseline and differential.
DR   Genevisible; Q9LYG9; 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; IDA:TAIR.
DR   GO; GO:0006820; P:anion transport; IDA:TAIR.
DR   GO; GO:0050982; P:detection of mechanical stimulus; IMP:TAIR.
DR   GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR   GO; GO:0097468; P:programmed cell death in response to reactive oxygen species; 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..734
FT                   /note="Mechanosensitive ion channel protein 10"
FT                   /id="PRO_0000311999"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        516..536
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        551..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q84M97"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:14506206,
FT                   ECO:0007744|PubMed:15308754"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:14506206,
FT                   ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   734 AA;  83032 MW;  ACE37655EEFFC149 CRC64;
     MAEQKSSNGG GGGGDVVINV PVEEASRRSK EMASPESEKG VPFSKSPSPE ISKLVGSPNK
     PPRAPNQNNV GLTQRKSFAR SVYSKPKSRF VDPSCPVDTS ILEEEVREQL GAGFSFSRAS
     PNNKSNRSVG SPAPVTPSKV VVEKDEDEEI YKKVKLNREM RSKISTLALI ESAFFVVILS
     ALVASLTINV LKHHTFWGLE VWKWCVLVMV IFSGMLVTNW FMRLIVFLIE TNFLLRRKVL
     YFVHGLKKSV QVFIWLCLIL VAWILLFNHD VKRSPAATKV LKCITRTLIS ILTGAFFWLV
     KTLLLKILAA NFNVNNFFDR IQDSVFHQYV LQTLSGLPLM EEAERVGREP STGHLSFATV
     VKKGTVKEKK VIDMGKVHKM KREKVSAWTM RVLMEAVRTS GLSTISDTLD ETAYGEGKEQ
     ADREITSEME ALAAAYHVFR NVAQPFFNYI EEEDLLRFMI KEEVDLVFPL FDGAAETGRI
     TRKAFTEWVV KVYTSRRALA HSLNDTKTAV KQLNKLVTAI LMVVTVVIWL LLLEVATTKV
     LLFFSTQLVA LAFIIGSTCK NLFESIVFVF VMHPYDVGDR CVVDGVAMLV EEMNLLTTVF
     LKLNNEKVYY PNAVLATKPI SNYFRSPNMG ETVEFSISFS TPVSKIAHLK ERIAEYLEQN
     PQHWAPVHSV VVKEIENMNK LKMALYSDHT ITFQENRERN LRRTELSLAI KRMLEDLHID
     YTLLPQDINL TKKN
 
 
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