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MSL2_ARATH
ID   MSL2_ARATH              Reviewed;         673 AA.
AC   Q56X46; B9DHF7; F4KGW2; Q9LXA1;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Mechanosensitive ion channel protein 2, chloroplastic;
DE   AltName: Full=Mechanosensitive channel of small conductance-like 2;
DE   AltName: Full=MscS-Like protein 2;
DE   Flags: Precursor;
GN   Name=MSL2; OrderedLocusNames=At5g10490; ORFNames=F12B17.160;
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] (ISOFORM 1).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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   [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   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   [7]
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   [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 (By similarity). Controls plastid
CC       size, shape, and perhaps division during normal plant development by
CC       altering ion flux in response to changes in membrane tension. Acts as a
CC       component of the chloroplast division machinery. {ECO:0000250,
CC       ECO:0000269|PubMed:16401419, 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q56X46-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q56X46-2; Sequence=VSP_042196;
CC       Name=3;
CC         IsoId=Q56X46-3; Sequence=VSP_042195;
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=CAB89394.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL353995; CAB89394.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED91551.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91552.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91553.1; -; Genomic_DNA.
DR   EMBL; AK221831; BAD94053.1; -; mRNA.
DR   EMBL; AK230015; BAF01838.1; -; mRNA.
DR   EMBL; AK317509; BAH20174.1; -; mRNA.
DR   PIR; T49990; T49990.
DR   RefSeq; NP_001078567.1; NM_001085098.2. [Q56X46-3]
DR   RefSeq; NP_001190278.1; NM_001203349.1. [Q56X46-2]
DR   RefSeq; NP_568230.2; NM_121087.3. [Q56X46-1]
DR   AlphaFoldDB; Q56X46; -.
DR   SMR; Q56X46; -.
DR   STRING; 3702.AT5G10490.1; -.
DR   TCDB; 1.A.23.4.4; the small conductance mechanosensitive ion channel (mscs) family.
DR   PaxDb; Q56X46; -.
DR   PRIDE; Q56X46; -.
DR   ProteomicsDB; 250958; -. [Q56X46-1]
DR   EnsemblPlants; AT5G10490.1; AT5G10490.1; AT5G10490. [Q56X46-1]
DR   EnsemblPlants; AT5G10490.2; AT5G10490.2; AT5G10490. [Q56X46-3]
DR   EnsemblPlants; AT5G10490.3; AT5G10490.3; AT5G10490. [Q56X46-2]
DR   GeneID; 830913; -.
DR   Gramene; AT5G10490.1; AT5G10490.1; AT5G10490. [Q56X46-1]
DR   Gramene; AT5G10490.2; AT5G10490.2; AT5G10490. [Q56X46-3]
DR   Gramene; AT5G10490.3; AT5G10490.3; AT5G10490. [Q56X46-2]
DR   KEGG; ath:AT5G10490; -.
DR   Araport; AT5G10490; -.
DR   TAIR; locus:2142414; AT5G10490.
DR   eggNOG; ENOG502QTPM; Eukaryota.
DR   InParanoid; Q56X46; -.
DR   OMA; WGLAPLM; -.
DR   OrthoDB; 1186886at2759; -.
DR   PhylomeDB; Q56X46; -.
DR   PRO; PR:Q56X46; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q56X46; baseline and differential.
DR   Genevisible; Q56X46; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
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; 2.
DR   Pfam; PF00924; MS_channel; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chloroplast; Ion channel; Ion transport; Membrane;
KW   Phosphoprotein; Plastid; Reference proteome; Transit peptide;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..75
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           76..673
FT                   /note="Mechanosensitive ion channel protein 2,
FT                   chloroplastic"
FT                   /id="PRO_0000415325"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          492..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..673
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         571
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7W1"
FT   VAR_SEQ         1..28
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_042195"
FT   VAR_SEQ         2..8
FT                   /note="ALYGTLQ -> RNFNF (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_042196"
SQ   SEQUENCE   673 AA;  74429 MW;  A8F1DCCD9353C6AD CRC64;
     MALYGTLQLS HSLGLCRNQR FCNPENSAMR RRLHISNGPL SLGVPLGQHG FSNILLSNYL
     RRPICSVPCR TTAFRCHSFS ASGKAIEPAV KAVTVVLTKS HGLMQQFPFV YKLVPAVALL
     VFSLWGLVPF ARQGRNILLN KNDNGWKKSG TYHVMTSYVQ PLLLWLGALF ICRALDPVVL
     PTEASKIVKD RLLNFVRSLS TVLAFAYCLS SLIQQTQKLF SETSNPSDTR NMGFQFAGKA
     LYSAVWVAAV SLFMELLGFS TQKWLTAGGL GTVLITLAGR EILTNFLSSV MIHATRPFVL
     NEWIQTKIEG YEVSGTVEHV GWWSPTIIRG EDREAIHIPN HKFTVNVVRN LTQKTHWRIK
     THLAISHLDV NKINNIVADM RKVLAKNPMV EQQRLHRRVF LENVIPENQA LSILISCFVK
     TSHHEEYLGV KEAILLDLLR VISHHRARLA TPIRTIRKMY TETDVENTPF GESMYGGVTS
     RRPLMLIEPA YKINGEDKSK SQNRAAKPTA EQENKGSNPK SKETSSPDLK ANVKVGESPV
     SDTNKVPEET VAKPVIKAVS KPPTPKDTET SGTEKPKAKR SGGTIKSTKT DETDSSTSSA
     SRSTLEENIV LGVALEGSKR TLPIEEEIHS PPMETDAKEL TGARRSGGNG PLVADKEQKD
     SQSQPNSGAS TEP
 
 
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