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MSL5_ARATH
ID   MSL5_ARATH              Reviewed;         881 AA.
AC   Q9LH74; Q56YB1;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Mechanosensitive ion channel protein 5;
DE   AltName: Full=Mechanosensitive channel of small conductance-like 5;
DE   AltName: Full=MscS-Like protein 5;
GN   Name=MSL5; OrderedLocusNames=At3g14810; ORFNames=T21E2.7;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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] OF 1-318.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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   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: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9LH74-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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DR   EMBL; AP002061; BAB02647.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75568.1; -; Genomic_DNA.
DR   EMBL; AK221412; BAD94388.1; -; mRNA.
DR   RefSeq; NP_188099.2; NM_112342.4. [Q9LH74-1]
DR   AlphaFoldDB; Q9LH74; -.
DR   SMR; Q9LH74; -.
DR   STRING; 3702.AT3G14810.1; -.
DR   TCDB; 1.A.23.4.8; the small conductance mechanosensitive ion channel (mscs) family.
DR   iPTMnet; Q9LH74; -.
DR   PaxDb; Q9LH74; -.
DR   PRIDE; Q9LH74; -.
DR   ProteomicsDB; 239005; -. [Q9LH74-1]
DR   EnsemblPlants; AT3G14810.1; AT3G14810.1; AT3G14810. [Q9LH74-1]
DR   GeneID; 820710; -.
DR   Gramene; AT3G14810.1; AT3G14810.1; AT3G14810. [Q9LH74-1]
DR   KEGG; ath:AT3G14810; -.
DR   Araport; AT3G14810; -.
DR   TAIR; locus:2099382; AT3G14810.
DR   eggNOG; KOG4629; Eukaryota.
DR   HOGENOM; CLU_013552_0_0_1; -.
DR   InParanoid; Q9LH74; -.
DR   OMA; GSRYIHM; -.
DR   PhylomeDB; Q9LH74; -.
DR   PRO; PR:Q9LH74; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LH74; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0008381; F:mechanosensitive ion channel activity; IBA:GO_Central.
DR   GO; GO:0006820; P:anion transport; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Alternative splicing; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..881
FT                   /note="Mechanosensitive ion channel protein 5"
FT                   /id="PRO_0000415328"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        642..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        677..697
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LYG9"
FT   CONFLICT        205
FT                   /note="T -> A (in Ref. 3; BAD94388)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   881 AA;  100366 MW;  42E3D5CBB471FBF1 CRC64;
     MAAVDSTDRR DFIVNINGQE SGAVGATGSS SNAEGGNIWK ESSYDFWDGE KGKNDKKGDD
     EDEDGGSFHF RQRGERRHSS AELSDPPSKL IGQFLHKQRA SGDEISLDVE LNMAELQSNT
     PPRPATASNT PRRGLTTISE SSSPVKTKVK ADAVRRRQNR TSLGGSSDEE GRNRDEAEVL
     KCGSKKPMLS RNKTKSRLQD PPTPTHPAID KTEMKSGRRS GIFKSGFLGK SPKAGTPGRN
     GFEEEEEEDP FLDEDLPEEF KRDKLSFWVF LEWISLVLIV TSLVCSLTIH NLQRKTWWKL
     DLWKWEVTVL VLICGRLVSS WIVRIIVFLV EKNFTWRKRV LYFVYGVRKS VQNCLWLGLV
     LLAWHFLFDK KVERETRSTA LRYVTRVLVC LLVALIIWLV KTILVKVLAS SFHMSTYFDR
     IQESLFTQYV IETLSGPPLM EIQRMEEEEQ QVAEDVKSLE KLAGAKLPPA LKATVKSFMK
     VGKSPGLNRI GSKRGEDGEG IRIDQLKRMN TKNVSAWNMK RLMNIILKGA ISTLDQNMQD
     TTQEDEDATH IRSEYEAKCA ARKIFHNVTE PGSRYIYLED FLRFLCEEEA ERAMALFEGA
     SESDKISKSC LKNWVVKAFR ERRALALTLN DTKTAVDRLH RIINVVIGII IIIIWLLILG
     IATTRFLLVL SSQLLLVAFV FGNSCKTIFE AIIFLFVMHP FDVGDRCEID GVQLVVEEMN
     ILTTVFLRYD NQKIIYPNSV LGTKPIANYY RSPDMGDAVE FCVHIATPPE KITAIKQRIL
     SYVDNKKDYW YPAPMIVFLS MDDLNSVKIA VWLTHRMNHQ DMGERYIRRG LLLEEVGKTC
     RELDIEYRLY PLNINVRSLP PTANPTSSDR IPPSWMQQRG P
 
 
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