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RMV1_ARATH
ID   RMV1_ARATH              Reviewed;         490 AA.
AC   Q9FFL1;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Polyamine transporter RMV1;
DE   AltName: Full=Protein RESISTANT TO METHYL VIOLOGEN 1;
GN   Name=RMV1; OrderedLocusNames=At5g05630; ORFNames=MJJ3.2;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, MUTAGENESIS OF ILE-377, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=22492932; DOI=10.1073/pnas.1121406109;
RA   Fujita M., Fujita Y., Iuchi S., Yamada K., Kobayashi Y., Urano K.,
RA   Kobayashi M., Yamaguchi-Shinozaki K., Shinozaki K.;
RT   "Natural variation in a polyamine transporter determines paraquat tolerance
RT   in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:6343-6347(2012).
CC   -!- FUNCTION: Cell membrane polyamine/proton symporter involved in the
CC       polyamine uptake in cells. Possesses high affinity for spermine and
CC       spermidine and lower affinity for putrescine. Transports paraquat, a
CC       polyamine analog, and thus confers sensitivity to this chemical which
CC       is used as a herbicide. {ECO:0000269|PubMed:22492932}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.6 uM for spermine {ECO:0000269|PubMed:22492932};
CC         KM=2.2 uM for spermidine {ECO:0000269|PubMed:22492932};
CC         KM=56.5 uM for putrescine {ECO:0000269|PubMed:22492932};
CC         KM=24.4 uM for paraquat {ECO:0000269|PubMed:22492932};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22492932};
CC       Multi-pass membrane protein {ECO:0000305|PubMed:22492932}. Note=Plasma
CC       membrane.
CC   -!- DEVELOPMENTAL STAGE: Expressed in hypocotyls and petioles of cotyledons
CC       in 1- to 3-day-old seedlings. {ECO:0000269|PubMed:22492932}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants show increased tolerance to paraquat.
CC       {ECO:0000269|PubMed:22492932}.
CC   -!- MISCELLANEOUS: Methyl viologen is the brand name of paraquat. Plants
CC       over-expressing RMV1 show hypersensitivity to paraquat
CC       (PubMed:22492932). {ECO:0000305|PubMed:22492932}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. Polyamine:cation symporter (PHS) (TC 2.A.3.12) family.
CC       {ECO:0000305}.
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DR   EMBL; AB005237; BAB09657.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90901.1; -; Genomic_DNA.
DR   EMBL; AK119108; BAC43680.1; -; mRNA.
DR   EMBL; BT008298; AAP37657.1; -; mRNA.
DR   RefSeq; NP_196182.1; NM_120645.3.
DR   AlphaFoldDB; Q9FFL1; -.
DR   SMR; Q9FFL1; -.
DR   STRING; 3702.AT5G05630.1; -.
DR   TCDB; 2.A.3.12.3; the amino acid-polyamine-organocation (apc) family.
DR   PaxDb; Q9FFL1; -.
DR   PRIDE; Q9FFL1; -.
DR   ProteomicsDB; 228186; -.
DR   EnsemblPlants; AT5G05630.1; AT5G05630.1; AT5G05630.
DR   GeneID; 830446; -.
DR   Gramene; AT5G05630.1; AT5G05630.1; AT5G05630.
DR   KEGG; ath:AT5G05630; -.
DR   Araport; AT5G05630; -.
DR   TAIR; locus:2166354; AT5G05630.
DR   eggNOG; KOG1287; Eukaryota.
DR   HOGENOM; CLU_007946_17_3_1; -.
DR   InParanoid; Q9FFL1; -.
DR   OMA; ASLNICH; -.
DR   OrthoDB; 621852at2759; -.
DR   PhylomeDB; Q9FFL1; -.
DR   PRO; PR:Q9FFL1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FFL1; baseline and differential.
DR   Genevisible; Q9FFL1; 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:0015203; F:polyamine transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0015839; P:cadaverine transport; IMP:TAIR.
DR   GO; GO:0015846; P:polyamine transport; IDA:TAIR.
DR   GO; GO:0009408; P:response to heat; IMP:TAIR.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR044566; RMV1-like.
DR   PANTHER; PTHR45826; PTHR45826; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..490
FT                   /note="Polyamine transporter RMV1"
FT                   /id="PRO_0000418912"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         377
FT                   /note="I->F: Loss of sensitivity to paraquat."
FT                   /evidence="ECO:0000269|PubMed:22492932"
SQ   SEQUENCE   490 AA;  53694 MW;  E478743784CFE309 CRC64;
     MTELSSPNLD SASQKPRIST ENPPPPPPHI SIGVTTGDPA TSPARTVNQI KKITVLPLVF
     LIFYEVSGGP FGIEDSVKAA GPLLAIVGFI VFPFIWSIPE ALITAEMGTM FPENGGYVVW
     VTLAMGPYWG FQQGWVKWLS GVIDNALYPI LFLDYLKSGI PILGSGIPRV AAILVLTVAL
     TYLNYRGLSI VGVAAVLLGV FSILPFVVMS FMSIPKLKPS RWLVVSKKMK GVNWSLYLNT
     LFWNLNYWDS VSTLTGEVEN PSKTLPRALF YALLLVVFSY IFPVLTGTGA IALDQKLWTD
     GYFADIGKVI GGVWLGWWIQ AAAATSNMGM FLAEMSSDSF QLLGMAERGM LPEVFAKRSR
     YRTPWVGILF SASGVIILSW LSFQEIVAAE NLLYCFGMVL EFITFVRLRM KYPAASRPFK
     IPVGVLGSVL MCIPPTVLIG VIMAFTNLKV ALVSLAAIVI GLVLQPCLKQ VEKKGWLKFS
     TSSHLPNLME
 
 
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