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OCT6_ARATH
ID   OCT6_ARATH              Reviewed;         521 AA.
AC   Q9SA36;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Organic cation/carnitine transporter 6;
DE            Short=AtOCT6;
GN   Name=OCT6; Synonyms=6-Oct; OrderedLocusNames=At1g16370; ORFNames=F3O9.17;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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].
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   SUBCELLULAR LOCATION, INDUCTION BY ABIOTIC STRESS, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=18710496; DOI=10.1186/1756-0500-1-43;
RA   Kuefner I., Koch W.;
RT   "Stress regulated members of the plant organic cation transporter family
RT   are localized to the vacuolar membrane.";
RL   BMC Res. Notes 1:43-43(2008).
CC   -!- FUNCTION: High affinity carnitine transporter involved in the active
CC       cellular uptake of carnitine. Also transports organic cations (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:18710496};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:18710496}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and stems. In the stem of
CC       secondary inflorescences, localized to the phloem. Also present in
CC       flowers, specifically in the stamen, in the filaments and the
CC       connective, and restricted to major veins in leaves.
CC       {ECO:0000269|PubMed:18710496}.
CC   -!- INDUCTION: During drought and salt stress treatments.
CC       {ECO:0000269|PubMed:18710496}.
CC   -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC       Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR   EMBL; AC006341; AAD34689.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29443.1; -; Genomic_DNA.
DR   EMBL; AK229354; BAF01217.1; -; mRNA.
DR   PIR; H86298; H86298.
DR   RefSeq; NP_173087.1; NM_101503.4.
DR   AlphaFoldDB; Q9SA36; -.
DR   SMR; Q9SA36; -.
DR   STRING; 3702.AT1G16370.1; -.
DR   TCDB; 2.A.1.19.39; the major facilitator superfamily (mfs).
DR   PaxDb; Q9SA36; -.
DR   PRIDE; Q9SA36; -.
DR   ProteomicsDB; 250866; -.
DR   EnsemblPlants; AT1G16370.1; AT1G16370.1; AT1G16370.
DR   GeneID; 838207; -.
DR   Gramene; AT1G16370.1; AT1G16370.1; AT1G16370.
DR   KEGG; ath:AT1G16370; -.
DR   Araport; AT1G16370; -.
DR   TAIR; locus:2032790; AT1G16370.
DR   eggNOG; KOG0255; Eukaryota.
DR   HOGENOM; CLU_001265_33_5_1; -.
DR   InParanoid; Q9SA36; -.
DR   OMA; MFLAFEF; -.
DR   OrthoDB; 396963at2759; -.
DR   PhylomeDB; Q9SA36; -.
DR   PRO; PR:Q9SA36; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SA36; baseline and differential.
DR   Genevisible; Q9SA36; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0071472; P:cellular response to salt stress; IEP:UniProtKB.
DR   GO; GO:0042631; P:cellular response to water deprivation; IEP:UniProtKB.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycoprotein; Ion transport; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..521
FT                   /note="Organic cation/carnitine transporter 6"
FT                   /id="PRO_0000415362"
FT   TOPO_DOM        1..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..123
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..177
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..182
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..200
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        201..213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..326
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        348..356
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        378..385
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        407..412
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        434..447
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        469..473
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        474..494
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        495..521
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         200..207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   521 AA;  58351 MW;  33FFB80C620A616E CRC64;
     MADPISEPLL SHLTDDSGVN EKTRLEALTF DKIVEQSLSD FGFWQFFQIS LVGLALLFDA
     QQIFITVYTD AYPTWHCLNH TICDPSASDI CKLPRSAWEW DGGSQGKSVI SEFGLECSSS
     LLRGMPSSAF YIGAIVGGFF LALIPDDSLG RKKLVLFSTF AMSITSISVI FSTNVWIYTF
     LKFIIGFSRS QTWSYALVLI SERVSTRWRP RATMIPFTLF VLGFMSLSGI AFLAQDSSWR
     YLYLYTSVPA VFYCIFLYLF ALESPRWLHM QGKDKEAIDV LTKMSPKEKA YLESVVSKLP
     LKQENFEQAP TYSIKDFFFR KWAFRRILVV MIIMFGLGIS YYGVPLAARD IDVNIYLSET
     LNALVELPTF VITPILLERF NRRSSVLVNT LLGGASGVLC FVLSILGKTE IAFAFELGTF
     FCARIGFNLM AVFMVEMFPT CVRSSATMMF RQALVVGGAC CPLIASIGRY IPSVSFAIFG
     IAMSGLGMFV LILPETKGLS LCDSMEEQEK RDQAVNTSHV C
 
 
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