OCT3_ARATH
ID OCT3_ARATH Reviewed; 518 AA.
AC Q9SA38;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Organic cation/carnitine transporter 3;
DE Short=AtOCT3;
GN Name=OCT3; Synonyms=3-Oct; OrderedLocusNames=At1g16390; ORFNames=F3O9.19;
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;
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 [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: Mostly expressed in siliques, mainly in young
CC seeds. Present in stems (cortical cells and parenchyma cells), at the
CC basis of secondary inflorescences, and at the base of trichomes.
CC {ECO:0000269|PubMed:18710496}.
CC -!- INDUCTION: During cold stress treatment. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC006341; AAD34691.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29445.1; -; Genomic_DNA.
DR EMBL; AY078972; AAL79578.1; -; mRNA.
DR EMBL; BT000863; AAN38700.1; -; mRNA.
DR PIR; B86299; B86299.
DR RefSeq; NP_173089.1; NM_101505.3.
DR AlphaFoldDB; Q9SA38; -.
DR SMR; Q9SA38; -.
DR STRING; 3702.AT1G16390.1; -.
DR PaxDb; Q9SA38; -.
DR PRIDE; Q9SA38; -.
DR ProteomicsDB; 250864; -.
DR EnsemblPlants; AT1G16390.1; AT1G16390.1; AT1G16390.
DR GeneID; 838209; -.
DR Gramene; AT1G16390.1; AT1G16390.1; AT1G16390.
DR KEGG; ath:AT1G16390; -.
DR Araport; AT1G16390; -.
DR TAIR; locus:2032825; AT1G16390.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_001265_33_5_1; -.
DR InParanoid; Q9SA38; -.
DR OMA; PWHCTGV; -.
DR OrthoDB; 762280at2759; -.
DR PhylomeDB; Q9SA38; -.
DR PRO; PR:Q9SA38; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SA38; baseline and differential.
DR Genevisible; Q9SA38; 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:0070417; P:cellular response to cold; 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..518
FT /note="Organic cation/carnitine transporter 3"
FT /id="PRO_0000415359"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..197
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..259
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..355
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..410
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..470
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 518 AA; 57393 MW; 53D48122D575645C CRC64;
MADSTRPLLS DFNSSESNLP PPRSLEETIE RCIGDFGWAQ FLQAALVSFA WFFDAQQTFI
TVFTDSQPMW HCDNSDRVDS VCNTSSSNLC TLPNQTWSWD LNPHVSIISE WGLQCAGSFL
KGFPASSFFL GCLIGGLALS TLADSSLGRK NMLLLSCLIM SLSSMLTAFS TSIWVYAFLR
FLNGCGRATI GTCALVLSTE LVGKKWRGQV GAMGFFCFTL GFLSLPMLGY INEGNSWRNL
YVWTSIPTLI YCCLVRSFVR ESPRWLIVKG RKEEAVSILQ SIASNAITMS FTNLCFEVEN
DQSKSNPDVY DALKILVRKS WSFRRLLAAM VVGFGIGMVY YGMPLALTNL NFNLYLGVVF
NALSEFPAFL ITFFFIDKIN RRDALIGFTA LSGISSALIA VLGQQLGSLQ IVLELVSFFS
ACTAFNMTLI YTIEMFPTCV RNSAISMVRQ ALVFGGVFSP VMVAAGRENQ FWSYGLFGLI
IGLCGLFVFG LPETRGSVLC DTMDEEEYKT LAKRQFIG
