OCT1_ARATH
ID OCT1_ARATH Reviewed; 539 AA.
AC Q9CAT6; Q8LAB6;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Organic cation/carnitine transporter 1;
DE Short=AtOCT1;
GN Name=OCT1; Synonyms=1-Oct; OrderedLocusNames=At1g73220; ORFNames=T18K17.11;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 212-539.
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION BY IMBIBITION.
RX PubMed=17521409; DOI=10.1111/j.1365-313x.2007.03131.x;
RA Lelandais-Briere C., Jovanovic M., Torres G.A.M., Perrin Y., Lemoine R.,
RA Corre-Menguy F., Hartmann C.;
RT "Disruption of AtOCT1, an organic cation transporter gene, affects root
RT development and carnitine-related responses in Arabidopsis.";
RL Plant J. 51:154-164(2007).
CC -!- FUNCTION: High affinity carnitine transporter involved in the active
CC cellular uptake of carnitine. Also transports organic cations.
CC Regulates lateral root development. {ECO:0000269|PubMed:17521409}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17521409};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17521409}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular tissues and at sites of
CC lateral root formation. Mostly present in floral buds, flowers and
CC immature siliques. {ECO:0000269|PubMed:17521409}.
CC -!- DEVELOPMENTAL STAGE: In flowers, expressed in anthers, sepals, petals
CC and peduncles. Accumulates during germination in embryos, reaching a
CC maximum during the radicle emergence. In seedlings, restricted to the
CC vasculature, with highest levels in the collar and the root. Later
CC present in both elongation and root hair zones in roots. Also present
CC in root cap columella. Detected before and during lateral root
CC initiation and emergence and thereafter remained in vascular tissues of
CC each lateral root. {ECO:0000269|PubMed:17521409}.
CC -!- INDUCTION: Accumulates in embryo upon imbibition.
CC {ECO:0000269|PubMed:17521409}.
CC -!- DISRUPTION PHENOTYPE: Reduced sensitivity to carnitine and high degree
CC of root branching. {ECO:0000269|PubMed:17521409}.
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; AC010556; AAG52125.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35431.1; -; Genomic_DNA.
DR EMBL; BT002455; AAO00815.1; -; mRNA.
DR EMBL; BT008894; AAP68333.1; -; mRNA.
DR EMBL; AY087932; AAM67370.1; -; mRNA.
DR PIR; C96758; C96758.
DR RefSeq; NP_565059.2; NM_105981.4.
DR AlphaFoldDB; Q9CAT6; -.
DR SMR; Q9CAT6; -.
DR STRING; 3702.AT1G73220.1; -.
DR TCDB; 2.A.1.19.13; the major facilitator superfamily (mfs).
DR PaxDb; Q9CAT6; -.
DR PRIDE; Q9CAT6; -.
DR ProteomicsDB; 250862; -.
DR EnsemblPlants; AT1G73220.1; AT1G73220.1; AT1G73220.
DR GeneID; 843656; -.
DR Gramene; AT1G73220.1; AT1G73220.1; AT1G73220.
DR KEGG; ath:AT1G73220; -.
DR Araport; AT1G73220; -.
DR TAIR; locus:2197244; AT1G73220.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_001265_33_5_1; -.
DR InParanoid; Q9CAT6; -.
DR OMA; TEVYQSI; -.
DR OrthoDB; 762280at2759; -.
DR PhylomeDB; Q9CAT6; -.
DR PRO; PR:Q9CAT6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAT6; baseline and differential.
DR Genevisible; Q9CAT6; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015226; F:carnitine transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015839; P:cadaverine transport; IEP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IEP:TAIR.
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; Cell membrane; Developmental protein; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..539
FT /note="Organic cation/carnitine transporter 1"
FT /id="PRO_0000415357"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..133
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..218
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..489
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 539 AA; 59660 MW; 746096B8EBED653B CRC64;
MEPSKQEVPK LMETPPNISN DSSATEKGEA TRQQQLPNNR YALTVDEVIE QHIGALGFAQ
ILHALLVSIA WIFDAQTTLI SIFSDAQPAA RLLATGAIVE GASLCGLASG EWEWIGPKSD
TVVSEWNLIC QHKFLVAVPS TLFFIGSLFG SGVYGYLADS WFGRKKTLLL SCVLTFVTAF
AISFSPNVWV YAFLRFANGF FRSGIGSCCI VLATEIVGKK WRGQVGQYGF FFFTLGFLSL
PLMAYLERKS WRNLYRIISF LPLGYAVCLL PFAYESPRWL LVKGRNKEAM VVLKKLARLN
GKQLPADLSL VDPIPERDDQ TSSSEKFWKT KWAVKRIIMV MMAGFGSGFV YYGIQLNAEN
LNFNLYLTVA VNALMEFPAV FIGSFLLGVM NRRPLFSNSS YLAGFACLLC AVLSIHRVIR
AISVAKWLQL AVEAVGFMAS STAYDVLYVY CVELFPTNVR NTAVSLLRQA FMLGASAAPL
LVALGRESAM MSFIVFGVAS VLSGIVSLWL RETRNAPLYE TLAQQGKAEE IENETIMIT
