OCT5_ARATH
ID OCT5_ARATH Reviewed; 515 AA.
AC Q9SAK7; Q8L7V4;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Organic cation/carnitine transporter 5;
DE Short=AtOCT5;
GN Name=OCT5; Synonyms=5-Oct; OrderedLocusNames=At1g79410; ORFNames=T8K14.17;
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] OF 31-515.
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 leaves and siliques, and, to a
CC lower extent, in roots, stems and flowers.
CC {ECO:0000269|PubMed:18710496}.
CC -!- INDUCTION: During drought, cold 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM78113.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007202; AAD30235.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36239.1; -; Genomic_DNA.
DR EMBL; AY125523; AAM78113.1; ALT_INIT; mRNA.
DR PIR; B96825; B96825.
DR RefSeq; NP_178059.1; NM_106589.3.
DR AlphaFoldDB; Q9SAK7; -.
DR SMR; Q9SAK7; -.
DR STRING; 3702.AT1G79410.1; -.
DR PaxDb; Q9SAK7; -.
DR PRIDE; Q9SAK7; -.
DR ProteomicsDB; 238995; -.
DR EnsemblPlants; AT1G79410.1; AT1G79410.1; AT1G79410.
DR GeneID; 844279; -.
DR Gramene; AT1G79410.1; AT1G79410.1; AT1G79410.
DR KEGG; ath:AT1G79410; -.
DR Araport; AT1G79410; -.
DR TAIR; locus:2206430; AT1G79410.
DR eggNOG; KOG0255; Eukaryota.
DR HOGENOM; CLU_001265_33_5_1; -.
DR InParanoid; Q9SAK7; -.
DR OMA; PGIMEVP; -.
DR OrthoDB; 704438at2759; -.
DR PhylomeDB; Q9SAK7; -.
DR PRO; PR:Q9SAK7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAK7; baseline and differential.
DR Genevisible; Q9SAK7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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: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; Ion transport; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..515
FT /note="Organic cation/carnitine transporter 5"
FT /id="PRO_0000415361"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..172
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..195
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..411
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..467
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 195..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 515 AA; 57151 MW; A78C0CC2145C8958 CRC64;
MADSLAPLLP THIEEDEDTS SPLTFDKILE KSLSDFGFSQ FLQIVLVGLA LTFDSQQIFI
TVFTDAYPTW HCLDHTICNP ATTDICKIPR SAWDWDGGFK GKSVISEFDL ECSSSFLRSL
PSSTFYVGSI VGGVVLAMIP DGSLGRKQLL FFSSFAMSLT GISIFLSSNI WIYSFLKFVI
GFARSQTGTY ALVLISERIS TKWRPRATMV PFTLFVLGFM SLSGIAYLVR HASWKVLYLC
TSIPAGIHSI FIYFFALESP RWLHLEGKNK EAIEVLKRIS PANRGYLESV SSRLRPKETL
EQTSSYSIKD LFIIKWAFRR VTLVMIIMFG LGMSYYGVPL AVRDIKVNIY MSEALNAMVE
LPTFVVTPIL LEQFSRRSSV LVNCLIGGAS GVLCFVMSLY GRTKIAFALE LGSFFCARIG
FNLMAIYLVE LFPTCVRNSA TMMLRQALVV GGACCPLIAS LGRNVPSLSF AVFGFAMSGL
GLFALLLPET KGLSLCDTME EQEQRDQALK TSHSC
