PUP1_ARATH
ID PUP1_ARATH Reviewed; 356 AA.
AC Q9FZ96; Q9M7R1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Purine permease 1 {ECO:0000303|PubMed:10662864};
DE Short=AtPUP1 {ECO:0000303|PubMed:10662864};
GN Name=PUP1 {ECO:0000303|PubMed:10662864};
GN OrderedLocusNames=At1g28230 {ECO:0000312|Araport:AT1G28230};
GN ORFNames=F3H9.22 {ECO:0000312|EMBL:AAF98432.1}, F3H9_10;
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 [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=10662864; DOI=10.2307/3870929;
RA Gillissen B., Buerkle L., Andre B., Kuehn C., Rentsch D., Brandl B.,
RA Frommer W.B.;
RT "A new family of high-affinity transporters for adenine, cytosine, and
RT purine derivatives in Arabidopsis.";
RL Plant Cell 12:291-300(2000).
RN [2]
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 [3]
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 [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 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 [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12662305; DOI=10.1046/j.1365-313x.2003.01700.x;
RA Buerkle L., Cedzich A., Doepke C., Stransky H., Okumoto S., Gillissen B.,
RA Kuehn C., Frommer W.B.;
RT "Transport of cytokinins mediated by purine transporters of the PUP family
RT expressed in phloem, hydathodes, and pollen of Arabidopsis.";
RL Plant J. 34:13-26(2003).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=23551747; DOI=10.1111/tpj.12195;
RA Szydlowski N., Buerkle L., Pourcel L., Moulin M., Stolz J.,
RA Fitzpatrick T.B.;
RT "Recycling of pyridoxine (vitamin B6) by PUP1 in Arabidopsis.";
RL Plant J. 75:40-52(2013).
CC -!- FUNCTION: Proton-coupled purine transporter mediating adenine and
CC trans-zeatin uptake (PubMed:12662305). High affinity transporter for
CC pyridoxine involved in the uptake of vitamin B6 (PubMed:23551747). Also
CC able to transport caffeine and adenosine (PubMed:12662305). May be
CC involved in the uptake of cytokinin, caffeine and nicotine from the
CC xylem sap into shoot tissues (PubMed:12662305).
CC {ECO:0000269|PubMed:12662305, ECO:0000269|PubMed:23551747}.
CC -!- ACTIVITY REGULATION: Inhibited by diethylstilbestrol, N,N'-
CC dicyclohexylcarbodiimide, carbonyl cyanide m-chlorphenyl-hydrazone and
CC 2,4-dinitrophenol. Competitive inhibition of adenine transport by
CC isopentenyladenine, cytosine, cytidine, hypoxanthine, kinetin, zeatin,
CC nicotine and caffeine, but not by zeatin riboside or kinetin riboside.
CC {ECO:0000269|PubMed:10662864, ECO:0000269|PubMed:12662305}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for adenine {ECO:0000269|PubMed:10662864,
CC ECO:0000269|PubMed:12662305};
CC KM=40 uM for trans-zeatin {ECO:0000269|PubMed:10662864,
CC ECO:0000269|PubMed:12662305};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23551747};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves, stems and flowers,
CC lower in siliques and not detected in roots (PubMed:10662864,
CC PubMed:12662305). Expressed in the epithem of hydathodes and the stigma
CC surface of siliques (PubMed:12662305, PubMed:23551747).
CC {ECO:0000269|PubMed:10662864, ECO:0000269|PubMed:12662305,
CC ECO:0000269|PubMed:23551747}.
CC -!- SIMILARITY: Belongs to the purine permeases (TC 2.A.7.14) family.
CC {ECO:0000305}.
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DR EMBL; AF078531; AAF64547.1; -; mRNA.
DR EMBL; AC021044; AAF98432.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30934.1; -; Genomic_DNA.
DR EMBL; BT005504; AAO63924.1; -; mRNA.
DR EMBL; AK117664; BAC42317.1; -; mRNA.
DR PIR; D86408; D86408.
DR RefSeq; NP_174144.1; NM_102588.3.
DR AlphaFoldDB; Q9FZ96; -.
DR SMR; Q9FZ96; -.
DR BioGRID; 24952; 9.
DR IntAct; Q9FZ96; 9.
DR STRING; 3702.AT1G28230.1; -.
DR TCDB; 2.A.7.14.1; the drug/metabolite transporter (dmt) superfamily.
DR PaxDb; Q9FZ96; -.
DR PRIDE; Q9FZ96; -.
DR ProteomicsDB; 226367; -.
DR EnsemblPlants; AT1G28230.1; AT1G28230.1; AT1G28230.
DR GeneID; 839717; -.
DR Gramene; AT1G28230.1; AT1G28230.1; AT1G28230.
DR KEGG; ath:AT1G28230; -.
DR Araport; AT1G28230; -.
DR TAIR; locus:2032148; AT1G28230.
DR eggNOG; ENOG502QTN9; Eukaryota.
DR HOGENOM; CLU_043459_1_1_1; -.
DR InParanoid; Q9FZ96; -.
DR OMA; FLMETPL; -.
DR OrthoDB; 1112849at2759; -.
DR PhylomeDB; Q9FZ96; -.
DR BioCyc; MetaCyc:MON-14768; -.
DR SABIO-RK; Q9FZ96; -.
DR PRO; PR:Q9FZ96; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ96; baseline and differential.
DR Genevisible; Q9FZ96; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:TAIR.
DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0010184; P:cytokinin transport; IDA:TAIR.
DR GO; GO:0006863; P:purine nucleobase transport; IDA:TAIR.
DR InterPro; IPR030182; PUP_plant.
DR PANTHER; PTHR31376; PTHR31376; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..356
FT /note="Purine permease 1"
FT /id="PRO_0000317388"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 35..158
FT /note="EamA"
FT CONFLICT 63
FT /note="S -> G (in Ref. 1; AAF64547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 39280 MW; FA2701E954CF797B CRC64;
MKNGLIIINC IILTIGTCGG PLLTRLYFTN GGKRIWFMSF LSTAGFPIIL IPLLVSFLSR
RRSNRNPNNA ENKRKTKLFL METPLFIASI VIGLLTGLDN YLYSYGLAYL PVSTSSLIIG
TQLAFNALFA FLLVKQKFTP FSINAVVLLT VGIGILALHS DGDKPAKESK KEYVVGFLMT
VVAALLYAFI LPLVELTYKK ARQEITFPLV LEIQMVMCLA ATFFCVIGMF IVGDFKVIAR
EAREFKIGGS VFYYALIVIT GIIWQGFFLG AIGIVFCASS LASGVLISVL LPVTEVFAVV
CFREKFQAEK GVSLLLSLWG FVSYFYGEFK SGKKVVDKPQ PPETELPILP VSDYVA
