PUP18_ARATH
ID PUP18_ARATH Reviewed; 390 AA.
AC Q9C508;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable purine permease 18;
DE Short=AtPUP18;
GN Name=PUP18; OrderedLocusNames=At1g57990; ORFNames=F13D13.3, T15M6.24;
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17869214; DOI=10.1016/j.bbrc.2007.08.177;
RA Hem S., Rofidal V., Sommerer N., Rossignol M.;
RT "Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify
RT phosphorylation sites in secondary active transporters.";
RL Biochem. Biophys. Res. Commun. 363:375-380(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the purine permeases (TC 2.A.7.14) family.
CC {ECO:0000305}.
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DR EMBL; AC079604; AAG50699.1; -; Genomic_DNA.
DR EMBL; AC079991; AAG50663.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33482.1; -; Genomic_DNA.
DR EMBL; BT000962; AAN41362.1; -; mRNA.
DR PIR; D96613; D96613.
DR RefSeq; NP_176100.1; NM_104584.3.
DR AlphaFoldDB; Q9C508; -.
DR BioGRID; 27391; 18.
DR IntAct; Q9C508; 18.
DR STRING; 3702.AT1G57990.1; -.
DR TCDB; 2.A.7.14.2; the drug/metabolite transporter (dmt) superfamily.
DR iPTMnet; Q9C508; -.
DR PaxDb; Q9C508; -.
DR PRIDE; Q9C508; -.
DR ProteomicsDB; 226269; -.
DR EnsemblPlants; AT1G57990.1; AT1G57990.1; AT1G57990.
DR GeneID; 842166; -.
DR Gramene; AT1G57990.1; AT1G57990.1; AT1G57990.
DR KEGG; ath:AT1G57990; -.
DR Araport; AT1G57990; -.
DR TAIR; locus:2010060; AT1G57990.
DR eggNOG; ENOG502QRUH; Eukaryota.
DR HOGENOM; CLU_043459_2_1_1; -.
DR InParanoid; Q9C508; -.
DR OMA; TRWIILS; -.
DR OrthoDB; 741120at2759; -.
DR PhylomeDB; Q9C508; -.
DR PRO; PR:Q9C508; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C508; baseline and differential.
DR Genevisible; Q9C508; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; TAS:TAIR.
DR GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006863; P:purine nucleobase transport; TAS:TAIR.
DR InterPro; IPR030182; PUP_plant.
DR PANTHER; PTHR31376; PTHR31376; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..390
FT /note="Probable purine permease 18"
FT /id="PRO_0000317405"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:17586839,
FT ECO:0007744|PubMed:17869214, ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 390 AA; 44182 MW; D122A30E05E7D808 CRC64;
MEMTEASKQT TAEGSANPEP DQILSPRRSL ELKQKKWWIS VSLCIFLVLL GDSLVMLLLN
FFYVQDNRED SDQDLQYRGT WLQALVQNAA FPLLIPLFFI FPSPKQNQET TNTRFLSFRL
ILLYISLGVL VAAHSKLFAL GKLYANFGVF TLISATQLIF TAIFAAIINR FKFTRWIILS
IIGSILIYVF GSPEFGGEPD ENEEFYSIQA WLTFAASVAF ALSLCLFQLC FEKVLVKTKR
YGNKKVFRMV IEMQICVSFV ATVVCLVGLF ASGENKELQG DSHRFKKGET YYVLSLIGLA
LSWQVWAVGL MGLVLYVSGV FGDVVHMCTS PLVALFVVLA FDFMDDEFSW PRIGTLIATV
VALGSYFYTL HKRNKKKMVE LYQTENNIDV
