LPE1_MAIZE
ID LPE1_MAIZE Reviewed; 527 AA.
AC Q41760;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Nucleobase-ascorbate transporter LPE1;
DE AltName: Full=Leaf permease protein 1;
GN Name=LPE1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC TISSUE=Leaf;
RX PubMed=8721750; DOI=10.2307/3870325;
RA Schultes N.P., Brutnell T.P., Allen A., Dellaporta S.L., Nelson T.,
RA Chen J.;
RT "Leaf permease1 gene of maize is required for chloroplast development.";
RL Plant Cell 8:463-475(1996).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11283348; DOI=10.2307/3871352;
RA Argyrou E., Sophianopoulou V., Schultes N.P., Diallinas G.;
RT "Functional characterization of a maize purine transporter by expression in
RT Aspergillus nidulans.";
RL Plant Cell 13:953-964(2001).
CC -!- FUNCTION: High affinity uric acid-xanthine transporter in A.nidulans.
CC Binds, but cannot transport ascorbic acid.
CC {ECO:0000269|PubMed:11283348}.
CC -!- ACTIVITY REGULATION: Inhibited by excess of xanthin, uric acid and
CC ascorbic acid, and by 100 um N,N-dicyclohexylcarbodiimide and 30 um
CC carbonyl cyanide m-chlorophenyl-hydrazone.
CC {ECO:0000269|PubMed:11283348}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for xanthine {ECO:0000269|PubMed:11283348};
CC Note=Measured in the absence of ascorbic acid.;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots.
CC {ECO:0000269|PubMed:8721750}.
CC -!- DISRUPTION PHENOTYPE: Disrupted chloroplast ultrastructure.
CC {ECO:0000269|PubMed:8721750}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. {ECO:0000305}.
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DR EMBL; U43034; AAB17501.2; -; mRNA.
DR PIR; T02719; T02719.
DR RefSeq; NP_001105384.1; NM_001111914.1.
DR AlphaFoldDB; Q41760; -.
DR SMR; Q41760; -.
DR STRING; 4577.GRMZM5G858417_P01; -.
DR TCDB; 2.A.40.6.3; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR PaxDb; Q41760; -.
DR GeneID; 542332; -.
DR KEGG; zma:542332; -.
DR eggNOG; KOG1292; Eukaryota.
DR OrthoDB; 387031at2759; -.
DR BioCyc; MetaCyc:MON-14782; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q41760; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0071702; P:organic substance transport; IEA:UniProt.
DR InterPro; IPR006043; NCS2.
DR Pfam; PF00860; Xan_ur_permease; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..527
FT /note="Nucleobase-ascorbate transporter LPE1"
FT /id="PRO_0000270170"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 527 AA; 58122 MW; 5A6208081DDDFA7A CRC64;
MPPVKAEDLV VHAVKEQFAG LDYCITSPPP WITTVLVGFQ HYLVMLGTTV LIATIIVPLM
GGGHAEKAIV IQTILFLSGI NTLLQVHFGT RLPAVMSGSY TYIYPAVAII LSPRYALLID
PLERFVFTMR SLQGALIIAG VFQAVVGFFG IWRVFIRFLS PLAAVPFVTL TGLGLFFFAF
PGVTKCIEVG LPALVLLVIF AEYASHLFAK GSFVFSRCAV LVTVVIIWIY AEILTAAGAY
NERGPVTQFS CRADRSGIIQ GSPWVRFPYP FQWGYPIFCF QDCFAMLAAS FASLIESTGT
LIAVSRYSGA TFCPPSVFSR GIGWEGISII LDGMCGTLTG TAASVENAGL LAVTRVGSRR
VIKISALFMI FFSLFAKFGA VLASIPLPIF AALYCVLFAY SAGAGFSLLQ YCNLNSLRTK
FILSISLFLG LSIPQYFRVY EMFFGFGPVH THSVAFNVMV NVIFSSPATV AAILAYLLDC
THLYWEASVK KDRGWFWWEK FKSYKYDGRS EEFYRLPYGL SRYFPSL