ID   5NG4_PINTA              Reviewed;         410 AA.
AC   Q6J163;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Auxin-induced protein 5NG4;
OS   Pinus taeda (Loblolly pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3352;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAT37621.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC   TISSUE=Shoot {ECO:0000312|EMBL:AAT37621.1};
RX   PubMed=14722770; DOI=10.1007/s00425-003-1175-4;
RA   Busov V.B., Johannes E., Whetten R.W., Sederoff R.R., Spiker S.L.,
RA   Lanz-Garcia C., Goldfarb B.;
RT   "An auxin-inducible gene from loblolly pine (Pinus taeda L.) is
RT   differentially expressed in mature and juvenile-phase shoots and encodes a
RT   putative transmembrane protein.";
RL   Planta 218:916-927(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Note=Detected in the periphery of cells and
CC       punctate structures throughout cytoplasm.
CC       {ECO:0000269|PubMed:14722770}.
CC   -!- INDUCTION: By auxin in hypocotyls, root and stems but not in cotyledons
CC       and needles. To a greater degree in juvenile than mature shoots.
CC       {ECO:0000269|PubMed:14722770}.
CC   -!- SIMILARITY: Belongs to the drug/metabolite transporter (DMT)
CC       superfamily. Plant drug/metabolite exporter (P-DME) (TC 2.A.7.4)
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY608411; AAT37621.1; -; mRNA.
DR   AlphaFoldDB; Q6J163; -.
DR   GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IDA:UniProtKB.
DR   InterPro; IPR000620; EamA_dom.
DR   InterPro; IPR030184; WAT1-related.
DR   PANTHER; PTHR31218; PTHR31218; 1.
DR   Pfam; PF00892; EamA; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..410
FT                   /note="Auxin-induced protein 5NG4"
FT                   /id="PRO_0000235823"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..47
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..74
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..109
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..141
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..196
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..264
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        286..292
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        314..317
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        339..410
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          209..338
FT                   /note="EamA"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   410 AA;  44975 MW;  DD40B4039ADDA8C3 CRC64;
     MASNIMQRCN VFMSERVKLH AAMLALQFGY AGFHIVSRAA LNMGVSKVVF PVYRNILALM
     LIGPCAYFLE KKERPALTLS FLIQFFLLAL CGITGQSRIL SLRIVLHIPT FASAIQNSVP
     AITFIMAAAL RLEKVHISRR DGLAKIIGTV ACVSGATIIT LYKGPPITHI WRPNLEVTAS
     YFKAFQGNDL SAKSENWTLG CIYLLGNCLA WSGWIVLQAP VLKRYPARLS VTSFTCFFGV
     IQFLIIAAFF ETDLEHWKIH SGGELFTILY AGFVASGIAF SVQIWCIDRG GPVFVAVYQP
     VQTIAVAIMA SIILGEQFYL GGIFGAILII IGLYLVLWGK SEEKRLGLLQ AKSSMVPENQ
     PDNMDQSATL IINSSNGIKP NTSSSLTQPL LLDTSYKTVN IPSPSDEPQP