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LAX4_MEDTR
ID   LAX4_MEDTR              Reviewed;         482 AA.
AC   Q8L884;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Auxin transporter-like protein 4;
DE   AltName: Full=AUX1-like protein 4;
DE   AltName: Full=MtLAX4;
GN   Name=LAX4;
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE FAMILY, AND TISSUE SPECIFICITY.
RX   PubMed=15375694; DOI=10.1007/s00438-004-1057-x;
RA   Schnabel E.L., Frugoli J.;
RT   "The PIN and LAX families of auxin transport genes in Medicago
RT   truncatula.";
RL   Mol. Genet. Genomics 272:420-432(2004).
RN   [2]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11277424; DOI=10.1094/mpmi.2001.14.3.267;
RA   de Billy F., Grosjean C., May S., Bennett M.J., Cullimore J.V.;
RT   "Expression studies on AUX1-like genes in Medicago truncatula suggest that
RT   auxin is required at two steps in early nodule development.";
RL   Mol. Plant Microbe Interact. 14:267-277(2001).
CC   -!- FUNCTION: Carrier protein involved in proton-driven auxin influx.
CC       Mediates the formation of auxin gradient from developing leaves (site
CC       of auxin biosynthesis) to tips by contributing to the loading of auxin
CC       in vascular tissues and facilitating acropetal (base to tip) auxin
CC       transport within inner tissues of the root apex, and basipetal (tip to
CC       base) auxin transport within outer tissues of the root apex (By
CC       similarity). May be involved in lateral roots and nodules formation.
CC       {ECO:0000250, ECO:0000269|PubMed:11277424}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Shoots and roots of nodulating plants, at low
CC       levels. {ECO:0000269|PubMed:11277424, ECO:0000269|PubMed:15375694}.
CC   -!- DEVELOPMENTAL STAGE: In primary roots, mostly localized in tips and to
CC       a lower extent in vasculature of older regions. In root tips, mostly
CC       expressed in the central tissues of the elongating zone (developing
CC       vasculature), in the starch-filled cells of the root cap and in some
CC       cortical cells. During lateral root development, striking expression in
CC       the proximal region of the primordium, close to the primary root
CC       central cylinder, and then in elongating cells of the developing
CC       vasculature and in developing root cap. During nodule formation,
CC       expressed in young elongated primordium, mostly in cells close to the
CC       root vasculature. In later stages, confined in small cells rich in
CC       amyloplasts with small nuclei. Near the periphery of developing nodules
CC       strong expression at the base that tapers off toward the apex. Not
CC       expressed in mature nodules. {ECO:0000269|PubMed:11277424}.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC       Amino acid/auxin permease (AAAP) (TC 2.A.18.1) subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Because of the similarity in sequence, the probe used to
CC       describe the developmental stages did not discriminate among the
CC       various MtLAX mRNAs. {ECO:0000305}.
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DR   EMBL; AY115844; AAM55305.1; -; Genomic_DNA.
DR   RefSeq; XP_013455165.1; XM_013599711.1.
DR   AlphaFoldDB; Q8L884; -.
DR   EnsemblPlants; KEH28865; KEH28865; MTR_4g415390.
DR   GeneID; 25494399; -.
DR   Gramene; KEH28865; KEH28865; MTR_4g415390.
DR   OrthoDB; 509343at2759; -.
DR   ExpressionAtlas; Q8L884; differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   Pfam; PF01490; Aa_trans; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid transport; Auxin signaling pathway; Cell membrane; Glycoprotein;
KW   Membrane; Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..482
FT                   /note="Auxin transporter-like protein 4"
FT                   /id="PRO_0000093848"
FT   TOPO_DOM        1..59
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..79
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..172
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..196
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..232
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..266
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..314
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        336..356
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        378
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        400..422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        444..482
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   482 AA;  54412 MW;  367C5E516D9D5C94 CRC64;
     MLSQNQAEEA IVTNMNETEQ EGGSSLEEIA EDQSMFNFKS FLWHGGSVWD AWFSCASNQV
     AQVLLTLPYS FSQLGMVSGI VFQIFYGLIG SWTAYLISVL YVEYRARKEK ENVNFKNHVI
     QWFEVLDGLL GRYWKALGLA FNCTFLLFGS VIQLIACASN IYYINDKLDK RTWTYIFGAC
     CATTVFIPSF HNYRIWSFLG LGMTTYTAWY MAIAAIVNGQ IENVVHSGPT KLVLYFTGAT
     NILYTFGGHA VTVEIMHAMW KPQKFKYIYF LATLYVFTLT IPSAVAVYWA FGDELLNHSN
     AFSLLPKNGF RDAAVILMLI HQFITFGFAC TPLYFVWEKV IGMHDTKSIC LRALVRLPVV
     IPIWFLAIIF PFFGPINSAV GALLVTFTVY IIPALAHMLT YRTASARKNA VEKPPSFLPS
     WTAVYVLNAF IVVWVLVVGF GFGGWASMTN FIRQIDTFGL FAKCYQCKPP TPPQAPSPHA
     RH
 
 
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