LAX2_MEDTR
ID LAX2_MEDTR Reviewed; 484 AA.
AC Q9FEL7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Auxin transporter-like protein 2;
DE AltName: Full=AUX1-like protein 2;
DE AltName: Full=MtLAX2;
GN Name=LAX2;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Jemalong; TISSUE=Root;
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).
RN [2]
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).
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. Higher
CC levels in roots, flowers and stems, lower in nodules, leaves, petioles
CC and shoot apices. {ECO:0000269|PubMed:11277424,
CC 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 -!- INDUCTION: Transient induction in roots by S.meliloti.
CC {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; AJ299398; CAC12996.1; -; mRNA.
DR EMBL; AY115843; AAM55304.1; -; Genomic_DNA.
DR RefSeq; XP_003623228.1; XM_003623180.2.
DR AlphaFoldDB; Q9FEL7; -.
DR SMR; Q9FEL7; -.
DR STRING; 3880.AES79446; -.
DR EnsemblPlants; AES79446; AES79446; MTR_7g067450.
DR GeneID; 11407085; -.
DR Gramene; AES79446; AES79446; MTR_7g067450.
DR eggNOG; KOG1303; Eukaryota.
DR HOGENOM; CLU_027994_2_0_1; -.
DR OMA; GNCSKEE; -.
DR OrthoDB; 509343at2759; -.
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..484
FT /note="Auxin transporter-like protein 2"
FT /id="PRO_0000093846"
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..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 484 AA; 54719 MW; AA6A62655755EA9A CRC64;
MLPQKQGEEA IVSSFNETDQ QEGVVGREEE VEDHSFSVKN FLWHGGSVWD AWFSCASNQV
AQVLLTLPYS FSQLGMLSGI LLQVFYGILG SWTAYLISVL YVEYRSRKEK ENVNFKNHVI
QWFEVLDGLL GPYWKALGLA FNCTFLLFGS VIQLIACASN IYYINDNLDK RTWTYIFGAC
CATTVFIPSF HNYRIWSFLG LGMTTYTAWY LTIASIVHGQ AENVTHTGPK KLVLYFTGAT
NILYTFGGHA VTVEIMHAMW KPQKFKYIYL MATLYVFTLT IPSATAVYWA FGDELLNHSN
AFSLLPKNGW RDGAVILMLI HQFITFGFAC TPLYFVWEKV IGMHDTRSIC LRALARLPVV
IPIWFLAIIF PFFGPINSAV GALLVSFTVY IIPSAAHMLT YRKASARKNA AEKPPFFMPS
WTAMYIFNAF IVIWVLVVGF GFGGWASMTN FIRQIDTFGL FAKCYQCKPP PVMAAAPPPH
ALHH
